1000 Sentences With "enzyme" | Random Sentence Generator

The concept is similar: a deaminating enzyme is attached to a CRISPR enzyme, but this time Cas-13, an enzyme that acts on RNA.

DHT forms when an enzyme converts testosterone into it; finasteride blocks the enzyme, lowering DHT levels.

As an enzyme cranks away and builds up product, the product feeds back and shuts down the enzyme.

Luciferin is the substrate in a chemical reaction catalyzed by the enzyme luciferase — it is not itself an enzyme.

However, delivering the active enzyme to addicts by injection and keeping this enzyme functioning in living animals is challenging.

The first part is called a deaminase enzyme (deamination means it removes an amino acid) and this is the enzyme that actually converts the C to a T. The deaminase enzyme is attached to a modified Cas-9; the same enzyme from CRISPR that is good at finding and sitting at specific positions within the genome.

But then the product falls back to a low level—because the enzyme has been shut down—and the enzyme starts cranking away again.

So instead of giving the enzyme to the animals, we decided to engineer skin stem cells that carried the gene for the BChE enzyme.

The new tool relies on an enzyme known as Cpf1, rather than Cas9, the enzyme typically paired with the CRISPR system to cut up DNA.

According to Genentech, the pharmaceutical company that makes Xofluza, this new drug works by blocking an enzyme within the influenza virus, called the endonuclease enzyme.

It is a molecule that transfers energy within cells, not an enzyme; ATP synthase, which makes ATP and which Dr. Boyer studied, is an enzyme.

The system consists of a DNA-cutting enzyme called Cas9 and a stretch of RNA that guides the cutting enzyme to the correct spot in the genome.

During the teams' attempt to understand the how the enzyme evolved, they made alterations that inadvertently led to the enzyme eating plastic 20 percent faster than before.

Pro-opiomelanocortin converting enzyme (, prohormone converting enzyme, pro- opiomelanocortin-converting enzyme, proopiomelanocortin proteinase, PCE) is an enzyme. This enzyme catalyses the following chemical reaction : Cleavage at paired basic residues in certain prohormones, either between them, or on the carboxyl side This membrane-bound enzyme is isolated from cattle pituitary secretory vesicle.

Induction or inhibition of these enzymes can cause drug interactions. Enzyme levels can also be regulated by changing the rate of enzyme degradation. The opposite of enzyme induction is enzyme repression.

Limulus clotting factor B () is an enzyme. This enzyme catalyses the following chemical reaction : Selective cleavage of -Arg98-Ile- bond in limulus proclotting enzyme to form active clotting enzyme From the hemocyte granules of the horseshoe crabs Limulus and Tachypleus. This enzyme is downstream of Limulus clotting factor C, but upstream of Limulus clotting enzyme.

In enzymology, a cysteine desulfurase () is an enzyme that catalyzes the chemical reaction :L-cysteine + [enzyme]-cysteine \rightleftharpoons L-alanine + [enzyme]-S-sulfanylcysteine Thus, the two substrates of this enzyme are L-cysteine and [enzyme]-cysteine], whereas its two products are L-alanine and [enzyme]-S-sulfanylcysteine. This enzyme belongs to the family of transferases, specifically the sulfurtransferases, which transfer sulfur- containing groups. The systematic name of this enzyme class is L-cysteine:[enzyme cysteine] sulfurtransferase. Other names in common use include IscS, NIFS, NifS, SufS, and cysteine desulfurylase.

Kinetic scheme for reversible enzyme inhibitors. Enzyme inhibitors are molecules that reduce or abolish enzyme activity, while enzyme activators are molecules that increase the catalytic rate of enzymes. These interactions can be either reversible (i.e., removal of the inhibitor restores enzyme activity) or irreversible (i.e.

An enzyme inducer is a type of drug that increases the metabolic activity of an enzyme either by binding to the enzyme and activating it, or by increasing the expression of the gene coding for the enzyme. It is the opposite of an enzyme repressor.

Linoleate 8R-lipoxygenase (, linoleic acid 8R-dioxygenase, 5,8-LDS (bifunctional enzyme), 7,8-LDS (bifunctional enzyme), 5,8-linoleate diol synthase (bifunctional enzyme), 7,8-linoleate diol synthase (bifunctional enzyme), PpoA) is an enzyme with systematic name linoleate:oxygen (8R)-oxidoreductase. This enzyme catalyses the following chemical reaction : linoleate + O2 \rightleftharpoons (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate Linoleate 8R-lipoxygenase contains heme.

In enzymology, an UDP-N-acetylglucosamine—lysosomal-enzyme N-acetylglucosaminephosphotransferase () is an enzyme that catalyzes the chemical reaction :UDP-N-acetyl-D-glucosamine + lysosomal-enzyme D-mannose \rightleftharpoons UMP + lysosomal-enzyme N-acetyl-D-glucosaminyl-phospho-D- mannose Thus, the two substrates of this enzyme are UDP-N-acetyl-D-glucosamine and lysosomal-enzyme D-mannose, whereas its two products are UMP and lysosomal-enzyme N-acetyl-D-glucosaminyl-phospho-D-mannose. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups transferases for other substituted phosphate groups. The systematic name of this enzyme class is UDP-N-acetyl-D- glucosamine:lysosomal-enzyme N-acetylglucosaminephosphotransferase. Other names in common use include UDP-N-acetylglucosamine:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase, UDP-GlcNAc:glycoprotein N-acetylglucosamine-1-phosphotransferase, uridine diphosphoacetylglucosamine- lysosomal enzyme precursor acetylglucosamine-1-phosphotransferase, uridine diphosphoacetylglucosamine-glycoprotein acetylglucosamine-1-phosphotransferase, lysosomal enzyme precursor acetylglucosamine-1-phosphotransferase, UDP-acetylglucosamine:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase, UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase, UDP-N-acetylglucosamine:glycoprotein N-acetylglucosamine-1-phosphotransferase, and UDP-N- acetylglucosamine:glycoprotein N-acetylglucosaminyl-1-phosphotransferase.

Limulus clotting enzyme (, clotting enzyme) is an enzyme. This enzyme catalyses the following chemical reaction : Selective cleavage of -Arg18\- and -Arg47\- bonds in coagulogen to form coagulin and fragments This enzyme is present in the hemocyte granules of horseshoe crabs Limulus and Tachypleus. In the immunity-related clotting pathways of these organisms, it is the final enzyme responsible for the activation of coagulin.

Envelysin (, sea-urchin-hatching proteinase, hatching enzyme, chorionase, chorion-digesting proteinase, chymostrypsin, sea urchin embryo hatching enzyme) is an enzyme. This enzyme catalyses the following chemical reaction : Hydrolysis of proteins of the fertilization envelope and dimethylcasein This enzyme is a glycoprotein from various members of the class Echinoidea.

Yeast ribonuclease () is an enzyme. This enzyme catalyses the following chemical reaction : Exonucleolytic cleavage to nucleoside 3'-phosphates This enzyme is similar RNase U4.

Stratum corneum chymotryptic enzyme (, kallikrein 7, SCCE, KLK7, PRSS6, hK7) is an enzyme. This enzyme catalyses the following chemical reaction : Cleavage of proteins with aromatic side chains in the P1 position This enzyme has wide substrate specificity.

Enzyme reaction rates can be decreased by various types of enzyme inhibitors.

N-formylmethionyl-peptidase (, (fMet)-releasing enzyme, formylmethionine aminopeptidase) is an enzyme. This enzyme catalyses the following chemical reaction : Release of an N-terminal, formyl-methionyl residue from a polypeptide This enzyme is highly specific for N-formylmethionyl peptides.

A core enzyme consists of the subunits of an enzyme that are needed for catalytic activity, as in the core enzyme RNA polymerase.Genetics: Analysis & Principles, 3rd Edition. pp. 811. Brooker, Robert J. An example of a core enzyme is a RNA polymerase enzyme without the sigma factor (σ). This enzyme consists of only two alpha (2α), one beta (β), one beta prime (β') and one omega (ω).

Beckman DU640 UV/Vis spectrophotometer Enzyme assays are laboratory methods for measuring enzymatic activity. They are vital for the study of enzyme kinetics and enzyme inhibition.

This enzyme is also called biphenyl dioxygenase. This enzyme participates in biphenyl degradation.

This enzyme is also called alkene epoxygenase. This enzyme participates in tetrachloroethene degradation.

This enzyme is also called HAPMO. This enzyme participates in bisphenol a degradation.

This enzyme is also called monoterpenoid dehydrogenase. This enzyme participates in monoterpenoid biosynthesis.

Endothelin-converting enzyme 1 (, endothelin-converting enzyme, ECE-1) is an enzyme. This enzyme catalyses the following chemical reaction : Hydrolysis of the -Trp21-Val- bond in big endothelin to form endothelin 1 This metalloendopeptidase belongs to the peptidase family M13.

Tentoxilysin (, tetanus neurotoxin) is an enzyme. This enzyme catalyses the following chemical reaction : Hydrolysis of -Gln76-Phe- bond in synaptobrevin This cinc enzyme produced by Clostridium tetani.

After anesthetic, the enzyme or a complex of the enzyme and the channel traffic to PIP2 domains where the enzyme makes phosphatidic acid that opens the channel.

Asclepain () is an enzyme. This enzyme catalyses the following chemical reaction : Similar to that of papain This enzyme is isolated from the latex of milkweed, Asclepias syriaca.

This enzyme is also called trehalase. This enzyme participates in starch and sucrose metabolism.

This enzyme is also called lysine N6-hydroxylase. This enzyme participates in lysine degradation.

This enzyme is also called gibberellin 2beta-hydroxylase. This enzyme participates in diterpenoid biosynthesis.

This enzyme participates in aminosugars metabolism. This enzyme has at least one effector, Dithiothreitol.

In enzymology, a malate dehydrogenase (oxaloacetate-decarboxylating) () is an enzyme that catalyzes the chemical reaction :(S)-malate + NAD+ \rightleftharpoons pyruvate + CO2 \+ NADH Thus, the two substrates of this enzyme are (S)-malate and NAD+, whereas its 3 products are pyruvate, CO2, and NADH. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (S)-malate:NAD+ oxidoreductase (oxaloacetate-decarboxylating). Other names in common use include malic enzyme, pyruvic-malic carboxylase, NAD+-specific malic enzyme, NAD+-malic enzyme, and NAD+-linked malic enzyme.

Acetoin dehydrogenase (, acetoin dehydrogenase complex, acetoin dehydrogenase enzyme system, AoDH ES) is an enzyme with systematic name acetyl-CoA:acetoin O-acetyltransferase. This enzyme catalyses the following chemical reaction : acetoin + CoA + NAD+ \rightleftharpoons acetaldehyde + acetyl-CoA + NADH + H+ This enzyme requires thiamine diphosphate.

Choriolysin L (, teleost hatching enzyme (component), low choriolytic enzyme (LCE)) is an enzyme. This enzyme catalyses the following chemical reaction : Hydrolysis of the inner layer of fish egg envelope. Also hydrolysis of casein and small molecule substrates such as succinyl-Leu-Leu-Val- Tyr-7-(4-methyl)coumarylamide This enzyme is present in teleost fish Oryzias latipes.

Choriolysin H (, teleost hatching enzyme (component), high choriolytic enzyme (HCE)) is an enzyme. This enzyme catalyses the following chemical reaction : Hydrolysis of the inner layer of fish egg envelope. Also hydrolysis of casein and small molecule substrates such as succinyl-Leu-Leu-Val- Tyr-7-(4-methyl)coumarylamide This enzyme is present in teleost fish Oryzias latipes.

Cathepsin T () is an enzyme. This enzyme catalyses the following chemical reaction : Interconversion of the three forms of tyrosine aminotransferase, EC 2.6.1.5 This enzyme degrades azocasein and denatured hemoglobin.

Ribonuclease alpha (, 2'-O-methyl RNase) is an enzyme. This enzyme catalyses the following chemical reaction : Endonucleolytic cleavage to 5'-phosphomonoester This enzyme is specific for O-methylated RNA.

An enzyme repressor is a substance that negatively regulates the amount of an enzyme by decreasing the rate of its biosynthesis. It is the opposite of an enzyme inducer.

Dipyridamole also inhibits the enzyme adenosine deaminase, the enzyme that catalyzes the breakdown of adenosine.

This enzyme participates in retinol metabolism. This enzyme has at least one effector, Bile salt.

This enzyme is also called creatinine hydrolase. This enzyme participates in arginine and proline metabolism.

This enzyme is also called protopine 6-hydroxylase. This enzyme participates in alkaloid biosynthesis i.

This enzyme is also called zeta-carotene desaturase. This enzyme participates in carotenoid biosynthesis - general.

This enzyme is also called dihydrosanguinarine 10-hydroxylase. This enzyme participates in alkaloid biosynthesis i.

This enzyme is also called dihydrochelirubine 12-hydroxylase. This enzyme participates in alkaloid biosynthesis i.

This enzyme is also called linoleate (8R)-dioxygenase. This enzyme participates in linoleic acid metabolism.

Clostridial aminopeptidase (, Clostridium histolyticum aminopeptidase) is an enzyme. This enzyme catalyses the following chemical reaction : Release of any N-terminal amino acid, including proline and hydroxyproline, but no cleavage of Xaa-Pro- This enzyme is secreted enzyme from Clostridium histolyticum. It requiring Mn2+ or Co2+.

Sortase B (, SrtB) is an enzyme. This enzyme catalyses the following chemical reaction : The enzyme catalyses a cell wall sorting reaction in which a surface protein with a sorting signal containing a NXTN motif is cleaved. This enzyme belongs to the peptidase family C60.

Calpain-1 (, mu-calpain, calcium-activated neutral protease I) is an enzyme. This enzyme catalyses the following chemical reaction : Broad endopeptidase specificity This enzyme belongs to the peptidase family C2.

ADAM10 endopeptidase (, Kuzbanian protein, myelin-associated disintegrin metalloproteinase) is an enzyme. This enzyme catalyses the following chemical reaction : Endopeptidase of broad specificity This enzyme belongs to the peptidase family M12.

HIV-2 retropepsin () is an enzyme. This enzyme catalyses the following chemical reaction : Endopeptidase for which the P1 residue is preferably hydrophobic This enzyme belongs to the peptidase family A2.

The enzyme quercitrinase can be found in Aspergillus flavus. This enzyme hydrolyzes the glycoside quercitrin to release quercetin and L-rhamnose. It is an enzyme in the rutin catabolic pathway.

Ribonuclease V (, endoribonuclease V) is an enzyme. This enzyme catalyses the following chemical reaction : Hydrolysis of poly(A), forming oligoribonucleotides and ultimately 3'-AMP This enzyme also hydrolyses poly(U).

The analyte-enzyme-fragment-conjugate is still able to reassemble with the other enzyme fragment to form an active enzyme. However it is unable to do this if the analyte is bound to an antibody. To determine the quantity of analyte in a sample, an aliquot of sample must be added to a solution containing enzyme-fragment-analyte-conjugate, the other enzyme fragment, antibody directed against the analyte and substrate for the enzyme reaction. Competition for the antibody occurs between the analyte in the sample and the enzyme-fragment-analyte-conjugate.

This enzyme is also called progesterone 11alpha-hydroxylase. This enzyme participates in c21-steroid hormone metabolism.

This enzyme is also called toluene 2,3-dioxygenase. This enzyme participates in toluene and xylene degradation.

This enzyme is also called leukotriene-E4 omega- hydroxylase. This enzyme participates in arachidonic acid metabolism.

This enzyme is also called estradiol 6beta-hydroxylase. This enzyme participates in androgen and estrogen metabolism.

This enzyme is also called linoleate dioxygenase, manganese lipoxygenase. This enzyme participates in linoleic acid metabolism.

This enzyme is also called (4-hydroxybenzoyl)methanol oxygenase. This enzyme participates in bisphenol a degradation.

A depsidase is a type of enzyme that cuts depside bonds. One such enzyme is tannase.

A cloned enzyme donor immunoassay (CEDIA) is a competitive homogenous enzyme immunoassay. This assay makes use of two component fragments of an enzyme which are each individually inactive. Under the right conditions in solution these fragments can spontaneously reassemble to form the active enzyme. For use in biochemical assays one of the enzyme fragments is attached to an analyte of interest.

High concentrations of analyte in the sample lead to a relatively small amount of the enzyme- fragment-analyte-conjugate being prevented from forming active enzyme and therefore high enzyme activity. Conversely, low concentrations of analyte in the sample lead to a relatively large amount of the enzyme-fragment-analyte- conjugate being prevented from forming active enzymes and therefore low enzyme activity.

In enzymology, an acetoin racemase () is an enzyme that catalyzes the chemical reaction :(S)-acetoin \rightleftharpoons (R)-acetoin This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on hydroxy acids and derivatives. The systematic name of this enzyme class is acetoin racemase. This enzyme is also called acetylmethylcarbinol racemase. This enzyme participates in butanoate metabolism.

In enzymology, a cycloeucalenol cycloisomerase () is an enzyme that catalyzes the chemical reaction :cycloeucalenol \rightleftharpoons obtusifoliol Hence, this enzyme has one substrate, cycloeucalenol, and one product, obtusifoliol. This enzyme belongs to the family of isomerases, specifically the class of intramolecular lyases. The systematic name of this enzyme class is cycloeucalenol lyase (cyclopropane-decyclizing). This enzyme is also called cycloeucalenol---obtusifoliol isomerase.

In enzymology, a maleylpyruvate isomerase () is an enzyme that catalyzes the chemical reaction :3-maleylpyruvate \rightleftharpoons 3-fumarylpyruvate Hence, this enzyme has one substrate, 3-maleylpyruvate, and one product, 3-fumarylpyruvate. This enzyme belongs to the family of isomerases, specifically cis-trans isomerases. The systematic name of this enzyme class is 3-maleylpyruvate cis-trans-isomerase. This enzyme participates in tyrosine metabolism.

In enzymology, a neoxanthin synthase () is an enzyme that catalyzes the chemical reaction: :violaxanthin \rightleftharpoons neoxanthin Hence, this enzyme has one substrate, violaxanthin, and one product, neoxanthin. This enzyme belongs to the family of isomerases, specifically a class of other intramolecular oxidoreductases. The systematic name of this enzyme class is violaxanthin---neoxanthin isomerase (epoxide-opening). This enzyme is also called NSY.

Morquio syndrome is a rare birth defect caused by a deficiency in this essential enzyme. Treatment options include enzyme replacement therapy with a synthetic version of the enzyme called elosulfase alfa.

Spermosin () is an enzyme. This enzyme catalyses the following chemical reaction : Hydrolyses arginyl bonds, preferably with Pro in the P2 position This enzyme is isolated from the ascidian (Prochordate) Halocynthia roretzi.

Gingipain K (, Lys-gingipain, PrtP proteinase) is an enzyme. This enzyme catalyses the following chemical reaction : Endopeptidase with strict specificity for lysyl bonds Activity of this enzyme is stimulated by glycine.

In enzymology, a dihydrolipoyllysine-residue (2-methylpropanoyl)transferase () is an enzyme that catalyzes the chemical reaction :2-methylpropanoyl-CoA + enzyme N6-(dihydrolipoyl)lysine \rightleftharpoons CoA + enzyme N6-(S-[2-methylpropanoyl]dihydrolipoyl)lysine Thus, the two substrates of this enzyme are 2-methylpropanoyl-CoA and enzyme N6-(dihydrolipoyl)lysine, whereas its two products are CoA and enzyme N6-(S-[2-methylpropanoyl]dihydrolipoyl)lysine. This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is 2-methylpropanoyl-CoA:enzyme-N6-(dihydrolipoyl)lysine S-(2-methylpropanoyl)transferase. Other names in common use include dihydrolipoyl transacylase, enzyme-dihydrolipoyllysine:2-methylpropanoyl-CoA, S-(2-methylpropanoyl)transferase, 2-methylpropanoyl- CoA:enzyme-6-N-(dihydrolipoyl)lysine, and S-(2-methylpropanoyl)transferase.

In enzymology, a dihydrolipoyllysine-residue succinyltransferase () is an enzyme that catalyzes the chemical reaction :succinyl-CoA + enzyme N6-(dihydrolipoyl)lysine \rightleftharpoons CoA + enzyme N6-(S-succinyldihydrolipoyl)lysine Thus, the two substrates of this enzyme are succinyl-CoA and enzyme N6-(dihydrolipoyl)lysine, whereas its two products are CoA and enzyme N6-(S-succinyldihydrolipoyl)lysine. This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is succinyl-CoA:enzyme-N6-(dihydrolipoyl)lysine S-succinyltransferase. Other names in common use include dihydrolipoamide S-succinyltransferase, dihydrolipoamide succinyltransferase, dihydrolipoic transsuccinylase, dihydrolipolyl transsuccinylase, dihydrolipoyl transsuccinylase, lipoate succinyltransferase (Escherichia coli), lipoic transsuccinylase, lipoyl transsuccinylase, succinyl-CoA:dihydrolipoamide S-succinyltransferase, succinyl-CoA:dihydrolipoate S-succinyltransferase, and enzyme- dihydrolipoyllysine:succinyl-CoA S-succinyltransferase.

Calpain-2 (, calcium-activated neutral protease II, m-calpain, milli-calpain) is an enzyme. This enzyme catalyses the following chemical reaction : Broad endopeptidase specificity This enzyme belongs to the peptidase family C2.

Avermitilol synthase () is an enzyme with systematic name avermitilol hydrolase (cyclizing, avermitilol-forming). This enzyme catalyses the following chemical reaction : (2E,6E)-farnesyl diphosphate + H2O \rightleftharpoons avermitilol + diphosphate This enzyme requires Mg2+.

Propionate kinase (, PduW, TdcD, propionate/acetate kinase) is an enzyme with systematic name ATP:propanoate phosphotransferase. This enzyme catalyses the following chemical reaction : ATP + propanoate \rightleftharpoons ADP + propanoyl phosphate This enzyme requires Mg2+.

Maltokinase () is an enzyme with systematic name ATP:alpha-maltose 1-phosphotransferase. This enzyme catalyses the following chemical reaction : ATP + maltose \rightleftharpoons ADP + alpha-maltose 1-phosphate This enzyme requires Mg2+ for activity.

Carboxypeptidase T (, CPT) is an enzyme. This enzyme catalyses the following chemical reaction: : Releases a C-terminal residue, which may be hydrophobic or positively charged. This enzyme is isolated from Thermoactinomyces vulgaris.

This enzyme is also called 2-aminosulfobenzene 2,3-dioxygenase. This enzyme participates in benzoate degradation via hydroxylation.

The systematic name of this enzyme class is arsenite:azurin oxidoreductase. This enzyme is also called arsenite oxidase.

The enzyme contains five fingerprint regions containing Gln-Trp motifs, which are also present in the highly analogous bacterial enzyme squalene-hopene cyclase. Residues of these fingerprint regions contain stacked sidechains which are thought to contribute to enzyme stability during the highly exergonic cyclization reactions catalyzed by the enzyme.

M7GpppN-mRNA hydrolase (, DCP2, NUDT16, D10 protein, D9 protein, D10 decapping enzyme, decapping enzyme) is an enzyme with systematic name m7GpppN-mRNA m7GDP phosphohydrolase. This enzyme catalyses the following chemical reaction : m7G5'ppp5'-mRNA + H2O \rightleftharpoons m7GDP + 5'-phospho-mRNA Decapping of mRNA is essential in eukaryotic mRNA turnover.

Isoamylase (, debranching enzyme, glycogen alpha-1,6-glucanohydrolase) is an enzyme with systematic name glycogen 6-alpha-D-glucanohydrolase. This enzyme catalyses the following chemical reaction : Hydrolysis of (1->6)-alpha-D- glucosidic branch linkages in glycogen, amylopectin and their beta-limit dextrins This enzyme also readily hydrolyses amylopectin.

In biochemistry, a cross-linked enzyme aggregate is an immobilized enzyme prepared via cross-linking of the physical enzyme aggregates with a difunctional cross-linker. They can be used as stereoselective industrial biocatalysts.

Dihydroorotate dehydrogenase (fumarate) (, dihydroorotate oxidase, pyr4 (gene)) is an enzyme with systematic name (S)-dihydroorotate:fumarate oxidoreductase. This enzyme catalyses the following chemical reaction : (S)-dihydroorotate + fumarate \rightleftharpoons orotate + succinate This enzyme contains FMN.

Before that, it was considered an "orphan" enzyme. An orphan enzyme is an enzyme activity that has been experimentally characterized but for which there is no known amino-acid or nucleotide sequence data.

Tryptophanyl aminopeptidase (, tryptophan aminopeptidase, L-tryptophan aminopeptidase) is an enzyme. This enzyme catalyses the following chemical reaction : Preferential release of N-terminal tryptophan This enzyme from Trichosporon cutaneum also acts on L-tryptophanamide.

Glutathione hydrolase (, glutathionase, GGT, gamma-glutamyltranspeptidase) is an enzyme. This enzyme catalyses the following chemical reaction : glutathione + H2O \rightleftharpoons L-cysteinylglycine + L-glutamate This protein also acts as enzyme EC 2.3.2.2 (gamma-glutamyltransferase).

In enzymology, a trimetaphosphatase () is an enzyme that catalyzes the chemical reaction :trimetaphosphate + H2O \rightleftharpoons triphosphate Thus, the two substrates of this enzyme are trimetaphosphate and H2O, whereas its product is triphosphate. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides in phosphorus-containing anhydrides. The systematic name of this enzyme class is trimetaphosphate hydrolase. This enzyme is also called inorganic trimetaphosphatase.

In enzymology, a dihydrocoumarin hydrolase () is an enzyme that catalyzes the chemical reaction :dihydrocoumarin + H2O \rightleftharpoons melilotate Thus, the two substrates of this enzyme are dihydrocoumarin and H2O, whereas its product is melilotate. This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is dihydrocoumarin lactonohydrolase. This enzyme participates in fluorene degradation.

In enzymology, an aconitate Delta-isomerase () is an enzyme that catalyzes the chemical reaction :trans-aconitate \rightleftharpoons cis-aconitate Hence, this enzyme has one substrate, trans-aconitate, and one product, cis- aconitate. This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases transposing C=C bonds. The systematic name of this enzyme class is aconitate Delta2-Delta3-isomerase. This enzyme is also called aconitate isomerase.

In enzymology, an allantoin racemase () is an enzyme that catalyzes the chemical reaction :(S)(+)-allantoin \rightleftharpoons (R)(-)-allantoin Hence, this enzyme has one substrate, (S)(+)-allantoin, and one product, (R)(-)-allantoin. This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on other compounds. The systematic name of this enzyme class is allantoin racemase. This enzyme participates in purine metabolism.

In enzymology, a chalcone isomerase () is an enzyme that catalyzes the chemical reaction :a chalcone \rightleftharpoons a flavanone Hence, this enzyme has one substrate, a chalcone, and one product, a flavanone. This enzyme belongs to the family of isomerases, specifically the class of intramolecular lyases. The systematic name of this enzyme class is flavanone lyase (decyclizing). This enzyme is also called chalcone-flavanone isomerase.

In enzymology, a proline racemase () is an enzyme that catalyzes the chemical reaction :L-proline \rightleftharpoons D-proline Hence, this enzyme has two substrates, L- and D-proline, and two products, D- and L- proline. This enzyme belongs to the family of proline racemases acting on free amino acids. The systematic name of this enzyme class is proline racemase. This enzyme participates in arginine and proline metabolism.

In enzymology, a copalyl diphosphate synthase () is an enzyme that catalyzes the chemical reaction :geranylgeranyl diphosphate \rightleftharpoons (+)-copalyl diphosphate Hence, this enzyme has one substrate, geranylgeranyl diphosphate, and one product, (+)-copalyl diphosphate. This enzyme belongs to the family of isomerases, specifically the class of intramolecular lyases. The systematic name of this enzyme class is (+)-copalyl-diphosphate lyase (decyclizing). This enzyme participates in diterpenoid biosynthesis.

In enzymology, a lysine racemase () is an enzyme that catalyzes the chemical reaction :L-lysine ⇌ D-lysine Hence, this enzyme has one substrate, L-lysine, and one product, D-lysine. This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on amino acids and derivatives. The systematic name of this enzyme class is lysine racemase. This enzyme participates in lysine degradation.

In enzymology, a lysolecithin acylmutase () is an enzyme that catalyzes the chemical reaction :2-lysolecithin \rightleftharpoons 3-lysolecithin Hence, this enzyme has one substrate, 2-lysolecithin, and one product, 3-lysolecithin. This enzyme belongs to the family of isomerases, specifically those intramolecular transferases transferring acyl groups. The systematic name of this enzyme class is lysolecithin 2,3-acylmutase. This enzyme is also called lysolecithin migratase.

In enzymology, a methylitaconate Delta-isomerase () is an enzyme that catalyzes the chemical reaction :methylitaconate \rightleftharpoons 2,3-dimethylmaleate Hence, this enzyme has one substrate, methylitaconate, and one product, 2,3-dimethylmaleate. This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases transposing C=C bonds. The systematic name of this enzyme class is methylitaconate Delta2-Delta3-isomerase. This enzyme is also called methylitaconate isomerase.

In enzymology, a styrene-oxide isomerase () is an enzyme that catalyzes the chemical reaction :styrene oxide \rightleftharpoons phenylacetaldehyde Hence, this enzyme has one substrate, styrene oxide, and one product, phenylacetaldehyde. This enzyme belongs to the family of isomerases, specifically a class of other intramolecular oxidoreductases. The systematic name of this enzyme class is styrene-oxide isomerase (epoxide-cleaving). This enzyme is also called SOI.

In enzymology, an ethanolamine ammonia-lyase () is an enzyme that catalyzes the chemical reaction :ethanolamine \rightleftharpoons acetaldehyde + NH3 Hence, this enzyme has one substrate, ethanolamine, and two products, acetaldehyde and NH3. This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic name of this enzyme class is ethanolamine ammonia-lyase (acetaldehyde-forming). This enzyme is also called ethanolamine deaminase.

Neurolysin (, neurotensin endopeptidase, endopeptidase 24.16, endo- oligopeptidase B (proline-endopeptidase)) is an enzyme. This enzyme catalyses the following chemical reaction : Preferential cleavage in neurotensin: Pro10-Tyr This enzyme belongs to the peptidase family M3.

Cyclohexane-1,2-dione hydrolase () is an enzyme with systematic name cyclohexane-1,2-dione acylhydrolase (decyclizing). This enzyme catalyses the following chemical reaction : cyclohexane-1,2-dione + H2O \rightleftharpoons 6-oxohexanoate This enzyme is highly specific.

IntEnz (Integrated relational Enzyme database) contains data on enzymes organized by enzyme EC number and is the official version of the Enzyme Nomenclature system developed by the International Union of Biochemistry and Molecular Biology.

D-lactate dehydratase (, glyoxylase III) is an enzyme with systematic name (R)-lactate hydro-lyase. This enzyme catalyses the following chemical reaction : (R)-lactate \rightleftharpoons methylglyoxal + H2O The enzyme converts methylglyoxal to D-lactate.

Terpinolene synthase (, ag9, PmeTPS2, LaLIMS_RR) is an enzyme with systematic name geranyl-diphosphate diphosphate-lyase (cyclizing, terpinolene-forming). This enzyme catalyses the following chemical reaction : geranyl diphosphate \rightleftharpoons terpinolene + diphosphate This enzyme requires Mg2+.

TRNA pseudouridine31 synthase (, Pus6p) is an enzyme with systematic name tRNA-uridine31 uracil mutase. This enzyme catalyses the following chemical reaction : tRNA uridine31 \rightleftharpoons tRNA pseudouridine31 The enzyme specifically acts on uridine31 in tRNA.

Sulfoacetaldehyde reductase (, ISFD) is an enzyme with systematic name isethionate:NADP+ oxidoreductase. This enzyme catalyses the following chemical reaction : isethionate + NADP+ \rightleftharpoons 2-sulfoacetaldehyde + NADPH + H+ This enzyme catalyses the reaction in the reverse direction.

Isopullulanase () is an enzyme with systematic name pullulan 4-glucanohydrolase (isopanose-forming). This enzyme catalyses the following chemical reaction : Hydrolysis of pullulan to isopanose (6-alpha- maltosylglucose) The enzyme has no activity on starch.

Xaa-His dipeptidase (, aminoacylhistidine dipeptidase, carnosinase, homocarnosinase, dipeptidase M) is an enzyme. This enzyme catalyses the following chemical reaction : Hydrolysis of Xaa-His dipeptides This mammalian cytosolic enzyme also acts on anserine and homocarnosine.

Carboxypeptidase Taq () is an enzyme. This enzyme catalyses the following chemical reaction : Release of a C-terminal amino acid with broad specificity, except for -Pro This 56-kDa enzyme is isolated from Thermus aquaticus.

Carboxypeptidase M (, CPM) is an enzyme. This enzyme catalyses the following chemical reaction : Cleavage of C-terminal arginine or lysine residues from polypeptides This is a membrane-bound enzyme optimally active at neutral pH.

Assemblin () is an enzyme with systematic name. This enzyme catalyses the following chemical reaction : Cleaves -Ala-Ser- and -Ala-Ala- bonds in the scaffold protein This enzyme is coded by the herpes-virus virion.

Cucumisin (, euphorbain, solanain, hurain, tabernamontanain) is an enzyme. This enzyme catalyses the following chemical reaction : Hydrolysis of proteins with broad specificity This enzyme is isolated from the sarcocarp of the musk melon (Cucumis melo).

Vibriolysin (, Aeromonas proteolytica neutral proteinase, aeromonolysin) is an enzyme. This enzyme catalyses the following chemical reaction : Preferential cleavage of bonds with bulky hydrophobic groups in P2 and P1'. Phe at P1' is the most favoured residue, which distinguished this enzyme from thermolysin This thermostable enzyme is isolated from Vibrio proteolyticus.

Immobilization using affinity relies on the specificity of an enzyme to couple an affinity ligand to an enzyme to form a covalently bound enzyme-ligand complex. The complex is introduced into a support matrix for which the ligand has high binding affinity, and the enzyme is immobilized through ligand- support interactions.

Sulfur carrier protein ThiS adenylyltransferase (, thiF (gene)) is an enzyme with systematic name ATP:(ThiS) adenylyltransferase. This enzyme catalyses the following chemical reaction : ATP + [ThiS] \rightleftharpoons diphosphate + adenylyl-[ThiS] This enzyme binds Zn2+. The enzyme catalyses the adenylation of ThiS, a sulfur carrier protein involved in the biosynthesis of thiamine.

Acylaminoacyl-peptidase (, acylamino-acid-releasing enzyme, N-acylpeptide hydrolase, N-formylmethionine (fMet) aminopeptidase, alpha-N-acylpeptide hydrolase) is an enzyme. This enzyme catalyses the following chemical reaction : Cleavage of an N-acetyl or N-formyl amino acid from the N-terminus of a polypeptide This enzyme is active at neutral pH.

Molybdopterin adenylyltransferase (, MogA, Cnx1) is an enzyme with systematic name ATP:molybdopterin adenylyltransferase. This enzyme catalyses the following chemical reaction : ATP + molybdopterin \rightleftharpoons diphosphate + adenylyl-molybdopterin This enzyme catalyses the activation of molybdopterin for molybdenum insertion.

Futalosine hydrolase (, futalosine nucleosidase, MqnB) is an enzyme with systematic name futalosine ribohydrolase. This enzyme catalyses the following chemical reaction : futalosine + H2O \rightleftharpoons dehypoxanthine futalosine + hypoxanthine This enzyme catalyses the second step of menaquinone biosynthesis.

Enterobacter ribonuclease () is an enzyme. This enzyme catalyses the following chemical reaction : Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides with 2',3'-cyclic phosphate intermediates This enzyme has preference for cleavage at CpA.

Aspergillus deoxyribonuclease K1 (, Aspergillus DNase K1) is an enzyme. This enzyme catalyses the following chemical reaction : Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotide end-products This enzyme has preference for single-stranded DNA.

This enzyme participates in aminosugars metabolism. This enzyme has at least one effector, N-Acetyl-D-glucosamine 6-phosphate.

This enzyme is also called (R)-reticuline oxidase (C-C phenol-coupling). This enzyme participates in alkaloid biosynthesis i.

This enzyme is also called isoflavone 3'-monooxygenase. This enzyme participates in isoflavonoid biosynthesis. It employs one cofactor, heme.

This enzyme is also called AAoxygenase. This enzyme participates in ascorbate and aldarate metabolism. It employs one cofactor, iron.

This enzyme participates in aminosugars metabolism. This enzyme has at least one effector, N-Acetyl-D-glucosamine 1,6-bisphosphate.

In enzymology, a (+)-neomenthol dehydrogenase () is an enzyme that catalyzes the chemical reaction :(+)-neomenthol + NADP \rightleftharpoons (−)-menthone + NADPH + H Thus, the two substrates of this enzyme are (+)-neomenthol and NADP, whereas its 3 products are (−)-menthone, NADPH, and H. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD or NADP as acceptor. The systematic name of this enzyme class is (+)-neomenthol:NADP oxidoreductase. This enzyme is also called monoterpenoid dehydrogenase. This enzyme participates in monoterpenoid biosynthesis.

In enzymology, a citrate dehydratase () is an enzyme that catalyzes the chemical reaction :citrate \rightleftharpoons cis-aconitate + H2O Hence, this enzyme has one substrate, citrate, and two products, cis-aconitate and H2O. This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is citrate hydro-lyase (cis-aconitate-forming). This enzyme is also called citrate hydro-lyase.

In enzymology, a cyanamide hydratase () is an enzyme that catalyzes the chemical reaction :urea \rightleftharpoons cyanamide + H2O Hence, this enzyme has one substrate, urea, and two products, cyanamide and H2O. This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is urea hydro- lyase (cyanamide-forming). This enzyme is also called urea hydro-lyase.

In enzymology, a myrcene synthase () is an enzyme that catalyzes the chemical reaction :geranyl diphosphate \rightleftharpoons myrcene + diphosphate Hence, this enzyme has one substrate, geranyl diphosphate, and two products, myrcene and diphosphate. This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on phosphates. The systematic name of this enzyme class is geranyl-diphosphate diphosphate-lyase (myrcene-forming). This enzyme participates in monoterpenoid biosynthesis.

In enzymology, a guanosine-diphosphatase () is an enzyme that catalyzes the chemical reaction :GDP + H2O \rightleftharpoons GMP + phosphate Thus, the two substrates of this enzyme are GDP and H2O, whereas its two products are GMP and phosphate. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides in phosphorus-containing anhydrides. The systematic name of this enzyme class is GDP phosphohydrolase. This enzyme is also called GDPase.

In enzymology, a triphosphatase () is an enzyme that catalyzes the chemical reaction :triphosphate + H2O \rightleftharpoons diphosphate + phosphate Thus, the two substrates of this enzyme are triphosphate and H2O, whereas its two products are diphosphate and phosphate. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides in phosphorus- containing anhydrides. The systematic name of this enzyme class is triphosphate phosphohydrolase. This enzyme is also called inorganic triphosphatase.

In enzymology, a S-formylglutathione hydrolase () is an enzyme that catalyzes the chemical reaction :S-formylglutathione + H2O \rightleftharpoons glutathione + formate Thus, the two substrates of this enzyme are S-formylglutathione and H2O, whereas its two products are glutathione and formate. This enzyme belongs to the family of hydrolases, specifically those acting on thioester bonds. The systematic name of this enzyme class is S-formylglutathione hydrolase. This enzyme participates in methane metabolism.

In enzymology, a sinapine esterase () is an enzyme that catalyzes the chemical reaction :sinapoylcholine + H2O \rightleftharpoons sinapate + choline Thus, the two substrates of this enzyme are sinapoylcholine and H2O, whereas its two products are sinapate and choline. This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is sinapoylcholine sinapohydrolase. This enzyme is also called aromatic choline esterase.

In enzymology, an orsellinate-depside hydrolase () is an enzyme that catalyzes the chemical reaction :orsellinate depside + H2O \rightleftharpoons 2 orsellinate Thus, the two substrates of this enzyme are orsellinate depside and H2O, whereas its product is orsellinate. This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is orsellinate-depside hydrolase. This enzyme is also called lecanorate hydrolase.

In enzymology, a phosphoenolpyruvate phosphatase () is an enzyme that catalyzes the chemical reaction :phosphoenolpyruvate + H2O \rightleftharpoons pyruvate + phosphate Thus, the two substrates of this enzyme are phosphoenolpyruvate and H2O, whereas its two products are pyruvate and phosphate. This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name of this enzyme class is phosphoenolpyruvate phosphohydrolase. This enzyme is also called PEP phosphatase.

In enzymology, a 4-pyridoxolactonase () is an enzyme that catalyzes the chemical reaction :4-pyridoxolactone + H2O \rightleftharpoons 4-pyridoxate Thus, the two substrates of this enzyme are 4-pyridoxolactone and H2O, whereas its product is 4-pyridoxate. This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is 4-pyridoxolactone lactonohydrolase. This enzyme participates in vitamin B6 metabolism.

In enzymology, a phosphonoacetate hydrolase () is an enzyme that catalyzes the chemical reaction :phosphonoacetate + H2O \rightleftharpoons acetate + phosphate Thus, the two substrates of this enzyme are phosphonoacetate and H2O, whereas its two products are acetate and phosphate. This enzyme belongs to the family of hydrolases, specifically those acting on carbon-phosphorus bonds. The systematic name of this enzyme class is phosphonoacetate phosphonohydrolase. This enzyme participates in aminophosphonate metabolism.

In enzymology, a phosphonopyruvate hydrolase () is an enzyme that catalyzes the chemical reaction :3-phosphonopyruvate + H2O \rightleftharpoons pyruvate + phosphate Thus, the two substrates of this enzyme are 3-phosphonopyruvate and H2O, whereas its two products are pyruvate and phosphate. This enzyme belongs to the family of hydrolases, specifically those acting on carbon-phosphorus bonds. The systematic name of this enzyme class is '. This enzyme is also called PPH'.

In enzymology, a trithionate hydrolase () is an enzyme that catalyzes the chemical reaction :trithionate + H2O \rightleftharpoons thiosulfate + sulfate + 2 H+ Thus, the two substrates of this enzyme are trithionate and H2O, whereas its 3 products are thiosulfate, sulfate, and H+. This enzyme belongs to the family of hydrolases, specifically those acting on sulfur-sulfur bonds. The systematic name of this enzyme class is trithionate thiosulfohydrolase. This enzyme participates in sulfur metabolism.

In enzymology, an oxaloacetase () is an enzyme that catalyzes the chemical reaction: :oxaloacetate + H2O \rightleftharpoons oxalate + acetate Thus, the two substrates of this enzyme are oxaloacetate and H2O, whereas its two products are oxalate and acetate. This enzyme belongs to the family of hydrolases, specifically those acting on carbon-carbon bonds in ketonic substances. The systematic name of this enzyme class is oxaloacetate acetylhydrolase. This enzyme is also called oxalacetic hydrolase.

In enzymology, a phosphoamidase () is an enzyme that catalyzes the chemical reaction :N-phosphocreatine + H2O \rightleftharpoons creatine + phosphate Thus, the two substrates of this enzyme are N-phosphocreatine and H2O, whereas its two products are creatine and phosphate. This enzyme belongs to the family of hydrolases, specifically those acting on phosphorus-nitrogen bonds. The systematic name of this enzyme class is phosphamide hydrolase. This enzyme is also called creatine phosphatase.

In enzymology, a dihydroxyfumarate decarboxylase () is an enzyme that catalyzes the chemical reaction :dihydroxyfumarate \rightleftharpoons tartronate semialdehyde + CO2 Hence, this enzyme has one substrate, dihydroxyfumarate, and two products, tartronate semialdehyde and CO2. This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is dihydroxyfumarate carboxy-lyase (tartronate-semialdehyde-forming). This enzyme is also called dihydroxyfumarate carboxy-lyase.

In enzymology, a benzylsuccinate synthase () is an enzyme that catalyzes the chemical reaction :benzylsuccinate \rightleftharpoons toluene + fumarate Hence, this enzyme has one substrate, benzylsuccinate, and two products, toluene and fumarate. This enzyme belongs to the family of lyases, specifically in the "catch-all" class of carbon-carbon lyases. The systematic name of this enzyme class is benzylsuccinate fumarate-lyase (toluene-forming). This enzyme is also called benzylsuccinate fumarate-lyase.

In enzymology, a hydroxypyruvate decarboxylase () is an enzyme that catalyzes the chemical reaction :hydroxypyruvate \rightleftharpoons glycolaldehyde + CO2 Hence, this enzyme has one substrate, hydroxypyruvate, and two products, glycolaldehyde and CO2. This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is hydroxypyruvate carboxy-lyase (glycolaldehyde-forming). This enzyme is also called hydroxypyruvate carboxy- lyase.

In enzymology, a stipitatonate decarboxylase () is an enzyme that catalyzes the chemical reaction :stipitatonate \rightleftharpoons stipitatate + CO2 Hence, this enzyme has one substrate, stipitatonate, and two products, stipitatate and CO2. This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is stipitatonate carboxy-lyase (decyclizing, stipitatate- forming). This enzyme is also called stipitatonate carboxy-lyase (decyclizing).

In enzymology, a phenylpyruvate decarboxylase () is an enzyme that catalyzes the chemical reaction :phenylpyruvate \rightleftharpoons phenylacetaldehyde + CO2 Hence, this enzyme has one substrate, phenylpyruvate, and two products, phenylacetaldehyde and CO2. This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is phenylpyruvate carboxy-lyase (phenylacetaldehyde-forming). This enzyme is also called phenylpyruvate carboxy-lyase.

In enzymology, a carnitine decarboxylase () is an enzyme that catalyzes the chemical reaction :carnitine \rightleftharpoons 2-methylcholine + CO2 Hence, this enzyme has one substrate, carnitine, and two products, 2-methylcholine and CO2. This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is carnitine carboxy-lyase (2-methylcholine-forming). This enzyme is also called carnitine carboxy-lyase.

In enzymology, an alanine racemase () is an enzyme that catalyzes the chemical reaction :L-alanine \rightleftharpoons D-alanine Hence, this enzyme has one substrate, L-alanine, and one product, D-alanine. This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on amino acids and derivatives. The systematic name of this enzyme class is alanine racemase. This enzyme is also called L-alanine racemase.

In enzymology, a 2-methyleneglutarate mutase () is an enzyme that catalyzes the chemical reaction :2-methyleneglutarate \rightleftharpoons 2-methylene-3-methylsuccinate Hence, this enzyme has one substrate, 2-methyleneglutarate, and one product, 2-methylene-3-methylsuccinate. This enzyme belongs to the family of isomerases, specifically those intramolecular transferases transferring other groups. The systematic name of this enzyme class is 2-methyleneglutarate carboxy-methylenemethylmutase. This enzyme is also called alpha-methyleneglutarate mutase.

In enzymology, a diaminopimelate epimerase () is an enzyme that catalyzes the chemical reaction :LL-2,6-diaminoheptanedioate \rightleftharpoons meso- diaminoheptanedioate Hence, this enzyme has one substrate, LL-2,6-diaminoheptanedioate, and one product, meso-diaminoheptanedioate. This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on amino acids and derivatives. The systematic name of this enzyme class is LL-2,6-diaminoheptanedioate 2-epimerase. This enzyme participates in lysine biosynthesis.

In enzymology, a L-arabinose isomerase () is an enzyme that catalyzes the chemical reaction :L-arabinose \rightleftharpoons L-ribulose Hence, this enzyme has one substrate, L-arabinose, and one product, L-ribulose. This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases interconverting aldoses and ketoses. The systematic name of this enzyme class is L-arabinose aldose-ketose-isomerase. This enzyme participates in pentose and glucuronate interconversions.

251x251px Depending on the microorganism PRAI's structure can vary between a mono-functional enzyme (monomeric and labile) or a stable bi-functional dimeric enzyme. Within Saccharomyces cerevisiae, Bacillus subtilis, Pseudomonas putida, and Acinetobacter calcoaceticus the enzyme is monmeric. In contrast, in hyperthermophile Thermotoga maritima, Escherichia coli (Fig. 5), Salmonella typhimurium, and Aerobacter aerogenes, and Serratia marcescens, it is a bi-functional enzyme with indoleglycerol phosphate synthase as the paired enzyme.

In enzymology, a leucine 2,3-aminomutase () is an enzyme that catalyzes the chemical reaction :(2S)-alpha-leucine \rightleftharpoons (3R)-beta-leucine Hence, this enzyme is responsible for the conversion of -leucine to β-leucine. This enzyme belongs to the family of isomerases, specifically those intramolecular transferases transferring amino groups. The systematic name of this enzyme class is (2S)-alpha-leucine 2,3-aminomutase. This enzyme participates in valine, leucine and isoleucine degradation.

In enzymology, a L-fucose isomerase () is an enzyme that catalyzes the chemical reaction :L-fucose \rightleftharpoons L-fuculose Hence, this enzyme has one substrate, L-fucose, and one product, L-fuculose. This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases interconverting aldoses and ketoses. The systematic name of this enzyme class is L-fucose aldose-ketose-isomerase. This enzyme participates in fructose and mannose metabolism.

In enzymology, a hydroxypyruvate isomerase () is an enzyme that catalyzes the chemical reaction :hydroxypyruvate \rightleftharpoons 2-hydroxy-3-oxopropanoate Hence, this enzyme has one substrate, hydroxypyruvate, and one product, 2-hydroxy-3-oxopropanoate. This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases interconverting aldoses and ketoses. The systematic name of this enzyme class is hydroxypyruvate aldose-ketose-isomerase. This enzyme participates in glyoxylate and dicarboxylate metabolism.

In enzymology, a nocardicin-A epimerase () is an enzyme that catalyzes the chemical reaction :isonocardicin A \rightleftharpoons nocardicin A Hence, this enzyme has one substrate, isonocardicin A, and one product, nocardicin A. This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on amino acids and derivatives. The systematic name of this enzyme class is nocardicin-A epimerase. This enzyme is also called isonocardicin A epimerase.

In enzymology, an ornithine racemase () is an enzyme that catalyzes the chemical reaction :L-ornithine \rightleftharpoons D-ornithine Hence, this enzyme has one substrate, L-ornithine, and one product, D-ornithine. This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on amino acids and derivatives. The systematic name of this enzyme class is ornithine racemase. This enzyme participates in d-arginine and d-ornithine metabolism.

In enzymology, an oxaloacetate tautomerase () is an enzyme that catalyzes the chemical reaction :keto-oxaloacetate \rightleftharpoons enol-oxaloacetate Hence, this enzyme has one substrate, keto-oxaloacetate, and one product, enol-oxaloacetate. This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases interconverting keto- and enol-groups. The systematic name of this enzyme class is oxaloacetate keto--- enol-isomerase. This enzyme is also called oxaloacetic keto-enol isomerase.

Metabolic flux refers to the rate of metabolite conversion in a metabolic network. For a reaction this rate is a function of both enzyme abundance and enzyme activity. Enzyme concentration is itself a function of transcriptional and translational regulation in addition to the stability of the protein. Enzyme activity is affected by the kinetic parameters of the enzyme, the substrate concentrations, the product concentrations, and the effector molecules concentration.

In enzymology, a tartrate epimerase () is an enzyme that catalyzes the chemical reaction :(R,R)-tartrate \rightleftharpoons meso-tartrate Hence, this enzyme has one substrate, (R,R)-tartrate, and one product, meso-tartrate. This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on hydroxy acids and derivatives. The systematic name of this enzyme class is tartrate epimerase. This enzyme is also called tartaric racemase.

In enzymology, a FMN adenylyltransferase () is an enzyme that catalyzes the chemical reaction :ATP + FMN \rightleftharpoons diphosphate + FAD Thus, the two substrates of this enzyme are ATP and FMN, whereas its two products are diphosphate and FAD. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is ATP:FMN adenylyltransferase. This enzyme participates in riboflavin metabolism.

There are a few ways to help pinpoint the presence of Krabbe disease. Newborn screening for Krabbe disease includes assaying dried blood cells for GALC enzyme activity and molecular analysis for evidence of GALC enzyme mutations. Infants displaying low enzyme activity and/or enzyme mutations should be referred for additional diagnostic testing and neurological examination. 0-5% GALC enzyme activity is observed in all symptomatic individuals with Krabbe disease.

FAD-dependent urate hydroxylase (, HpxO enzyme, FAD-dependent urate oxidase, urate hydroxylase) is an enzyme with systematic name urate,NADH:oxygen oxidoreductase (5-hydroxyisourate forming). A non-homologous isofunctional enzyme (NISE) to HpxO was found, and named HpyO. HpyO was determined to be a typical Michaelian enzyme. These FAD-dependent urate hydroxylases are flavoproteins.

Prosolanapyrone-III cycloisomerase (, Sol5, SPS, solanapyrone synthase (bifunctional enzyme: prosolanapyrone II oxidase/prosolanapyrone III cyclosiomerase)) is an enzyme with systematic name prosolanapyrone- III:(-)-solanapyrone A isomerase. This enzyme catalyses the following chemical reaction : prosolanapyrone III \rightleftharpoons (-)-solanapyrone A The enzyme is involved in the biosynthesis of the phytotoxin solanapyrone in some fungi.

Neutrophil collagenase (, matrix metalloproteinase 8, PMNL collagenase, MMP-8) is an enzyme. This enzyme catalyses the following chemical reaction : Cleavage of interstitial collagens in the triple helical domain. Unlike EC 3.4.24.7, interstitial collagenase, this enzyme cleaves type III collagen more slowly than type I This enzyme belongs to the peptidase family M10.

Leukotriene-C4 hydrolase (, gamma-glutamyl leukotrienase) is an enzyme. Gamma- glutamyltransferase 5 (GGT5) is a human gene which encodes an enzyme protein that belongs to this class of enzymes. This enzyme catalyses the following chemical reaction : leukotriene C4 + H2O \rightleftharpoons leukotriene D4 + L-glutamate The mouse enzyme is specific for leukotriene C4.

FMN reductase (NAD(P)H) (, FRG) is an enzyme with systematic name FMNH2:NAD(P)+ oxidoreductase. This enzyme catalyses the following chemical reaction : FMNH2 + NAD(P)+ \rightleftharpoons FMN + NAD(P)H + H+ This enzyme contains FMN.

FMN reductase (NADH) (, NADH-FMN reductase) is an enzyme with systematic name FMNH2:NAD+ oxidoreductase. This enzyme catalyses the following chemical reaction : FMNH2 \+ NAD+ \rightleftharpoons FMN + NADH + H+ The enzyme often forms a complex with monooxygenases.

Signal-recognition-particle GTPase () is an enzyme with systematic name GTP phosphohydrolase (protein-synthesis-assisting). This enzyme catalyses the following chemical reaction : GTP + H2O \rightleftharpoons GDP + phosphate Enzyme activity is associated with the signal-recognition particle.

Thermopsin () is an enzyme. This enzyme catalyses the following chemical reaction : Similar in specificity to pepsin A preferring bulky hydrophobic amino acids in P1 and P1' This enzyme is isolated from the thermophilic archeaon Sulfolobus acidocaldarius.

Elisabethatriene synthase (, elisabethatriene cyclase) is an enzyme with systematic name geranylgeranyl-diphosphate diphosphate-lyase (elisabethatriene-forming). This enzyme catalyses the following chemical reaction : geranylgeranyl diphosphate \rightleftharpoons elisabethatriene + diphosphate This enzyme requires Mg2+ or less efficiently Mn2+.

Terpentedienyl-diphosphate synthase (, terpentedienol diphosphate synthase, Cyc1, clerodadienyl diphosphate synthase) is an enzyme with systematic name terpentedienyl-diphosphate lyase (decyclizing). This enzyme catalyses the following chemical reaction : geranylgeranyl diphosphate \rightleftharpoons terpentedienyl diphosphate This enzyme requires Mg2+.

Isopentenyl phosphate kinase () is an enzyme with systematic name ATP:isopentenyl phosphate phosphotransferase. This enzyme catalyses the following chemical reaction : ATP + isopentenyl phosphate \rightleftharpoons ADP + isopentenyl diphosphate This enzyme takes part in the mevalonate pathway in Archaea.

Bacterial leucyl aminopeptidase (, Aeromonas proteolytica aminopeptidase) is an enzyme. This enzyme catalyses the following chemical reaction : Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids This is a zinc enzyme.

Aminopeptidase Y (, aminopeptidase Co, aminopeptidase (cobalt-activated), lysyl aminopeptidase) is an enzyme. This enzyme catalyses the following chemical reaction : Preferentially, release of N-terminal lysine This enzyme requires Co2+. It is inhibited by Zn2+ and Mn2+.

Tuberculosinol synthase (, Rv3378c) is an enzyme with systematic name tuberculosinyl diphosphate diphosphohydrolase (tuberculosinol forming). This enzyme catalyses the following chemical reaction : tuberculosinyl diphosphate + H2O \rightleftharpoons [tuberculosinol] + diphosphate This enzyme is present in Mycobacterium that cause tuberculosis.

Deoxyribonuclease X (, Escherichia coli endodeoxyribonuclease, Escherichia coli endodeoxyribonuclease X) is an enzyme. This enzyme catalyses the following chemical reaction : Endonucleolytic cleavage of supercoiled plasma DNA to linear DNA duplexes This enzyme has preference for supercoiled DNA.

This gene encodes pterin-4 alpha- carbinolamine dehydratase, an enzyme involved in phenylalanine hydroxylation. A deficiency of this enzyme leads to hyperphenylalaninemia. The enzyme regulates the homodimerization of the transcription factor hepatocyte nuclear factor 1 (HNF1).

Staphopain (, staphylopain) is an enzyme. This enzyme catalyses the following chemical reaction : Broad endopeptidase action on proteins including elastin, but rather limited hydrolysis of small-molecule substrates. This enzyme is present in several species of Staphylococcus.

A metalloprotease enzyme isolated from bacteria at Lake Rotorua, among other locations, is called microcystinase, is part of a 3 enzyme biodegradation pathway. This particular enzyme results in a product with 160-fold decrease in toxicity.

This enzyme is also called (S)-N-methylcoclaurine oxidase (C-O phenol-coupling). This enzyme participates in alkaloid biosynthesis i.

This enzyme is also called 3-hydroxyphenylacetate 6-monooxygenase. This enzyme participates in styrene degradation. It employs one cofactor, FAD.

The systematic name of this enzyme class is ferrocytochrome-c:Fe3+ oxidoreductase. This enzyme is also called iron-cytochrome c reductase.

This enzyme participates in alanine and aspartate metabolism. It employs one cofactor, FAD. The enzyme is encoded by DDO gene.

Endothelin converting enzyme 1, also known as ECE1, is an enzyme which in humans is encoded by the ECE1 gene.

Indole-3-carboxylate decarboxylase () is an enzyme with systematic name indole-3-carboxylate carboxy-lyase. This enzyme catalyses the following chemical reaction : indole-3-carboxylate \rightleftharpoons indole + CO2 This enzyme is activated by Zn2+, Mn2+ or Mg2+.

Ethylmalonyl-CoA decarboxylase () is an enzyme with systematic name (S)-ethylmalonyl-CoA carboxy-lyase (butanoyl-CoA-forming). This enzyme catalyses the following chemical reaction : (S)-ethylmalonyl-CoA \rightleftharpoons butanoyl-CoA + CO2 The vertebrate enzyme decarboxylates ethylmalonyl-CoA.

Angelicin synthase (, CYP71AJ4 (gene)) is an enzyme with systematic name (+)-columbianetin,NADPH:oxygen oxidoreductase. This enzyme catalyses the following chemical reaction: : (+)-columbianetin + NADPH + H+ \+ O2 \rightleftharpoons angelicin + NADP+ \+ acetone + 2 H2O Angelicin synthase is a P450 monooxygenase enzyme.

3-dehydroshikimate dehydratase () is an enzyme with systematic name 3-dehydroshikimate hydro-lyase. This enzyme catalyses the following chemical reaction : 3-dehydro-shikimate \rightleftharpoons protocatechuate + H2O This enzyme catalyses an early step in the biosynthesis of petrobactin.

Cubebol synthase (, Cop4) is an enzyme with systematic name (2E,6E)-farnesyl- diphosphate diphosphate-lyase (cyclizing, cubebol-forming). This enzyme catalyses the following chemical reaction : (2E,6E)-farnesyl diphosphate + H2O \rightleftharpoons cubebol + diphosphate This enzyme requires Mg2+.

Benzil reductase ((S)-benzoin forming) (, YueD) is an enzyme with systematic name (S)-benzoin:NADP+ oxidoreductase. This enzyme catalyses the following chemical reaction : (S)-benzoin + NADP+ \rightleftharpoons benzil + NADPH + H+ The enzyme also reduces 1-phenylpropane-1,2-dione.

Prolyl aminopeptidase (, proline aminopeptidase, Pro-X aminopeptidase, cytosol aminopeptidase V, proline iminopeptidase) is an enzyme. This enzyme catalyses the following chemical reaction : Release of N-terminal proline from a peptide This enzyme requires Mn2+ ion to function.

Xaa-Pro dipeptidase (, prolidase, imidodipeptidase, proline dipeptidase, peptidase D, gamma-peptidase) is an enzyme. This enzyme catalyses the following chemical reaction : Hydrolysis of Xaa!Pro dipeptides; also acts on aminoacyl-hydroxyproline analogs This enzyme is Mn2+-activated.

Geranylgeranyl diphosphate diphosphatase (, geranylgeranyl diphosphate phosphatase) is an enzyme with systematic name geranyl-diphosphate diphosphohydrolase. This enzyme catalyses the following chemical reaction : geranylgeranyl diphosphate + H2O \rightleftharpoons geranylgeraniol + diphosphate This enzyme is involved in the biosynthesis of plaunotol.

Sometimes such enzyme metal preferences vary among closely related species: For example, the reverse transcriptase enzyme of lentiviruses like HIV, SIV and FIV is typically dependent on Mg2+, whereas the analogous enzyme for other retroviruses prefers Mn2+.

Chymotrypsin C () is an enzyme. This enzyme catalyses the following chemical reaction : Preferential cleavage: Leu-, Tyr-, Phe-, Met-, Trp-, Gln-, Asn! This enzyme is formed from pig chymotrypsinogen C, and from cattle subunit II of procarboxypeptidase A.

Fruit bromelain (, juice bromelain, ananase, Bromelase (a trademark), bromelin, extranase, pinase, pineapple enzyme, traumanase, fruit bromelain FA2) is an enzyme. This enzyme catalyses the following chemical reaction : Hydrolysis of proteins with broad specificity for peptide bonds. Bz-Phe-Val- Arg-NHMec is a good synthetic substrate This enzyme is isolated from pineapple plant, Ananas comosus.

Prosolanapyrone-II oxidase (, Sol5, SPS, solanapyrone synthase (bifunctional enzyme: prosolanapyrone II oxidase/prosolanapyrone III cycloisomerase), prosolanapyrone II oxidase) is an enzyme with systematic name prosolanapyrone- II:oxygen 3'-oxidoreductase. This enzyme catalyses the following chemical reaction : prosolanapyrone II + O2 \rightleftharpoons prosolanapyrone III + H2O2 This enzyme participates in the biosynthesis of the phytotoxin solanapyrone by some fungi.

L-serine-phosphatidylethanolamine phosphatidyltransferase (, phosphatidylserine synthase 2, serine-exchange enzyme II, PTDSS2 (gene)) is an enzyme with systematic name L-1-phosphatidylethanolamine:L-serine phosphatidyltransferase. This enzyme catalyses the following chemical reaction : L-1-phosphatidylethanolamine + L-serine \rightleftharpoons L-1-phosphatidylserine + ethanolamine This enzyme catalyses replacement of a polar head group of phosphatidylethanolamine with L-serine.

Insulysin () (Also called insulinase, insulin-degrading enzyme, insulin protease, insulin proteinase, insulin-degrading neutral proteinase, insulin- specific protease, insulin-glucagon protease, metalloinsulinase, IDE) is an enzyme. This enzyme catalyses the degradation reaction of insulin, glucagon and other polypeptides. This cytosolic enzyme is present in mammals and in many arthropods such as the fly Drosophila melanogaster.

Arabinogalactan endo-beta-1,4-galactanase (, endo-1,4-beta-galactanase, galactanase, arabinogalactanase, ganB (gene)) is an enzyme with systematic name arabinogalactan 4-beta-D-galactanohydrolase. This enzyme catalyses the following chemical reaction : The enzyme specifically hydrolyses (1->4)-beta- D-galactosidic linkages in type I arabinogalactans. This enzyme is isolated from the bacterium Bacillus subtilis.

Production of siderophores also exhibited in some plant-infecting bacteria, such as Agrobacterium tumefaciens. The enzyme is controlled by gene cluster agb and the production of 2,3-diDHB dehydrogenase is controlled by the gene agbA. The enzyme AgbA is homologous to the EntA enzyme in E. coli, the same enzyme that produces 2,3-diDHB dehydrogenase.

Sortase A (, SrtA, SrtA protein, SrtA sortase) is an enzyme. This enzyme catalyses the following chemical reaction : The enzyme catalyses a cell wall sorting reaction, in which a surface protein with a sorting signal containing a LPXTG motif, is cleaved between the Thr and Gly residue. This enzyme belongs to the peptidase family C60.

In enzymology, an orotate reductase (NADH) () is an enzyme that catalyzes the chemical reaction :(S)-dihydroorotate + NAD+ \rightleftharpoons orotate + NADH + H+ Thus, the two substrates of this enzyme are (S)-dihydroorotate and NAD+, whereas its 3 products are orotate, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (S)-dihydroorotate:NAD+ oxidoreductase. This enzyme is also called orotate reductase (NADH). This enzyme participates in pyrimidine metabolism.

In enzymology, a 2-enoate reductase () is an enzyme that catalyzes the chemical reaction :butanoate + NAD+ \rightleftharpoons 2-butenoate + NADH + H+ Thus, the two substrates of this enzyme are butanoate and NAD+, whereas its 3 products are 2-butenoate, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is butanoate:NAD+ Delta2-oxidoreductase. This enzyme is also called enoate reductase. This enzyme participates in phenylalanine metabolism.

In enzymology, a glycolaldehyde dehydrogenase () is an enzyme that catalyzes the chemical reaction :glycolaldehyde + NAD+ \+ H2O \rightleftharpoons glycolate + NADH + 2 H+ The 3 substrates of this enzyme are glycolaldehyde, NAD+, and H2O, whereas its 3 products are glycolate, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is glycolaldehyde:NAD+ oxidoreductase. This enzyme is also called glycol aldehyde dehydrogenase. This enzyme participates in glyoxylate and dicarboxylate metabolism.

In enzymology, a glutarate-semialdehyde dehydrogenase () is an enzyme that catalyzes the chemical reaction :glutarate semialdehyde + NAD+ \+ H2O \rightleftharpoons glutarate + NADH + 2 H+ The 3 substrates of this enzyme are glutarate semialdehyde, NAD+, and H2O, whereas its 3 products are glutarate, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is glutarate- semialdehyde:NAD+ oxidoreductase. This enzyme is also called glutarate semialdehyde dehydrogenase. This enzyme participates in lysine degradation.

In enzymology, a galactitol 2-dehydrogenase () is an enzyme that catalyzes the chemical reaction :galactitol + NAD+ \rightleftharpoons D-tagatose + NADH + H+ Thus, the two substrates of this enzyme are galactitol and NAD+, whereas its 3 products are D-tagatose, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is galactitol:NAD+ 2-oxidoreductase. This enzyme is also called dulcitol dehydrogenase. This enzyme participates in galactose metabolism.

In enzymology, a carveol dehydrogenase () is an enzyme that catalyzes the chemical reaction :(-)-trans-carveol + NADP+ \rightleftharpoons (-)-carvone + NADPH + H+ Thus, the two substrates of this enzyme are (-)-trans-carveol and NADP+, whereas its 3 products are (-)-carvone, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH- OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (-)-trans-carveol:NADP+ oxidoreductase. This enzyme is also called (-)-trans-carveol dehydrogenase. This enzyme participates in monoterpenoid biosynthesis and limonene and pinene degradation.

In enzymology, a -iditol 2-dehydrogenase () is an enzyme that catalyzes the chemical reaction :-iditol + NAD+ \rightleftharpoons -sorbose + NADH + H+ Thus, the two substrates of this enzyme are -iditol and NAD+, whereas its 3 products are -sorbose, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is -iditol:NAD+ 2-oxidoreductase. This enzyme is also called -sorbitol dehydrogenase. This enzyme participates in pentose and glucuronate interconversions and fructose and mannose metabolism.

In enzymology, an isopropanol dehydrogenase (NADP+) () is an enzyme that catalyzes the chemical reaction :propan-2-ol + NADP+ \rightleftharpoons acetone + NADPH + H+ Thus, the two substrates of this enzyme are propan-2-ol and NADP+, whereas its 3 products are acetone, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH- OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is propan-2-ol:NADP+ oxidoreductase. This enzyme is also called isopropanol dehydrogenase (NADP+). This enzyme participates in propanoate metabolism.

In enzymology, a glycerol dehydrogenase (NADP+) () is an enzyme that catalyzes the chemical reaction :glycerol + NADP+ \rightleftharpoons D-glyceraldehyde + NADPH + H+ Thus, the two substrates of this enzyme are glycerol and NADP+, whereas its 3 products are D-glyceraldehyde, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH- OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is glycerol:NADP+ oxidoreductase. This enzyme is also called glycerol dehydrogenase (NADP+). This enzyme participates in glycerolipid metabolism.

In enzymology, a tartrate dehydrogenase () is an enzyme that catalyzes the chemical reaction :tartrate + NAD+ \rightleftharpoons oxaloglycolate + NADH + H+ Thus, the two substrates of this enzyme are tartrate and NAD+, whereas its 3 products are oxaloglycolate, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is tartrate:NAD+ oxidoreductase. This enzyme is also called mesotartrate dehydrogenase. This enzyme participates in glyoxylate and dicarboxylate metabolism.

In enzymology, a perillyl-alcohol dehydrogenase () is an enzyme that catalyzes the chemical reaction :perillyl alcohol + NAD+ \rightleftharpoons perillyl aldehyde + NADH + H+ Thus, the two substrates of this enzyme are perillyl alcohol and NAD+, whereas its 3 products are perillyl aldehyde, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is perillyl-alcohol:NAD+ oxidoreductase. This enzyme is also called perillyl alcohol dehydrogenase. This enzyme participates in limonene and pinene degradation.

In enzymology, a pterocarpin synthase () is an enzyme that catalyzes the chemical reaction :medicarpin + NADP+ \+ H2O \rightleftharpoons vestitone + NADPH + H+ The 3 substrates of this enzyme are medicarpin, NADP+, and H2O, whereas its 3 products are vestitone, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is medicarpin:NADP+ 2'-oxidoreductase. This enzyme is also called pterocarpan synthase. This enzyme participates in isoflavonoid biosynthesis.

In enzymology, a pyridoxal 4-dehydrogenase () is an enzyme that catalyzes the chemical reaction :pyridoxal + NAD+ \rightleftharpoons 4-pyridoxolactone + NADH + H+ Thus, the two substrates of this enzyme are pyridoxal and NAD+, whereas its 3 products are 4-pyridoxolactone, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH- OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is pyridoxal:NAD+ 4-oxidoreductase. This enzyme is also called pyridoxal dehydrogenase. This enzyme participates in vitamin B6 metabolism.

In enzymology, a 4-alpha-glucanotransferase () is an enzyme that catalyzes a chemical reaction that transfers a segment of a 1,4-alpha-D-glucan to a new position in an acceptor carbohydrate, which may be glucose or a 1,4-alpha-D- glucan. This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is 1,4-alpha-D-glucan:1,4-alpha-D-glucan 4-alpha-D-glycosyltransferase. Other names in common use include disproportionating enzyme, dextrin glycosyltransferase, D-enzyme, debranching enzyme maltodextrin glycosyltransferase, amylomaltase, and dextrin transglycosylase.

In enzymology, a phaseollidin hydratase () is an enzyme that catalyzes the chemical reaction :phaseollidin hydrate \rightleftharpoons phaseollidin + H2O Hence, this enzyme has one substrate, phaseollidin hydrate, and two products, phaseollidin and H2O. This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is phaseollidin-hydrate hydro-lyase (phaseollidin-forming). This enzyme is also called phaseollidin-hydrate hydro- lyase.

In enzymology, a prephenate dehydratase () is an enzyme that catalyzes the chemical reaction :prephenate \rightleftharpoons phenylpyruvate + H2O + CO2 Hence, this enzyme has one substrate, prephenate, but 3 products: phenylpyruvate, H2O, and CO2. This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is prephenate hydro-lyase (decarboxylating; phenylpyruvate-forming). This enzyme is also called prephenate hydro-lyase (decarboxylating).

In enzymology, a scytalone dehydratase () is an enzyme that catalyzes the chemical reaction :scytalone \rightleftharpoons 1,3,8-trihydroxynaphthalene + H2O Hence, this enzyme has one substrate, scytalone, and two products, 1,3,8-trihydroxynaphthalene and H2O. This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is scytalone 7,8-hydro-lyase (1,3,8-trihydroxynaphthalene-forming). This enzyme is also called scytalone 7,8-hydro-lyase.

In enzymology, an abietadiene synthase () is an enzyme that catalyzes the chemical reaction :(+)-copalyl diphosphate \rightleftharpoons (−)-abietadiene + diphosphate Hence, this enzyme has one substrate, (+)-copalyl diphosphate, and two products, (−)-abietadiene and diphosphate. This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on phosphates. The systematic name of this enzyme class is (+)-copalyl- diphosphate diphosphate-lyase [cyclizing (−)-abietadiene-forming]. This enzyme is also called copalyl-diphosphate diphosphate-lyase (cyclizing).

In enzymology, a 2-hydroxyisoflavanone dehydratase () is an enzyme that catalyzes the chemical reaction :2,7,4'-trihydroxyisoflavanone \rightleftharpoons daidzein + H2O Hence, this enzyme has one substrate, 2,7,4'-trihydroxyisoflavanone, and two products, daidzein and H2O. This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is 2,7,4'-trihydroxyisoflavanone hydro-lyase (daidzein-forming). This enzyme is also called 2,7,4'-trihydroxyisoflavanone hydro-lyase.

In enzymology, a 1,4-lactonase () is an enzyme that catalyzes the generic chemical reaction: :a 1,4-lactone + HO \rightleftharpoons a 4-hydroxyacid Thus, the two substrates of this enzyme are 1,4-lactone and HO, whereas its product is 4-hydroxyacid. This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is 1,4-lactone . This enzyme is also called gamma-lactonase.

In enzymology, an uronolactonase () is an enzyme that catalyzes the chemical reaction :D-glucurono-6,2-lactone + H2O \rightleftharpoons D-glucuronate Thus, the two substrates of this enzyme are D-glucurono-6,2-lactone and H2O, whereas its product is D-glucuronate. This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is D-glucurono-6,2-lactone lactonohydrolase. This enzyme is also called glucuronolactonase.

In enzymology, a formyl-CoA hydrolase () is an enzyme that catalyzes the chemical reaction :formyl-CoA + H2O \rightleftharpoons CoA + formate Thus, the two substrates of this enzyme are formyl-CoA and H2O, whereas its two products are CoA and formate. This enzyme belongs to the family of hydrolases, specifically those acting on thioester bonds. The systematic name of this enzyme class is formyl-CoA hydrolase. This enzyme is also called formyl coenzyme A hydrolase.

In enzymology, a glutathione thiolesterase () is an enzyme that catalyzes the chemical reaction :S-acylglutathione + H2O \rightleftharpoons glutathione + a carboxylate Thus, the two substrates of this enzyme are S-acylglutathione and H2O, whereas its two products are glutathione and carboxylate. This enzyme belongs to the family of hydrolases, specifically those acting on thioester bonds. The systematic name of this enzyme class is S-acylglutathione hydrolase. This enzyme is also called citryl-glutathione thioesterhydrolase.

In enzymology, a polynucleotide 5'-phosphatase () is an enzyme that catalyzes the chemical reaction :a 5'-phosphopolynucleotide + H2O \rightleftharpoons a polynucleotide + phosphate Thus, the two substrates of this enzyme are 5'-phosphopolynucleotide and H2O, whereas its two products are polynucleotide and phosphate. This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name of this enzyme class is polynucleotide 5'-phosphohydrolase. This enzyme is also called 5'-polynucleotidase.

In enzymology, an oxamate carbamoyltransferase () is an enzyme that catalyzes the chemical reaction :carbamoyl phosphate + oxamate \rightleftharpoons phosphate + oxalureate Thus, the two substrates of this enzyme are carbamoyl phosphate and oxamate, whereas its two products are phosphate and oxalureate. This enzyme belongs to the family of transferases that transfer one-carbon groups, specifically the carboxy- and carbamoyltransferases. The systematic name of this enzyme class is carbamoyl-phosphate:oxamate carbamoyltransferase. This enzyme is also called oxamic transcarbamylase.

In enzymology, an o-pyrocatechuate decarboxylase () is an enzyme that catalyzes the chemical reaction :2,3-dihydroxybenzoate \rightleftharpoons catechol + CO2 Hence, this enzyme has one substrate, 2,3-dihydroxybenzoate, and two products, catechol and CO2. This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is 2,3-dihydroxybenzoate carboxy-lyase (catechol-forming). This enzyme is also called 2,3-dihydroxybenzoate carboxy- lyase.

In enzymology, an oxalate decarboxylase () is an enzyme that catalyzes the chemical reaction :oxalate + H+ \rightleftharpoons formate + CO2 Thus, the two substrates of this enzyme are oxalate and H+, whereas its two products are formate and CO2. This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is oxalate carboxy-lyase (formate-forming). This enzyme is also called oxalate carboxy-lyase.

In enzymology, a sulfopyruvate decarboxylase () is an enzyme that catalyzes the chemical reaction :3-sulfopyruvate \rightleftharpoons 2-sulfoacetaldehyde + CO2 Hence, this enzyme has one substrate, 3-sulfopyruvate, and two products, 2-sulfoacetaldehyde and CO2. This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is 3-sulfopyruvate carboxy-lyase (2-sulfoacetaldehyde-forming). This enzyme is also called sulfopyruvate carboxy-lyase.

In enzymology, a threonine aldolase () is an enzyme that catalyzes the chemical reaction :L-threonine \rightleftharpoons glycine + acetaldehyde Hence, this enzyme has one substrate, L-threonine, and two products, glycine and acetaldehyde. This enzyme belongs to the family of lyases, specifically the aldehyde-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is L-threonine acetaldehyde-lyase (glycine-forming). This enzyme is also called L-threonine acetaldehyde-lyase.

In enzymology, an oxalomalate lyase () is an enzyme that catalyzes the chemical reaction :3-oxalomalate \rightleftharpoons oxaloacetate + glyoxylate Hence, this enzyme has one substrate, 3-oxalomalate, and two products, oxaloacetate and glyoxylate. This enzyme belongs to the family of lyases, specifically the oxo-acid-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is 3-oxalomalate glyoxylate-lyase (oxaloacetate-forming). This enzyme is also called 3-oxalomalate glyoxylate- lyase.

In enzymology, a phosphonopyruvate decarboxylase () is an enzyme that catalyzes the chemical reaction :3-phosphonopyruvate \rightleftharpoons 2-phosphonoacetaldehyde + CO2 Hence, this enzyme has one substrate, 3-phosphonopyruvate, and two products, 2-phosphonoacetaldehyde and CO2. This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is 3-phosphonopyruvate carboxy-lyase (2-phosphonoacetaldehyde-forming). This enzyme is also called 3-phosphonopyruvate carboxy-lyase.

In enzymology, a malonate CoA-transferase () is an enzyme that catalyzes the chemical reaction :acetyl-CoA + malonate \rightleftharpoons acetate + malonyl- CoA Thus, the two substrates of this enzyme are acetyl-CoA and malonate, whereas its two products are acetate and malonyl-CoA. This enzyme belongs to the family of transferases, specifically the CoA-transferases. The systematic name of this enzyme class is acetyl-CoA:malonate CoA-transferase. This enzyme is also called malonate coenzyme A-transferase.

The chemical specificity of an enzyme for a particular substrate can be found using two variables that are derived from the Michaelis-Menten equation. km approximates the dissociation constant of enzyme-substrate complexes. kcat represents the turnover rate, or the number of reactions catalyzed by an enzyme over the enzyme amount. kcat over km is known as the specificity constant, which gives a measure of the affinity of a substrate to some particular enzyme.

Valencene synthase () is an enzyme with systematic name (2E,6E)-farnesyl- diphosphate diphosphate-lyase (valencene-forming). It is a terpene cyclase enzyme responsible for the biosynthesis of valencene, a sesquiterpene, using farnesyl pyrophosphate as its substrate. The first such enzyme was isolated using orange cDNA. This enzyme catalyses the following chemical reaction : (2E,6E)-farnesyl diphosphate \rightleftharpoons (+)-valencene + diphosphate The recombinant enzyme from Vitis vinifera forms (+)-valencene and (-)-7-epi- alpha-selinene.

Schematic diagram of the ubiquitylation system. The ubiquitin ligase is referred to as an E3, and operates in conjunction with an E1 ubiquitin-activating enzyme and an E2 ubiquitin-conjugating enzyme. There is one major E1 enzyme, shared by all ubiquitin ligases, that uses ATP to activate ubiquitin for conjugation and transfers it to an E2 enzyme. The E2 enzyme interacts with a specific E3 partner and transfers the ubiquitin to the target protein.

In enzymology, a pentanamidase () is an enzyme that catalyzes the chemical reaction :pentanamide + H2O \rightleftharpoons pentanoate + NH3 Thus, the two substrates of this enzyme are pentanamide and H2O, whereas its two products are valerate and NH3. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is pentanamide amidohydrolase. This enzyme is also called valeramidase.

In enzymology, an allantoinase () is an enzyme that catalyzes the chemical reaction :(S)-allantoin + H2O \rightleftharpoons allantoate Thus, the two substrates of this enzyme are (S)-allantoin and H2O, whereas its product is allantoate. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amides. The systematic name of this enzyme class is (S)-allantoin amidohydrolase. This enzyme participates in purine metabolism.

In enzymology, a chitin deacetylase () is an enzyme that catalyzes the chemical reaction :chitin + H2O \rightleftharpoons chitosan + acetate Thus, the two substrates of this enzyme are chitin and H2O, whereas its two products are chitosan and acetate. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is chitin amidohydrolase. This enzyme participates in aminosugars metabolism.

In enzymology, a methylguanidinase () is an enzyme that catalyzes the chemical reaction :methylguanidine + H2O \rightleftharpoons methylamine + urea Thus, the two substrates of this enzyme are methylguanidine and H2O, whereas its two products are methylamine and urea. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amidines. The systematic name of this enzyme class is methylguanidine amidinohydrolase. This enzyme is also called methylguanidine hydrolase.

In enzymology, a guanidinoacetase () is an enzyme that catalyzes the chemical reaction :guanidinoacetate + H2O \rightleftharpoons glycine + urea Thus, the two substrates of this enzyme are guanidinoacetate and H2O, whereas its two products are glycine and urea. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amidines. The systematic name of this enzyme class is guanidinoacetate amidinohydrolase. This enzyme is also called glycocyaminase.

In enzymology, an uridine nucleosidase () is an enzyme that catalyzes the chemical reaction :uridine + H2O \rightleftharpoons D-ribose + uracil Thus, the two substrates of this enzyme are uridine and H2O, whereas its two products are D-ribose and uracil. This enzyme belongs to the family of hydrolases, specifically those glycosylases that hydrolyse N-glycosyl compounds. The systematic name of this enzyme class is uridine ribohydrolase. This enzyme is also called uridine hydrolase.

In enzymology, a taurine-pyruvate aminotransferase () is an enzyme that catalyzes the chemical reaction :taurine + pyruvate \rightleftharpoons L-alanine + 2-sulfoacetaldehyde Thus, the two substrates of this enzyme are taurine and pyruvate, whereas its two products are L-alanine and 2-sulfoacetaldehyde. This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is taurine:pyruvate aminotransferase. This enzyme is also called Tpa.

In enzymology, a glycine-oxaloacetate transaminase () is an enzyme that catalyzes the chemical reaction :glycine + oxaloacetate \rightleftharpoons glyoxylate + L-aspartate Thus, the two substrates of this enzyme are glycine and oxaloacetate, whereas its two products are glyoxylate and L-aspartate. This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is glycine:oxaloacetate aminotransferase. This enzyme is also called glycine-oxaloacetate aminotransferase.

In enzymology, a pyridoxamine-pyruvate transaminase () is an enzyme that catalyzes the chemical reaction :pyridoxamine + pyruvate \rightleftharpoons pyridoxal + L-alanine Thus, the two substrates of this enzyme are pyridoxamine and pyruvate, whereas its two products are pyridoxal and L-alanine. This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is pyridoxamine:pyruvate aminotransferase. This enzyme is also called pyridoxamine-pyruvic transaminase.

In enzymology, a pyridoxamine-oxaloacetate transaminase () is an enzyme that catalyzes the chemical reaction :pyridoxamine + oxaloacetate \rightleftharpoons pyridoxal + L-aspartate Thus, the two substrates of this enzyme are pyridoxamine and oxaloacetate, whereas its two products are pyridoxal and L-aspartate. This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is pyridoxamine:oxaloacetate aminotransferase. This enzyme participates in vitamin B6 metabolism.

In enzymology, a phosphate butyryltransferase () is an enzyme that catalyzes the chemical reaction :butanoyl-CoA + phosphate \rightleftharpoons CoA + butanoyl phosphate Thus, the two substrates of this enzyme are butanoyl-CoA and phosphate, whereas its two products are CoA and butanoyl phosphate. This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is butanoyl-CoA:phosphate butanoyltransferase. This enzyme is also called phosphotransbutyrylase.

Acetylindoxyl oxidase () is an enzyme that catalyzes the chemical reaction :N-acetylindoxyl + O2 \rightleftharpoons N-acetylisatin + (?) Thus, the two substrates of this enzyme are N-acetylindoxyl and oxygen, whereas its product is N-acetylisatin. This enzyme belongs to the family of oxidoreductases, specifically those acting on other nitrogenous compounds as donors with oxygen as acceptor. The systematic name of this enzyme class is N-acetylindoxyl:oxygen oxidoreductase. This enzyme participates in tryptophan metabolism.

Instead, the newborn's urine is analyzed for levels of branched-chain alpha-hydroxyacids and alpha- ketoacids. The amount and type of enzyme activity in an affected individual with MSUD will determine which classification the affected individual will identify with. Classic MSUD: Less than 2% of normal enzyme activity Intermediate MSUD: 3-8% normal enzyme activity Intermittent MSUD: 8-15% of normal enzyme activity Thiamine-Responsive MSUD: Large doses of thiamine will increase enzyme activity.

In enzymology, an isopenicillin N epimerase () is an enzyme that catalyzes the chemical reaction :isopenicillin N \rightleftharpoons penicillin N Hence, this enzyme has one substrate, isopenicillin N, and one product, penicillin N. This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on amino acids and derivatives. The systematic name of this enzyme class is penicillin N 5-amino-5-carboxypentanoyl-epimerase. This enzyme participates in penicillin and cephalosporin biosynthesis.

In enzymology, a protein-serine epimerase () is an enzyme that catalyzes the chemical reaction :[protein]-L-serine \rightleftharpoons [protein]-D-serine Hence, this enzyme has one substrate, [protein]-L-serine, and one product, [protein]-D-serine. This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on amino acids and derivatives. The systematic name of this enzyme class is [protein]-serine epimerase. This enzyme is also called protein-serine racemase.

In enzymology, a thiocyanate isomerase () is an enzyme that catalyzes the chemical reaction :benzyl isothiocyanate \rightleftharpoons benzyl thiocyanate Hence, this enzyme has one substrate, benzyl isothiocyanate, and one product, benzyl thiocyanate. This enzyme belongs to the family of isomerases, specifically those other isomerases sole sub-subclass for isomerases that do not belong in the other subclasses. The systematic name of this enzyme class is benzyl-thiocyanate isomerase. This enzyme is also called isothiocyanate isomerase.

In enzymology, a deacetylipecoside synthase () is an enzyme that catalyzes the chemical reaction :deacetylipecoside + H2O \rightleftharpoons dopamine + secologanin Thus, the two substrates of this enzyme are deacetylipecoside and H2O, whereas its two products are dopamine and secologanin. This enzyme belongs to the family of lyases, specifically amine lyases, which cleave carbon-nitrogen bonds. The systematic name of this enzyme class is deacetylipecoside dopamine-lyase (secologanin-forming). This enzyme is also called deacetylipecoside dopamine-lyase.

In enzymology, a deacetylisoipecoside synthase () is an enzyme that catalyzes the chemical reaction :deacetylisoipecoside + H2O \rightleftharpoons dopamine + secologanin Thus, the two substrates of this enzyme are deacetylisoipecoside and H2O, whereas its two products are dopamine and secologanin. This enzyme belongs to the family of lyases, specifically amine lyases, which cleave carbon-nitrogen bonds. The systematic name of this enzyme class is deacetylisoipecoside dopamine-lyase (secologanin-forming). This enzyme is also called deacetylisoipecoside dopamine-lyase.

In enzymology, a vomilenine glucosyltransferase () is an enzyme that catalyzes the chemical reaction :UDP-glucose + vomilenine \rightleftharpoons UDP + raucaffricine Thus, the two substrates of this enzyme are UDP-glucose and vomilenine, whereas its two products are UDP and raucaffricine. This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP- glucose:vomilenine 21-O-beta-D-glucosyltransferase. This enzyme is also called UDPG:vomilenine 21-beta-D-glucosyltransferase.

In enzymology, an anthranilate adenylyltransferase () is an enzyme that catalyzes the chemical reaction :ATP + anthranilate \rightleftharpoons diphosphate + N-adenylylanthranilate Thus, the two substrates of this enzyme are ATP and anthranilate, whereas its two products are diphosphate and N-adenylylanthranilate. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is ATP:anthranilate N-adenylyltransferase. This enzyme is also called anthranilic acid adenylyltransferase.

In enzymology, a glycosaminoglycan galactosyltransferase () is an enzyme that catalyzes the chemical reaction :UDP-galactose + glycosaminoglycan \rightleftharpoons UDP + D-galactosylglycosaminoglycan Thus, the two substrates of this enzyme are UDP-galactose and glycosaminoglycan, whereas its two products are UDP and D-galactosylglycosaminoglycan. This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-galactose:glycosaminoglycan D-galactosyltransferase. This enzyme is also called uridine diphosphogalactose-mucopolysaccharide galactosyltransferase.

In enzymology, a guanosine phosphorylase () is an enzyme that catalyzes the chemical reaction :guanosine + phosphate \rightleftharpoons guanine + alpha-D- ribose 1-phosphate Thus, the two substrates of this enzyme are guanosine and phosphate, whereas its two products are guanine and alpha-D-ribose 1-phosphate. This enzyme belongs to the family of glycosyltransferases, specifically the pentosyltransferases. The systematic name of this enzyme class is guanosine:phosphate alpha-D-ribosyltransferase. This enzyme participates in purine metabolism.

In enzymology, an indoxyl-UDPG glucosyltransferase () is an enzyme that catalyzes the chemical reaction :UDP-glucose + indoxyl \rightleftharpoons UDP + indican Thus, the two substrates of this enzyme are UDP-glucose and indoxyl, whereas its two products are UDP and indican. This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-glucose:indoxyl 3-O-beta-D- glucosyltransferase. This enzyme is also called indoxyl-UDPG- glucosyltransferase.

Kallikrein 13 (, KLK13, kallikrein mK13, mGK-13, mK13, mKLK13, prorenin converting enzyme 1, PRECE-1, prorenin-converting enzyme, PRECE, proteinase P) is an enzyme. This enzyme catalyses the following chemical reaction : Hydrolyses mouse Ren2 protein (a species of prorenin present in the submandibular gland) on the carboxy side of the arginine residue at the Lys- Arg- pair in the N-terminus, to yield mature renin This enzyme belongs in peptidase family S1A.

Artemisinic aldehyde Delta11(13)-reductase (, Dbr2) is an enzyme with systematic name artemisinic aldehyde:NADP+ oxidoreductase. This enzyme catalyses the following chemical reaction : (11R)-dihydroartemisinic aldehyde + NADP+ \rightleftharpoons artemisinic aldehyde + NADPH + H+ This enzyme i present in Artemisia annua.

Miltiradiene synthase (, SmMDS, SmiKSL) is an enzyme with systematic name (+)-copaly-diphosphate diphosphate-lyase (cyclizing, miltiradiene-forming). This enzyme catalyses the following chemical reaction : (+)-copalyl diphosphate \rightleftharpoons miltiradiene + diphosphate This enzyme is isolated from the plant Selaginella moellendorffii.

Delta-guaiene synthase () is an enzyme with systematic name (2E,6E)-farnesyl- diphosphate diphosphate-lyase (cyclizing, delta-guaiene-forming). This enzyme catalyses the following chemical reaction : (2E,6E)-farnesyl diphosphate \rightleftharpoons delta-guaiene + diphosphate This enzyme requires Mg2+.

CTP-dependent riboflavin kinase (, Methanocaldococcus jannaschii Mj0056, Mj0056) is an enzyme with systematic name CTP:riboflavin 5′-phosphotransferase. This enzyme catalyses the following chemical reaction : CTP + riboflavin \rightleftharpoons CDP + FMN This archaeal enzyme uses CTP as the donor nucleotide.

4-sulfomuconolactone hydrolase () is an enzyme with systematic name 4-sulfomuconolactone sulfohydrolase. This enzyme catalyses the following chemical reaction : 4-sulfomuconolactone + H2O \rightleftharpoons maleylacetate + sulfite The enzyme was isolated from the bacteria Hydrogenophaga intermedia and Agrobacterium radiobacter S2.

Geraniol isomerase () is an enzyme with systematic name geraniol hydroxymutase. This enzyme catalyses the following chemical reaction : geraniol \rightleftharpoons (3S)-linalool In absence of oxygen the bifunctional linalool dehydratase-isomerase could act as an enzyme from this class.

To reduce enzyme activity, inhibitor molecules bind to enzymes. Reducing enzyme activity can disable a pathogen or correct an incorrectly function system; as such, many enzyme inhibitors are developed to be used as drugs by the general public.

Salicylate synthase is an enzyme that catalyzes the chemical reaction: :chorismate → salicylic acid MbtI is the responsible enzyme from Mycobacterium tuberculosis.

The enzyme quercitrinase can be found in Aspergillus flavus.quercitrinase on www.brenda-enzymes.org It is an enzyme in the rutin catabolic pathway.

This enzyme is also called formylmethanofuran:(acceptor) oxidoreductase. This enzyme participates in folate biosynthesis. It has 2 cofactors: molybdenum, and Pterin.

This enzyme is also called monohaloacetate dehalogenase and fluoroacetate dehalogenase. This enzyme participates in gamma-hexachlorocyclohexane degradation and 1,2-dichloroethane degradation.

The systematic name of this enzyme class is maltose-6'-phosphate 6-phosphoglucohydrolase. This enzyme is also called phospho-alpha-glucosidase.

This enzyme participates in glutamate metabolism and alanine and aspartate metabolism. This enzyme can be found in mammals, plants, and bacteria.

This enzyme is also called 4-hydroxybenzoate 1-monooxygenase. This enzyme participates in 2,4-dichlorobenzoate degradation. It employs one cofactor, FAD.

It employs one cofactor, heme. This enzyme needs Ca2+ for activity. White rot fungi secrete this enzyme to aid lignin degradation.

Other artificial enzyme inhibitors block acetylcholinesterase, an enzyme which breaks down acetylcholine, and are used as nerve agents in chemical warfare.

In the reaction that the enzyme uses it requires only one cofactor, a compound required for activation, which is NADP(+) however it is uncertain if this compound truly activates the enzyme. GDP- Fucose is an allosteric inhibitor of the enzyme. Here is a pymol view of the entire structure of the GDP-Mannose 4, 6-Dehydratase enzyme.

Malonyl-S-ACP decarboxylase (, malonyl-S-acyl-carrier protein decarboxylase, MdcD/MdcE, MdcD,E) is an enzyme with systematic name malonyl-(acyl-carrier- protein) carboxy-lyase. This enzyme catalyses the following chemical reaction : a malonyl-[acyl-carrier protein] + H+ \rightleftharpoons an acetyl-[acyl- carrier protein] + CO2 This enzyme comprises the beta and gamma subunits of the enzyme EC 4.1.1.88.

In enzymology, a steroid-lactonase () is an enzyme that catalyzes the chemical reaction :testololactone + H2O \rightleftharpoons testolate Thus, the two substrates of this enzyme are testololactone and H2O, whereas its product is testolate. This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is testololactone lactonohydrolase.

ADAMTS13 endopeptidase (, ADAMTS VWF cleaving metalloprotease, ADAMTS-13, ADAMTS13, vWF-cleaving protease, VWF-CP, vWF-degrading protease, Upshaw factor, von Willebrand factor cleaving protease, ADAMTS13 peptidase) is an enzyme. This enzyme catalyses the following chemical reaction : The enzyme cleaves the von Willebrand factor at bond Tyr842-Met843 within the A2 domain This enzyme belong in the peptidase family M12.

Chorismate lyase is an enzyme that transforms chorismate into 4-hydroxybenzoate and pyruvate. This enzyme catalyses the first step in ubiquinone biosynthesis in Escherichia coli and other Gram-negative bacteria. Benzoate 4-monooxygenase is an enzyme that utilizes benzoate, NADPH, H+ and O2 to produce 4-hydroxybenzoate, NADP+ and H2O. This enzyme can be found in Aspergillus niger.

HycI peptidase (, HycI, HycE processing protein) is an enzyme. This enzyme catalyses the following chemical reaction : This enzyme specifically removes a 32-amino acid peptide from the C-terminus of the precursor of the large subunit of hydrogenase 3 in Escherichia coli by cleavage at the C-terminal side of Arg537. This enzyme belongs to the peptidase family A31.

Pyrethroid hydrolase (, pyrethroid-hydrolyzing carboxylesterase, pyrethroid- hydrolysing esterase, pyrethroid-hydrolyzing esterase, pyrethroid-selective esterase, pyrethroid-cleaving enzyme, permethrinase, PytH, EstP) is an enzyme with systematic name pyrethroid-ester hydrolase. This enzyme catalyses the following chemical reaction : trans-permethrin + H2O \rightleftharpoons (3-phenoxyphenyl)methanol + (1S,3R)-3-(2,2-dichloroethenyl)-2,2-dimethylcyclopropanecarboxylate The enzyme is involved in degradation of pyrethroid pesticides.

Galactan endo-beta-1,3-galactanase (, endo-beta-1,3-galactanase) is an enzyme with systematic name arabinogalactan 3-beta-D-galactanohydrolase. This enzyme catalyses the following chemical reaction : The enzyme specifically hydrolyses beta-1,3-galactan and beta-1,3-galactooligosaccharides The enzyme from the fungus Flammulina velutipes (winter mushroom) hydrolyses the beta(1->3) bonds found in type II plant arabinogalactans.

In enzymology, a selenate reductase () is an enzyme that catalyzes the chemical reaction :selenite + H2O + acceptor \rightleftharpoons selenate + reduced acceptor The 3 substrates of this enzyme are selenite, H2O, and acceptor, whereas its two products are selenate and reduced acceptor. This enzyme belongs to the family of oxidoreductases. The systematic name of this enzyme class is selenite:reduced acceptor oxidoreductase.

In enzymology, a tetrachloroethene reductive dehalogenase () is an enzyme that catalyzes the chemical reaction. This is a member of reductive dehalogenase enzyme family. :trichloroethene + chloride + acceptor \rightleftharpoons tetrachloroethene + reduced acceptor The 3 substrates of this enzyme are trichloroethene, chloride, and acceptor, whereas its two products are tetrachloroethene and reduced acceptor. This enzyme belongs to the family of oxidoreductases.

In enzymology, an isopiperitenone Delta-isomerase () is an enzyme that catalyzes the chemical reaction :isopiperitenone \rightleftharpoons piperitenone Hence, this enzyme has one substrate, isopiperitenone, and one product, piperitenone. This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases transposing C=C bonds. The systematic name of this enzyme class is isopiperitenone Delta8-Delta4-isomerase.

Alanine carboxypeptidase (, N-benzoyl-L-alanine-amidohydrolase) is an enzyme. This enzyme catalyses the following chemical reaction : Release of a C-terminal alanine from a peptide or a variety of pteroyl or acyl groups This enzyme is isolated from soil bacteria. The enzyme from Corynebacterium equi also hydrolyses N-benzoylglycine and N-benzoyl-L-aminobutyric acid.

GPR endopeptidase (, germination proteinase) is an enzyme. This enzyme catalyses the following chemical reaction: : Endopeptidase action with P4 Glu or Asp, P1 preferably Glu > Asp, P1' hydrophobic and P2' Ala This enzyme participates in spore germination in Bacillus megaterium.

Sulfoacetaldehyde dehydrogenase (acylating) (, SauS) is an enzyme with systematic name 2-sulfoacetaldehyde:NADP+ oxidoreductase (CoA-acetylating). This enzyme catalyses the following chemical reaction : 2-sulfoacetaldehyde + CoA + NADP+ \rightleftharpoons sulfoacetyl-CoA + NADPH + H+ The enzyme is involved in degradation of sulfoacetate.

Festuclavine dehydrogenase (, FgaFS, festuclavine synthase) is an enzyme with systematic name festuclavine:NAD+ oxidoreductase. This enzyme catalyses the following chemical reaction : festuclavine + NAD+ \rightleftharpoons 6,8-dimethyl-6,7-didehydroergoline + NADH + H+ The enzyme takes part in the biosynthesis of fumigaclavine C.

Abstract In this sense, the medium environment in this system is close to that of an enzyme. The major difference between this system and enzyme is lattice flexibility. The lattice of zeolite is rigid, whereas the enzyme is flexible.

Squalene—-hopanol cyclase (, squalene—-hopene cyclase) is an enzyme with systematic name hopan-22-ol hydro-lyase. This enzyme catalyses the following chemical reaction : hopan-22-ol \rightleftharpoons squalene + H2O The enzyme produces the cyclization products hopene and hopanol.

Neoabietadiene synthase (, AgAS, PtTPS-LAS) is an enzyme with systematic name (+)-copaly-diphosphate diphosphate-lyase (cyclizing, neoabietadiene-forming). This enzyme catalyses the following chemical reaction: : (+)-copalyl diphosphate \rightleftharpoons neoabietadiene + diphosphate This enzyme is isolated from Abies grandis (grand fir).

21S rRNA pseudouridine2819 synthase (, Pus5p) is an enzyme with systematic name 21S rRNA-uridine2819 uracil mutase. This enzyme catalyses the following chemical reaction : 21S rRNA uridine2819 \rightleftharpoons 21S rRNA pseudouridine2819 The enzyme specifically acts on uridine2819 in 21S rRNA.

Quinate dehydrogenase (quinone) (, NAD(P)+-independent quinate dehydrogenase, quinate:pyrroloquinoline-quinone 5-oxidoreductase) is an enzyme with systematic name quinate:quinol 3-oxidoreductase. This enzyme catalyses the following chemical reaction : quinate + quinone \rightleftharpoons 3-dehydroquinate + quinol This enzyme is membrane-bound.

Zerumbone synthase (, ZSD1) is an enzyme with systematic name 10-hydroxy- alpha-humulene:NAD+ oxidoreductase. This enzyme catalyses the following chemical reaction : 10-hydroxy-alpha-humulene + NAD+ \rightleftharpoons zerumbone + NADH + H+ The enzyme was cloned from shampoo ginger, Zingiber zerumbet.

Secoisolariciresinol dehydrogenase () is an enzyme with the systematic name (-)-secoisolariciresinol:NAD+ oxidoreductase. This enzyme catalyses the following chemical reaction: : (-)-secoisolariciresinol + 2 NAD+ \rightleftharpoons (-)-matairesinol + 2 NADH + 2 H+ This enzyme is isolated from the plants Forsythia intermedia and Podophyllum peltatum.

Uracil dehydrogenase (, uracil oxidase) is an enzyme with systematic name uracil:(acceptor) oxidoreductase. This enzyme catalyses the following chemical reaction : uracil + acceptor \rightleftharpoons barbiturate + reduced acceptor Also oxidizes thymine. The enzyme acts on the hydrated derivative of the substrate.

L-threonine kinase (, PduX) is an enzyme with systematic name ATP:L-threonine O3-phosphotransferase. This enzyme catalyses the following chemical reaction : ATP + L-threonine \rightleftharpoons ADP + O-phospho-L-threonine The enzyme takes part in the synthesis of adenosylcobalamin.

Venom exonuclease (, venom phosphodiesterase) is an enzyme. This enzyme catalyses the following chemical reaction Exonucleolytic cleavage in the 3'- to 5'- direction to yield nucleoside 5'-phosphates (exonuclease type a) center This enzyme has preference for single-stranded substrate.

Isotuberculosinol synthase (, Rv3378c) is an enzyme with systematic name tuberculosinyl diphosphate diphosphohydrolase (isotuberculosinol forming). This enzyme catalyses the following chemical reaction : tuberculosinyl diphosphate + H2O \rightleftharpoons (13S)-isotuberculosinol + diphosphate This enzyme is present in species of Mycobacterium that cause tuberculosis.

This enzyme participates in pyruvate metabolism and carbon fixation. NAD-malic enzyme is one of three decarboxylation enzymes used in the inorganic carbon concentrating mechanisms of C4 and CAM plants. The others are NADP-malic enzyme and PEP carboxykinase.

Metallocarboxypeptidase D (, carboxypeptidase D (cattle, human, mouse, rat), gp180 (duck)) is an enzyme. This enzyme catalyses the following chemical reaction : Releases C-terminal Arg and Lys from polypeptides This enzyme is activated by Co2+, and inhibited by guanidinoethylmercaptosuccinic acid.

Streptopain (, Streptococcus peptidase A, streptococcal cysteine proteinase, Streptococcus protease) is an enzyme. This enzyme catalyses the following chemical reaction : Preferential cleavage with hydrophobic residues at P2, P1 and P1' This enzyme is isolated from the bacterium, group A Streptococcus.

Oligopeptidase B (, protease II, Escherichia coli alkaline proteinase II) is an enzyme. This enzyme catalyses the following chemical reaction : Hydrolysis of -Arg-, -Lys- bonds in oligopeptides, even when P1' residue is proline This enzyme is present in Escherichia coli.

The systematic name of this enzyme class is dethiobiotin:sulfur sulfurtransferase. This enzyme participates in biotin metabolism. It employs one cofactor, iron-sulfur.

This enzyme participates in fatty acid biosynthesis. A C-terminal conserved domain within this enzyme contains most of the active site residues.

This enzyme is also called 5-pyridoxate oxidase. This enzyme participates in vitamin B6 metabolism. It has 2 cofactors: FAD, and Flavoprotein.

This enzyme participates in starch and sucrose metabolism in plants. Studies of the enzyme from potato led to the discovery of cycloamylose.

Botryococcus squalene synthase (, SSL-2 (gene)) is an enzyme with systematic name squalene:NADP+ oxidoreductase. This enzyme catalyses the following chemical reaction : squalene + diphosphate + NADP+ \rightleftharpoons presqualene diphosphate + NADPH + H+ This enzyme is isolated from the green alga Botryococcus braunii BOT22.

Botryococcene synthase (, SSL-3 (gene)) is an enzyme with systematic name C30 botryococcene:NADP+ oxidoreductase. This enzyme catalyses the following chemical reaction : C30 botryococcene + NADP+ \+ diphosphate \rightleftharpoons presqualene diphosphate + NADPH + H+ This enzyme is isolated from the green alga Botryococcus braunii BOT22.

Salicylate decarboxylase (, salicylic acid decarboxylase, Scd) is an enzyme with systematic name salicylate carboxy-lyase. This enzyme catalyses the following chemical reaction : salicylate \rightleftharpoons phenol + CO2 In the reverse direction the enzyme catalyses the regioselective carboxylation of phenol into salicylate.

Glycine N-phenylacetyltransferase (, arylacetyl-CoA N-acyltransferase, arylacetyltransferase, GAT (gene)) is an enzyme with systematic name phenylacetyl-CoA:glycine N-phenylacetyltransferase. This enzyme catalyses the following chemical reaction : phenylacetyl-CoA + glycine \rightleftharpoons CoA + phenylacetylglycine This enzyme was purified from bovine liver mitochondria.

Mycolysin (, pronase component, Streptomyces griseus neutral proteinase, actinase E, SGNPI) is an enzyme. This enzyme catalyses the following chemical reaction : Preferential cleavage of bonds with hydrophobic residues in P1' This enzyme is present in Streptomyces griseus, S. naraensis, and S. cacaoi.

Streptothricin hydrolase (, sttH (gene)) is an enzyme with systematic name streptothricin-F hydrolase. This enzyme catalyses the following chemical reaction : streptothricin-F + H2O \rightleftharpoons streptothricin-F acid The enzyme also catalyses the hydrolysis of streptothricin-D to streptothricin-D acid.

In enzymology, a 3-mercaptopyruvate sulfurtransferase () is an enzyme that catalyzes the chemical reactions of 3-mercaptopyruvate. This enzyme belongs to the family of transferases, specifically the sulfurtransferases. This enzyme participates in cysteine metabolism. It is encoded by the MPST gene.

5-nitroanthranilic acid aminohydrolase (, naaA (gene), 5NAA deaminase) is an enzyme with systematic name 5-nitroanthranilate amidohydrolase. This enzyme catalyses the following chemical reaction : 5-nitroanthranilate + H2O \rightleftharpoons 5-nitrosalicylate + NH3 The enzyme is present in Bradyrhizobium sp. strain JS329.

Steroid-transporting ATPase (, pleiotropic-drug-resistance protein, PDR protein) is an enzyme with systematic name ATP phosphohydrolase (steroid- exporting). This enzyme catalyses the following chemical reaction : ATP + H2O + steroidin \rightleftharpoons ADP + phosphate + steroidout This enzyme has two similar ATP-binding domains.

In the presence of .5 mM of Co(2+) and Mn(2+) the enzyme activity was increased fourfold. Mg(2+) is the ion that increases the enzyme activity the most. With .5 mM of Mg(2+) enzyme activity was increased sixfold.

3-Fumarylpyruvate hydrolase (, nagK (gene), naaD (gene)) is an enzyme with systematic name 3-fumarylpyruvate hydrolyase. This enzyme catalyses the following chemical reaction : 3-fumarylpyruvate + H2O \rightleftharpoons fumarate + pyruvate The enzyme is involved in bacterial degradation of 5-substituted salicylates.

D-amino acid dehydrogenase (quinone) (, DadA) is an enzyme with systematic name D-amino acid:quinone oxidoreductase (deaminating). This enzyme catalyses the following chemical reaction : D-amino acid + H2O + quinone \rightleftharpoons 2-oxo carboxylate + NH3 \+ quinol This enzyme is iron- sulfur flavoprotein.

Methylamine dehydrogenase (amicyanin) (, amine dehydrogenase, primary-amine dehydrogenase) is an enzyme with systematic name methylamine:amicyanin oxidoreductase (deaminating). This enzyme catalyses the following chemical reaction: : methylamine + H2O + amicyanin \rightleftharpoons formaldehyde + ammonia + reduced amicyanin This enzyme contains tryptophan tryptophylquinone (TTQ) co-factor.

Flavin reductase (NADH) (, NADH-dependent flavin reductase, flavin:NADH oxidoreductase) is an enzyme with systematic name flavin:NAD+ oxidoreductase. This enzyme catalyses the following chemical reaction : reduced flavin + NAD+ \rightleftharpoons flavin + NADH + H+ The Escherichia coli enzyme reduces free flavins by NADH.

Spermine oxidase (, PAOh1/SMO, AtPAO1, AtPAO4, SMO) is an enzyme with systematic name spermidine:oxygen oxidoreductase (spermidine-forming). This enzyme catalyses the following chemical reaction : spermine + O2 \+ H2O \rightleftharpoons spermidine + 3-aminopropanal + H2O2 The enzyme from Arabidopsis thaliana oxidizes norspermine to norspermidine.

4-methylaminobutanoate oxidase (formaldehyde-forming) (, mabO (gene)) is an enzyme with systematic name 4-methylaminobutanoate:oxygen oxidoreductase (formaldehyde-forming). This enzyme catalyses the following chemical reaction : 4-methylaminobutanoate + O2 \+ H2O \rightleftharpoons 4-aminobutanoate + formaldehyde + H2O2 This enzyme is a flavoprotein (FAD).

Cysteate synthase () is an enzyme with systematic name sulfite:O-phospho-L- serine sulfotransferase (phosphate-hydrolysing, L-cysteate-forming). This enzyme catalyses the following chemical reaction : O-phospho-L-serine + sulfite \rightleftharpoons L-cysteate + phosphate This enzyme is a pyridoxal- phosphate protein.

Enzyme specificity refers to the interactions between any particular enzyme and its corresponding substrate. In addition to the specificity in binding its substrates, correct proximity and orientation as well as binding the transition state provide an additional layer of enzyme specificity.

Epi-isozizaene synthase (, SCO5222 protein) is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate diphosphate-lyase ((+)-epi-isozizaene-forming). This enzyme catalyses the following chemical reaction : (2E,6E)-farnesyl diphosphate \rightleftharpoons (+)-epi-isozizaene + diphosphate This enzyme requires Mg2+ for activity.

3-hydroxypropionyl-CoA dehydratase () is an enzyme with systematic name 3-hydroxypropionyl-CoA hydro-lyase. This enzyme catalyses the following chemical reaction : 3-hydroxypropanoyl-CoA \rightleftharpoons acrylyl-CoA + H2O This enzyme catalyses a step in the 3-hydroxypropionate/4-hydroxybutyrate cycle.

Tetrahymanol synthase (, squaleneatetrahymanol cyclase) is an enzyme with systematic name squalene hydro-lyase (tetrahymanol forming). This enzyme catalyses the following chemical reaction : tetrahymanol \rightleftharpoons squalene + H2O The reaction occurs in the reverse direction. This enzyme is isolated from Tetrahymena protozoans.

Alpha-santalene synthase () is an enzyme with systematic name (2E,6E)-farnesyl diphosphate lyase (cyclizing, (+)-alpha-santalene-forming). This enzyme catalyses the following chemical reaction : (2E,6E)-farnesyl diphosphate \rightleftharpoons (+)-alpha-santalene + diphosphate The enzyme synthesizes a mixture of sesquiterpenes.

Alpha-guaiene synthase (, PatTps177 (gene)) is an enzyme with systematic name (2Z,6E)-farnesyl-diphosphate diphosphate-lyase (cyclizing, alpha-guaiene- forming). This enzyme catalyses the following chemical reaction : (2E,6E)-farnesyl diphosphate \rightleftharpoons alpha-guaiene + diphosphate This enzyme requires Mg2+.

Presilphiperfolanol synthase (, BcBOT2, CND15) is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate diphosphohydrolase (presilphiperfolan-8beta- ol-forming). This enzyme catalyses the following chemical reaction : (2E,6E)-farnesyl diphosphate + H2O \rightleftharpoons presilphiperfolan-8beta- ol + diphosphate This enzyme requires Mg2+.

Alpha-terpinene synthase () is an enzyme with systematic name geranyl- diphosphate diphosphate-lyase (cyclizing, alpha-terpinene-forming). This enzyme catalyses the following chemical reaction : geranyl diphosphate \rightleftharpoons alpha-terpinene + diphosphate The enzyme has been characterized from Dysphania ambrosioides (American wormseed).

Longifolene synthase () is an enzyme with systematic name (2E,6E)-farnesyl- diphosphate diphosphate-lyase (longifolene-forming). This enzyme catalyses the following chemical reaction : (2E,6E)-farnesyl diphosphate \rightleftharpoons longifolene + diphosphate This enzyme forms alpha-longipinene, longicyclene and traces of other sesquiterpenoids.

Parkeol synthase () is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualene mutase (cyclizing, parkeol-forming). This enzyme catalyses the following chemical reaction : (3S)-2,3-epoxy-2,3-dihydrosqualene \rightleftharpoons parkeol The enzyme from rice (Oryza sativa) produces only parkeol.

Cyclic alcohol dehydrogenase (quinone) (, cyclic alcohol dehydrogenase, MCAD) is an enzyme with systematic name cyclic alcohol:quinone oxidoreductase. This enzyme catalyses the following chemical reaction : cyclic alcohol + quinone \rightleftharpoons cyclic ketone + quinol This enzyme oxidizes a wide variety of cyclic alcohols.

Eugenol synthase (, LtCES1, EGS1, EGS2) is an enzyme with systematic name eugenol:NADP+ oxidoreductase (coniferyl ester reducing). This enzyme catalyses the following chemical reaction: eugenol + a carboxylate + NADP+ \rightleftharpoons a coniferyl ester + NADPH + H+ The enzyme acts in the reverse direction.

Isoeugenol synthase (, IGS1, t-anol/isoeugenol synthase 1) is an enzyme with systematic name eugenol:NADP+ oxidoreductase (coniferyl acetate reducing). This enzyme catalyses the following chemical reaction. : isoeugenol + acetate + NADP+ \rightleftharpoons coniferyl acetate + NADPH + H+ The enzyme acts in the reverse direction.

The enzyme has a molecular weight of 16.9kDa. The pH optimum is reported as 9.2. The enzyme activity is strictly dependent on Ca2+ and the pH optimum varies according to Ca2+ concentration. The enzyme is therefore easily inactivated by EGTA.

Arginase (, arginine amidinase, canavanase, L-arginase, arginine transamidinase) is a manganese-containing enzyme. The reaction catalyzed by this enzyme is: arginine + H2O → ornithine + urea. It is the final enzyme of the urea cycle. It is ubiquitous to all domains of life.

Tellurite methyltransferase (, TehB) is an enzyme with systematic name S-adenosyl-L-methionine:tellurite methyltransferase. This enzyme catalyses the following chemical reaction : S-adenosyl-L-methionine + tellurite \rightleftharpoons S-adenosyl-L-homocysteine + methanetelluronate The enzyme is involved in the detoxification of tellurite.

Methylated-thiol-coenzyme M methyltransferase (, mtsA (gene)) is an enzyme with systematic name methylated-thiol:coenzyme M methyltransferase. This enzyme catalyses the following chemical reaction: This enzyme involved in methanogenesis from methylated thiols, such as methanethiol, dimethyl sulfide, and 3-S-methylmercaptopropionate.

Fumonisin B1 esterase (, fumD (gene)) is an enzyme with a systematic name fumonisin B1 acylhydrolase. This enzyme catalyses the following chemical reaction : fumonisin B1 + 2 H2O \rightleftharpoons aminopentol + 2 propane-1,2,3-tricarboxylate The enzyme is involved in degradation of fumonisin B1.

Alpha-agarase (, agarase, agaraseA33) is an enzyme with systematic name agarose 3-glycanohydrolase. This enzyme catalyses the following chemical reaction : Endohydrolysis of (1->3)-alpha-L-galactosidic linkages in agarose, yielding agarotetraose as the major product This enzyme requires Ca2+.

D-Ala-D-Ala dipeptidase (, D-alanyl-D-alanine dipeptidase, vanX D-Ala-D-Ala dipeptidase, VanX) is an enzyme. This enzyme catalyses the following chemical reaction : D-Ala-D-Ala + H2O \rightleftharpoons 2 D-Ala This enzyme is Zn2+-dependent.

It is believed that these structures tether the -fixing enzyme, RuBisCO, to the interior of the shell, as well as the enzyme carbonic anhydrase, using metabolic channeling to enhance the local concentrations and thus increase the efficiency of the RuBisCO enzyme.

Alternatively, the enzyme can be sequestered near its substrate to activate the enzyme. For example, the enzyme can be soluble and upon activation bind to a lipid in the plasma membrane and then act upon molecules in the plasma membrane.

The systematic name of this enzyme class is acceptor:trichloroethene oxidoreductase (chlorinating). This enzyme is also called tetrachloroethene reductase. This enzyme participates in tetrachloroethene degradation. Note that the physiologically relevant reaction actually occurs in the reverse direction from that shown above.

Aqualysin 1 (, caldolysin) is an enzyme. This enzyme catalyses the following chemical reaction : Exhibits low specificity towards esters of amino acids with small hydrophobic or aromatic residues at the P1 position This enzyme is isolated from the thermophile, Thermus aquaticus.

Peptidyl-glycinamidase (, carboxyamidase, peptidyl carboxy-amidase, peptidyl- aminoacylamidase, carboxamidopeptidase, peptidyl amino acid amide hydrolase) is an enzyme. This enzyme catalyses the following chemical reaction : Cleavage of C-terminal glycinamide from polypeptides This enzyme inactivates vasopressin and oxytocin by splitting off glycinamide.

In enzymology, a 5'-acylphosphoadenosine hydrolase () is an enzyme that catalyzes the chemical reaction :5'-acylphosphoadenosine + H2O \rightleftharpoons AMP + a carboxylate Thus, the two substrates of this enzyme are 5'-acylphosphoadenosine and H2O, whereas its two products are AMP and carboxylate. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides in phosphorus-containing anhydrides. The systematic name of this enzyme class is 5'-acylphosphoadenosine acylhydrolase. This enzyme is also called 5-phosphoadenosine hydrolase.

In enzymology, an adenosine-tetraphosphatase () is an enzyme that catalyzes the chemical reaction :adenosine 5'-tetraphosphate + H2O \rightleftharpoons ATP + phosphate Thus, the two substrates of this enzyme are adenosine 5'-tetraphosphate and H2O, whereas its two products are ATP and phosphate. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides in phosphorus-containing anhydrides. The systematic name of this enzyme class is adenosine-tetraphosphate phosphohydrolase. This enzyme participates in purine metabolism.

In enzymology, an oleate hydratase () is an enzyme that catalyzes the chemical reaction :(R)-10-hydroxystearate \rightleftharpoons oleate + H2O Hence, this enzyme has one substrate, (R)-10-hydroxystearate, and two products, oleate and H2O. This enzyme belongs to the family of lyases, specifically the hydro- lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is (R)-10-hydroxystearate 10-hydro-lyase (oleate-forming). This enzyme is also called (R)-10-hydroxystearate 10-hydro-lyase.

In enzymology, a nucleoside-triphosphate diphosphatase () is an enzyme that catalyzes the chemical reaction :a nucleoside triphosphate + H2O \rightleftharpoons a nucleotide + diphosphate Thus, the two substrates of this enzyme are nucleoside triphosphate and H2O, whereas its two products are nucleotide and diphosphate. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides in phosphorus-containing anhydrides. The systematic name of this enzyme class is nucleoside- triphosphate diphosphohydrolase. This enzyme is also called nucleoside- triphosphate pyrophosphatase.

In enzymology, a (S)-methylmalonyl-CoA hydrolase () is an enzyme that catalyzes the chemical reaction :(S)-methylmalonyl-CoA + HO \rightleftharpoons methylmalonate + CoA Thus, the two substrates of this enzyme are (S)-methylmalonyl-CoA and HO, whereas its two products are methylmalonate and CoA. This enzyme belongs to the family of hydrolases, specifically those acting on thioester bonds. The systematic name of this enzyme class is (S)-methylmalonyl-CoA hydrolase. This enzyme is also called D-methylmalonyl- coenzyme A hydrolase.

In enzymology, a sorbitol-6-phosphatase () is an enzyme that catalyzes the chemical reaction :sorbitol 6-phosphate + H2O \rightleftharpoons sorbitol + phosphate Thus, the two substrates of this enzyme are sorbitol 6-phosphate and H2O, whereas its two products are sorbitol and phosphate. This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name of this enzyme class is sorbitol-6-phosphate phosphohydrolase. This enzyme is also called sorbitol-6-phosphate phosphatase.

In enzymology, a glycosulfatase () is an enzyme that catalyzes the chemical reaction :D-glucose 6-sulfate + H2O \rightleftharpoons D-glucose + sulfate Thus, the two substrates of this enzyme are D-glucose 6-sulfate and H2O, whereas its two products are D-glucose and sulfate. This enzyme belongs to the family of hydrolases, specifically those acting on sulfuric ester bonds. The systematic name of this enzyme class is sugar-sulfate sulfohydrolase. This enzyme is also called glucosulfatase.

In enzymology, a L-arabinonolactonase () is an enzyme that catalyzes the chemical reaction :L-arabinono-1,4-lactone + H2O \rightleftharpoons L-arabinonate Thus, the two substrates of this enzyme are L-arabinono-1,4-lactone and H2O, whereas its product is L-arabinonate. This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is L-arabinono-1,4-lactone lactonohydrolase. This enzyme participates in ascorbate and aldarate metabolism.

In enzymology, a 4-hydroxybenzoyl-CoA thioesterase () is an enzyme that catalyzes the chemical reaction :4-hydroxybenzoyl-CoA + H2O \rightleftharpoons 4-hydroxybenzoate + CoA Thus, the two substrates of this enzyme are 4-hydroxybenzoyl-CoA and H2O, whereas its two products are 4-hydroxybenzoate and CoA. This enzyme belongs to the family of hydrolases, specifically those acting on thioester bonds. The systematic name of this enzyme class is 4-hydroxybenzoyl-CoA hydrolase. This enzyme participates in 2,4-dichlorobenzoate degradation.

In enzymology, a citramalate CoA-transferase () is an enzyme that catalyzes the chemical reaction :acetyl-CoA + citramalate \rightleftharpoons acetate + (3S)-citramalyl-CoA Thus, the two substrates of this enzyme are acetyl-CoA and citramalate, whereas its two products are acetate and (3S)-citramalyl-CoA. This enzyme belongs to the family of transferases, specifically the CoA- transferases. The systematic name of this enzyme class is acetyl- CoA:citramalate CoA-transferase. This enzyme participates in c5-branched dibasic acid metabolism.

In enzymology, a citrate CoA-transferase () is an enzyme that catalyzes the following chemical reaction: :acetyl-CoA + citrate \rightleftharpoons acetate + (3S)-citryl-CoA Thus, the two substrates of this enzyme are acetyl-CoA and citrate, whereas its two products are acetate and (3S)-citryl-CoA. This enzyme belongs to the family of transferases, specifically the CoA-transferases. The systematic name of this enzyme class is acetyl-CoA:citrate CoA-transferase. This enzyme participates in citrate cycle (tca cycle).

In enzymology, a phloretin hydrolase () is an enzyme that catalyzes the chemical reaction :phloretin + H2O \rightleftharpoons phloretate + phloroglucinol Thus, the two substrates of this enzyme are phloretin and H2O, whereas its two products are phloretate and phloroglucinol. This enzyme belongs to the family of hydrolases, specifically those acting on carbon–carbon bonds in ketonic substances. The systematic name of this enzyme class is 2',4,4',6'-tetrahydroxydehydrochalcone 1,3,5-trihydroxybenzenehydrolase. This enzyme is also called lactase-phlorizin hydrolase.

In enzymology, a 4-chlorobenzoate dehalogenase () is an enzyme that catalyzes the chemical reaction :4-chlorobenzoate + H2O \rightleftharpoons 4-hydroxybenzoate + chloride Thus, the two substrates of this enzyme are 4-chlorobenzoate and H2O, whereas its two products are 4-hydroxybenzoate and chloride. This enzyme belongs to the family of hydrolases, specifically those acting on halide bonds in carbon-halide compounds. The systematic name of this enzyme class is 4-chlorobenzoate chlorohydrolase. This enzyme is also called halobenzoate dehalogenase.

In enzymology, an acylpyruvate hydrolase () is an enzyme that catalyzes the chemical reaction :a 3-acylpyruvate + H2O \rightleftharpoons a carboxylate + pyruvate Thus, the two substrates of this enzyme are 3-acylpyruvate and water, whereas its two products are carboxylate and pyruvate. This enzyme belongs to the family of hydrolases, specifically those acting on carbon-carbon bonds in ketonic substances. The systematic name of this enzyme class is 3-acylpyruvate acylhydrolase. This enzyme participates in tyrosine metabolism.

In enzymology, a 3,4-dihydroxyphthalate decarboxylase () is an enzyme that catalyzes the chemical reaction :3,4-dihydroxyphthalate \rightleftharpoons 3,4-dihydroxybenzoate + CO2 Hence, this enzyme has one substrate, 3,4-dihydroxyphthalate, and two products, 3,4-dihydroxybenzoate and CO2. This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is 3,4-dihydroxyphthalate carboxy-lyase (3,4-dihydroxybenzoate-forming). This enzyme is also called 3,4-dihydroxyphthalate carboxy-lyase.

In enzymology, a 4,5-dihydroxyphthalate decarboxylase () is an enzyme that catalyzes the chemical reaction :4,5-dihydroxyphthalate \rightleftharpoons 3,4-dihydroxybenzoate + CO2 Hence, this enzyme has one substrate, 4,5-dihydroxyphthalate, and two products, 3,4-dihydroxybenzoate and CO2. This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is 4,5-dihydroxyphthalate carboxy-lyase (3,4-dihydroxybenzoate-forming). This enzyme is also called 4,5-dihydroxyphthalate carboxy-lyase.

In enzymology, a 4-hydroxyphenylpyruvate decarboxylase () is an enzyme that catalyzes the chemical reaction :4-hydroxyphenylpyruvate \rightleftharpoons 4-hydroxyphenylacetaldehyde + CO2 Hence, this enzyme has one substrate, 4-hydroxyphenylpyruvate, and two products, 4-hydroxyphenylacetaldehyde and CO2. This enzyme belongs to the family of lyases, specifically the carboxy- lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is 4-hydroxyphenylpyruvate carboxy-lyase (4-hydroxyphenylacetaldehyde- forming). This enzyme is also called 4-hydroxyphenylpyruvate carboxy-lyase.

In enzymology, an orsellinate decarboxylase () is an enzyme that catalyzes the chemical reaction :2,4-dihydroxy-6-methylbenzoate \rightleftharpoons orcinol + CO2 Hence, this enzyme has one substrate, 2,4-dihydroxy-6-methylbenzoate, and two products, orcinol and CO2. This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is 2,4-dihydroxy-6-methylbenzoate carboxy-lyase (orcinol-forming). This enzyme is also called orsellinate carboxy-lyase.

In enzymology, a tartrate decarboxylase () is an enzyme that catalyzes the chemical reaction :(R,R)-tartrate \rightleftharpoons D-glycerate + CO2 Hence, this enzyme has one substrate, (R,R)-tartrate, and two products, D-glycerate and CO2. This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is (R,R)-tartrate carboxy-lyase (D-glycerate-forming). This enzyme is also called (R,R)-tartrate carboxy-lyase.

In enzymology, a 1-methyladenosine nucleosidase () is an enzyme that catalyzes the chemical reaction :1-methyladenosine + H2O \rightleftharpoons 1-methyladenine + D-ribose Thus, the two substrates of this enzyme are 1-methyladenosine and H2O, whereas its two products are 1-methyladenine and D-ribose. This enzyme belongs to the family of hydrolases, specifically those glycosylases that hydrolyse N-glycosyl compounds. The systematic name of this enzyme class is 1-methyladenosine ribohydrolase. This enzyme is also called 1-methyladenosine hydrolase.

In enzymology, an alpha,alpha-trehalase () is an enzyme with system name alpha,alpha-trehalose glucohydrolase. This enzyme catalyzes the chemical reaction :alpha,alpha-trehalose + H2O \rightleftharpoons 2 D-glucose Thus, the two substrates of this enzyme are alpha,alpha-trehalose and H2O, whereas its product is D-glucose. This enzyme belongs to the family of hydrolases, specifically those glycosidases that hydrolyse O- and S-glycosyl compounds. The systematic name of this enzyme class is alpha,alpha-trehalose glucohydrolase.

In enzymology, a coniferin beta-glucosidase () is an enzyme that catalyzes the chemical reaction :coniferin + H2O \rightleftharpoons D-glucose + coniferol Thus, the two substrates of this enzyme are coniferin and H2O, whereas its two products are D-glucose and coniferol. This enzyme belongs to the family of hydrolases, specifically those glycosidases that hydrolyse O- and S-glycosyl compounds. The systematic name of this enzyme class is coniferin beta-D- glucosidase. This enzyme is also called coniferin-hydrolyzing beta- glucosidase.

In enzymology, an inosinate nucleosidase () is an enzyme that catalyzes the chemical reaction :5'-inosinate + H2O \rightleftharpoons D-ribose 5-phosphate + hypoxanthine Thus, the two substrates of this enzyme are 5'-inosinate and H2O, whereas its two products are D-ribose 5-phosphate and hypoxanthine. This enzyme belongs to the family of hydrolases, specifically those glycosylases that hydrolyse N-glycosyl compounds. The systematic name of this enzyme class is 5'-inosinate phosphoribohydrolase. This enzyme participates in purine metabolism.

In enzymology, a prunasin beta-glucosidase () is an enzyme that catalyzes the chemical reaction :(R)-prunasin + H2O \rightleftharpoons D-glucose + mandelonitrile Thus, the two substrates of this enzyme are (R)-prunasin and H2O, whereas its two products are D-glucose and mandelonitrile. This enzyme belongs to the family of hydrolases, specifically those glycosidases that hydrolyse O- and S-glycosyl compounds. The systematic name of this enzyme class is prunasin beta-D-glucohydrolase. This enzyme is also called prunasin hydrolase.

In enzymology, an urethanase () is an enzyme that catalyzes the chemical reaction :urethane + H2O \rightleftharpoons ethanol + CO2 \+ NH3 Thus, the two substrates of this enzyme are urethane and H2O, whereas its 3 products are ethanol, CO2, and NH3. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is urethane amidohydrolase (decarboxylating). This enzyme is also called urethane hydrolase.

In enzymology, an arylacetonitrilase () is an enzyme that catalyzes the chemical reaction :4-chlorophenylacetonitrile + 2 H2O \rightleftharpoons 4-chlorophenylacetate + NH3 Thus, the two substrates of this enzyme are 4-chlorophenylacetonitrile and H2O, whereas its two products are 4-chlorophenylacetate and NH3. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in nitriles. The systematic name of this enzyme class is arylacetonitrile aminohydrolase. This enzyme participates in cyanoamino acid metabolism.

In enzymology, an arylalkyl acylamidase () is an enzyme that catalyzes the chemical reaction :N-acetylarylalkylamine + H2O \rightleftharpoons arylalkylamine + acetate Thus, the two substrates of this enzyme are N-acetylarylalkylamine and H2O, whereas its two products are arylalkylamine and acetate. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N-acetylarylalkylamine amidohydrolase. This enzyme is also called aralkyl acylamidase.

In enzymology, an ATP deaminase () is an enzyme that catalyzes the chemical reaction :ATP + H2O \rightleftharpoons ITP + NH3 Thus, the two substrates of this enzyme are ATP and H2O, whereas its two products are ITP and NH3. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is ATP aminohydrolase. This enzyme is also called adenosine triphosphate deaminase.

In enzymology, an agmatine deiminase () is an enzyme that catalyzes the chemical reaction :agmatine + H2O \rightleftharpoons N-carbamoylputrescine + NH3 Thus, the two substrates of this enzyme are agmatine and H2O, whereas its two products are N-carbamoylputrescine and NH3. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amidines. The systematic name of this enzyme class is agmatine iminohydrolase. This enzyme is also called agmatine amidinohydrolase.

In enzymology, an allantoate deiminase () is an enzyme that catalyzes the chemical reaction :allantoate + H2O \rightleftharpoons ureidoglycine + NH3 \+ CO2 Thus, the two substrates of this enzyme are allantoate and H2O, whereas its 3 products are ureidoglycine, NH3, and CO2. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amidines. The systematic name of this enzyme class is allantoate amidinohydrolase (decarboxylating). This enzyme is also called allantoate amidohydrolase.

In enzymology, a chenodeoxycholoyltaurine hydrolase () is an enzyme that catalyzes the chemical reaction :chenodeoxycholoyltaurine + H2O \rightleftharpoons chenodeoxycholate + taurine Thus, the two substrates of this enzyme are chenodeoxycholoyltaurine and H2O, whereas its two products are chenodeoxycholate and taurine. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is chenodeoxycholoyltaurine amidohydrolase. This enzyme participates in bile acid biosynthesis.

In enzymology, a cyanuric acid amidohydrolase () is an enzyme that catalyzes the chemical reaction :cyanuric acid + H2O \rightleftharpoons biuret + CO2 Thus, the two substrates of this enzyme are cyanuric acid and H2O, whereas its two products are biuret and CO2. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amides. The systematic name of this enzyme class is cyanuric acid amidohydrolase. This enzyme participates in atrazine degradation.

In enzymology, a cytosine deaminase () is an enzyme that catalyzes the chemical reaction :cytosine + H2O \rightleftharpoons uracil + NH3 Thus, the two substrates of this enzyme are cytosine and H2O, whereas its two products are uracil and NH3. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is cytosine aminohydrolase. This enzyme is also called isocytosine deaminase.

In enzymology, a quercitrinase () is an enzyme that catalyzes the chemical reaction :quercitrin + H2O \rightleftharpoons L-rhamnose + quercetin Thus, the two substrates of this enzyme are quercitrin and H2O, whereas its two products are L-rhamnose and quercetin. This enzyme belongs to the family of hydrolases, specifically those glycosidases that hydrolyse O- and S-glycosyl compounds. The systematic name of this enzyme class is quercitrin 3-L-rhamnohydrolase. The enzyme can be found in Aspergillus flavus.

In enzymology, a deoxycytidine deaminase () is an enzyme that catalyzes the chemical reaction :deoxycytidine + H2O \rightleftharpoons deoxyuridine + NH3 Thus, the two substrates of this enzyme are deoxycytidine and H2O, whereas its two products are deoxyuridine and NH3. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is cytidine/2'-deoxycytidine aminohydrolase. This enzyme participates in pyrimidine metabolism.

In enzymology, a formamidase () is an enzyme that catalyzes the chemical reaction :formamide + H2O \rightleftharpoons formate + NH3 Thus, the two substrates of this enzyme are formamide and H2O, whereas its two products are formate and NH3. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is formamide amidohydrolase. This enzyme participates in glyoxylate and dicarboxylate metabolism and nitrogen metabolism.

In enzymology, a guanosine deaminase () is an enzyme that catalyzes the chemical reaction :guanosine + H2O \rightleftharpoons xanthosine + NH3 Thus, the two substrates of this enzyme are guanosine and H2O, whereas its two products are xanthosine and NH3. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is guanosine aminohydrolase. This enzyme is also called guanosine aminase.

In enzymology, a hippurate hydrolase () is an enzyme that catalyzes the chemical reaction :hippurate + H2O \rightleftharpoons benzoate + glycine Thus, the two substrates of this enzyme are hippurate and H2O, whereas its two products are benzoate and glycine. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N-benzoylamino-acid amidohydrolase. This enzyme participates in phenylalanine metabolism.

In enzymology, a vicianin beta-glucosidase () is an enzyme that catalyzes the chemical reaction :(R)-vicianin + H2O \rightleftharpoons mandelonitrile + vicianose Thus, the two substrates of this enzyme are (R)-vicianin and H2O, whereas its two products are mandelonitrile and vicianose. This enzyme belongs to the family of hydrolases, specifically those glycosidases that hydrolyse O- and S-glycosyl compounds. The systematic name of this enzyme class is (R)-vicianin beta-D-glucohydrolase. This enzyme is also called vicianin hydrolase.

3alpha(S)-strictosidine beta-glucosidase () is an enzyme with systematic name strictosidine beta-D-glucohydrolase. This enzyme catalyses the following chemical reaction : strictosidine + H2O \rightleftharpoons D-glucose + strictosidine aglycone Thus, the two substrates of this enzyme are strictosidine and H2O, whereas its two products are D-glucose and strictosidine aglycone. This enzyme belongs to the family of hydrolases, specifically those glycosidases that hydrolyse O- and S-glycosyl compounds. This enzyme participates in indole and ipecac alkaloid biosynthesis.

In enzymology, a trimethylsulfonium-tetrahydrofolate N-methyltransferase () is an enzyme that catalyzes the chemical reaction :trimethylsulfonium + tetrahydrofolate \rightleftharpoons dimethylsulfide + 5-methyltetrahydrofolate Thus, the two substrates of this enzyme are trimethylsulfonium and tetrahydrofolate, whereas its two products are dimethyl sulfide and 5-methyltetrahydrofolate. This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is trimethylsulfonium:tetrahydrofolate N-methyltransferase. This enzyme is also called trimethylsulfonium- tetrahydrofolate methyltransferase.

In enzymology, an aspartate-phenylpyruvate transaminase () is an enzyme that catalyzes the chemical reaction :L-aspartate + phenylpyruvate \rightleftharpoons oxaloacetate + L-phenylalanine Thus, the two substrates of this enzyme are L-aspartate and phenylpyruvate, whereas its two products are oxaloacetate and L-phenylalanine. This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-aspartate:phenylpyruvate aminotransferase. This enzyme is also called aspartate-phenylpyruvate aminotransferase.

In enzymology, a lavandulyl diphosphate synthase () is an enzyme that catalyzes the chemical reaction :2 dimethylallyl diphosphate \rightleftharpoons diphosphate + lavandulyl diphosphate Hence, this enzyme has one substrate, dimethylallyl diphosphate, and two products, diphosphate and lavandulyl diphosphate. This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is dimethylallyl- diphosphate:dimethylallyl-diphosphate dimethylallyltransferase (lavandulyl- diphosphate-forming). This enzyme is also called FDS-5.

In enzymology, a serine-glyoxylate transaminase () is an enzyme that catalyzes the chemical reaction :L-serine + glyoxylate \rightleftharpoons 3-hydroxypyruvate + glycine Thus, the two substrates of this enzyme are L-serine and glyoxylate, whereas its two products are 3-hydroxypyruvate and glycine. This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-serine:glyoxylate aminotransferase. This enzyme participates in glycine, serine and threonine metabolism.

In enzymology, a galactarate O-hydroxycinnamoyltransferase () is an enzyme that catalyzes the chemical reaction :feruloyl-CoA + galactarate \rightleftharpoons CoA + O-feruloylgalactarate Thus, the two substrates of this enzyme are feruloyl-CoA and galactarate, whereas its two products are CoA and O-feruloylgalactarate. This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is feruloyl-CoA:galactarate O-(hydroxycinnamoyl)transferase. This enzyme is also called galacturate hydroxycinnamoyltransferase.

In enzymology, a dolichol O-acyltransferase () is an enzyme that catalyzes the chemical reaction :palmitoyl-CoA + dolichol \rightleftharpoons CoA + dolichyl palmitate Thus, the two substrates of this enzyme are palmitoyl-CoA and dolichol, whereas its two products are CoA and dolichyl palmitate. This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is palmitoyl-CoA:dolichol O-palmitoyltransferase. This enzyme is also called acyl-CoA:dolichol acyltransferase.

In enzymology, a glutathione oxidase () is an enzyme that catalyzes the chemical reaction :2 glutathione + O2 \rightleftharpoons glutathione disulfide + H2O2 Thus, the two substrates of this enzyme are glutathione and O2, whereas its two products are glutathione disulfide and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with oxygen as acceptor. The systematic name of this enzyme class is glutathione:oxygen oxidoreductase. This enzyme participates in glutathione metabolism.

In enzymology, a cyclohexylamine oxidase () is an enzyme that catalyzes the chemical reaction :cyclohexylamine + O2 \+ H2O \rightleftharpoons cyclohexanone + NH3 \+ H2O2 The 3 substrates of this enzyme are cyclohexylamine, O2, and H2O, whereas its 3 products are cyclohexanone, NH3, and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with oxygen as acceptor. The systematic name of this enzyme class is cyclohexylamine:oxygen oxidoreductase (deaminating). This enzyme participates in caprolactam degradation.

In enzymology, a glyoxylate oxidase () is an enzyme that catalyzes the chemical reaction :glyoxylate + H2O + O2 \rightleftharpoons oxalate + H2O2 The 3 substrates of this enzyme are glyoxylate, H2O, and O2, whereas its two products are oxalate and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with oxygen as acceptor. The systematic name of this enzyme class is glyoxylate:oxygen oxidoreductase. This enzyme participates in glyoxylate and dicarboxylate metabolism.

In enzymology, a pyridoxal oxidase () is an enzyme that catalyzes the chemical reaction :pyridoxal + H2O + O2 \rightleftharpoons 4-pyridoxate + (?) The 3 substrates of this enzyme are pyridoxal, H2O, and O2, whereas its product is 4-pyridoxate. This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with oxygen as acceptor. The systematic name of this enzyme class is pyridoxal:oxygen 4-oxidoreductase. This enzyme participates in vitamin B6 metabolism.

Arsenate reductase (donor) () is an enzyme that catalyzes the chemical reaction :arsenite + acceptor \rightleftharpoons arsenate + reduced acceptor Thus, the two substrates of this enzyme are arsenite and an acceptor, whereas its two products are arsenate and a reduced acceptor. This enzyme belongs to the family of oxidoreductases, specifically those acting on phosphorus or arsenic in donor with other acceptors. The systematic name of this enzyme class is arsenate:acceptor oxidoreductase. This enzyme is also called arsenate:(acceptor) oxidoreductase.

In enzymology, an amino-acid racemase () is an enzyme that catalyzes the chemical reaction :an L-amino acid \rightleftharpoons a D-amino acid Hence, this enzyme has one substrate, L-amino acid, and one product, D-amino acid. This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on amino acids and derivatives. The systematic name of this enzyme class is amino-acid racemase. This enzyme is also called L-amino acid racemase.

In enzymology, a linoleate isomerase () is an enzyme that catalyzes the chemical reaction :9-cis,12-cis-octadecadienoate \rightleftharpoons 9-cis,11-trans-octadecadienoate Hence, this enzyme has one substrate, 9-cis,12-cis-octadecadienoate, and one product, 9-cis,11-trans- octadecadienoate. This enzyme belongs to the family of isomerases, specifically cis-trans isomerases. The systematic name of this enzyme class is linoleate Delta12-cis-Delta11-trans-isomerase. This enzyme is also called linoleic acid isomerase.

In enzymology, a galactose-6-phosphate isomerase () is an enzyme that catalyzes the chemical reaction :D-galactose 6-phosphate \rightleftharpoons D-tagatose 6-phosphate Hence, this enzyme has one substrate, D-galactose 6-phosphate, and one product, D-tagatose 6-phosphate. This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases interconverting aldoses and ketoses. The systematic name of this enzyme class is D-galactose-6-phosphate aldose-ketose-isomerase. This enzyme participates in galactose metabolism.

In enzymology, a glutamate-1-semialdehyde 2,1-aminomutase () is an enzyme that catalyzes the chemical reaction :L-glutamate 1-semialdehyde \rightleftharpoons 5-aminolevulinate Hence, this enzyme has one substrate, L-glutamate-1-semialdehyde, and one product, 5-aminolevulinate. This enzyme belongs to the family of isomerases, specifically those intramolecular transferases transferring amino groups. The systematic name of this enzyme class is (S)-4-amino-5-oxopentanoate 4,5-aminomutase. This enzyme is also called glutamate-1-semialdehyde aminotransferase.

In enzymology, a homocysteine S-methyltransferase () is an enzyme that catalyzes the chemical reaction :S-methylmethionine + L-homocysteine \rightleftharpoons 2 L-methionine Thus, the two substrates of this enzyme are S-methylmethionine and L-homocysteine, and it produces 2 molecules of L-methionine. This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:L-homocysteine S-methyltransferase. This enzyme participates in methionine metabolism.

In enzymology, a tyrosine 2,3-aminomutase () is an enzyme that catalyzes the chemical reaction :L-tyrosine \rightleftharpoons 3-amino-3-(4-hydroxyphenyl)propanoate Hence, this enzyme has one substrate, L-tyrosine, and one product, 3-amino-3-(4-hydroxyphenyl)propanoate. This enzyme belongs to the family of isomerases, specifically those intramolecular transferases transferring amino groups. The systematic name of this enzyme class is L-tyrosine 2,3-aminomutase. This enzyme is also called tyrosine alpha,beta-mutase.

In enzymology, a limonene-1,2-epoxide hydrolase () is an enzyme that catalyzes the chemical reaction :limonene-1,2-epoxide + H2O \rightleftharpoons limonene-1,2-diol Thus, the two substrates of this enzyme are limonene-1,2-epoxide and H2O, whereas its product is limonene-1,2-diol. This enzyme belongs to the family of hydrolases, specifically those acting on ether bonds (ether hydrolases). The systematic name of this enzyme class is limonene-1,2-epoxide hydrolase. This enzyme is also called limonene oxide hydrolase.

In enzymology, a nucleoside ribosyltransferase () is an enzyme that catalyzes the chemical reaction :D-ribosyl-base1 \+ base2 \rightleftharpoons D-ribosyl- base2 \+ base1 Thus, the two substrates of this enzyme are D-ribosyl-base1 and base2, whereas its two products are D-ribosyl-base2 and base1. This enzyme belongs to the family of glycosyltransferases, specifically the pentosyltransferases. The systematic name of this enzyme class is nucleoside:purine(pyrimidine) D-ribosyltransferase. This enzyme is also called nucleoside N-ribosyltransferase.

In enzymology, a kaempferol 3-O-galactosyltransferase () is an enzyme that catalyzes the chemical reaction :UDP-galactose + kaempferol \rightleftharpoons UDP + kaempferol 3-O-beta-D-galactoside Thus, the two substrates of this enzyme are UDP-galactose and kaempferol, whereas its two products are UDP and trifolin. This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-galactose:kaempferol 3-O-beta-D-galactosyltransferase. This enzyme is also called F3GalTase.

In enzymology, a maltose phosphorylase () is an enzyme that catalyzes the chemical reaction :maltose + phosphate \rightleftharpoons D-glucose + beta-D- glucose 1-phosphate Thus, the two substrates of this enzyme are maltose and phosphate, whereas its two products are D-glucose and beta-D-glucose 1-phosphate. This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is maltose:phosphate 1-beta-D-glucosyltransferase. This enzyme participates in starch and sucrose metabolism.

In enzymology, a cyclohexanol dehydrogenase () is an enzyme that catalyzes the chemical reaction :cyclohexanol + NAD+ \rightleftharpoons cyclohexanone + NADH + H+ Thus, the two substrates of this enzyme are cyclohexanol and NAD+, whereas its 3 products are cyclohexanone, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is cyclohexanol:NAD+ oxidoreductase. This enzyme participates in caprolactam degradation.

In enzymology, an acetate kinase (diphosphate) () is an enzyme that catalyzes the chemical reaction :diphosphate + acetate \rightleftharpoons phosphate + acetyl phosphate Thus, the two substrates of this enzyme are diphosphate and acetate, whereas its two products are phosphate and acetyl phosphate. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a carboxy group as acceptor. The systematic name of this enzyme class is diphosphate:acetate phosphotransferase. This enzyme is also called pyrophosphate-acetate phosphotransferase.

In enzymology, a phosphatidylcholine synthase () is an enzyme that catalyzes the chemical reaction :CDP-diacylglycerol + choline \rightleftharpoons CMP + phosphatidylcholine Thus, the two substrates of this enzyme are CDP- diacylglycerol and choline, whereas its two products are CMP and phosphatidylcholine. This enzyme belongs to the family of transferases, specifically those transferring non-standard substituted phosphate groups. The systematic name of this enzyme class is CDP-diacylglycerol:choline O-phosphatidyltransferase. This enzyme is also called CDP-diglyceride-choline O-phosphatidyltransferase.

In enzymology, a formate kinase () is an enzyme that catalyzes the chemical reaction :ATP + formate \rightleftharpoons ADP + formyl phosphate Thus, the two substrates of this enzyme are ATP and formate, whereas its two products are ADP and formyl phosphate. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a carboxy group as acceptor. The systematic name of this enzyme class is ATP:formate phosphotransferase. This enzyme participates in glyoxylate and dicarboxylate metabolism.

In enzymology, a deoxyadenosine kinase () is an enzyme that catalyzes the chemical reaction :ATP + deoxyadenosine \rightleftharpoons ADP + dAMP Thus, the two substrates of this enzyme are ATP and deoxyadenosine, whereas its two products are ADP and dAMP. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:deoxyadenosine 5'-phosphotransferase. This enzyme is also called purine-deoxyribonucleoside kinase.

In enzymology, a (deoxy)adenylate kinase () is an enzyme that catalyzes the chemical reaction :ATP + dAMP \rightleftharpoons ADP + dADP Thus, the two substrates of this enzyme are ATP and dAMP, whereas its two products are ADP and dADP. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. The systematic name of this enzyme class is ATP:(d)AMP phosphotransferase. This enzyme participates in purine metabolism.

In enzymology, a ceramide cholinephosphotransferase () is an enzyme that catalyzes the chemical reaction :CDP-choline + N-acylsphingosine \rightleftharpoons CMP + sphingomyelin Thus, the two substrates of this enzyme are CDP-choline and N-acylsphingosine, whereas its two products are CMP and sphingomyelin. This enzyme belongs to the family of transferases, specifically those transferring non-standard substituted phosphate groups. The systematic name of this enzyme class is CDP-choline:N-acylsphingosine cholinephosphotransferase. This enzyme is also called phosphorylcholine- ceramide transferase.

In enzymology, a lombricine kinase () is an enzyme that catalyzes the chemical reaction :ATP + lombricine \rightleftharpoons ADP + N-phospholombricine The two substrates of this enzyme are ATP and lombricine, and the two products are ADP and N-phospholombricine. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a nitrogenous group as acceptor. The systematic name of this enzyme class is ATP:lombricine N-phosphotransferase. This enzyme participates in glycine, serine and threonine metabolism.

In enzymology, a butyrate kinase () is an enzyme that catalyzes the chemical reaction :ADP + butyryl-phosphate \rightleftharpoons ATP + butyrate Thus, the two substrates of this enzyme are ADP and butyryl-phosphate, whereas its two products are ATP and butyrate. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a carboxy group as acceptor. The systematic name of this enzyme class is ATP:butanoate 1-phosphotransferase. This enzyme participates in butyrate metabolism.

In enzymology, a cellobiose phosphorylase () is an enzyme that catalyzes the chemical reaction :cellobiose + phosphate \rightleftharpoons alpha-D-glucose 1-phosphate + D-glucose Thus, the two substrates of this enzyme are cellobiose and phosphate, whereas its two products are alpha-D-glucose 1-phosphate and D-glucose. This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is cellobiose:phosphate alpha-D-glucosyltransferase. This enzyme participates in starch and sucrose metabolism.

In enzymology, an alginate synthase () is an enzyme that catalyzes the chemical reaction :GDP-D-mannuronate + (alginate)n \rightleftharpoons GDP + (alginate)n+1 Thus, the two substrates of this enzyme are GDP-D-mannuronate and (alginate)n, whereas its two products are GDP and (alginate)n+1. This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is GDP-D- mannuronate:alginate D-mannuronyltransferase. This enzyme is also called mannuronosyl transferase.

Temperature, salt concentration and the ratio of enzyme to DNA greatly affect enzyme activity, requiring reaction conditions to be tailored to specific applications.

There are 2 tissue-specific isozymes: a housekeeping enzyme encoded by the ALAS1 gene and an erythroid tissue-specific enzyme encoded by ALAS2.

Irinotecan is converted by an enzyme into its active metabolite SN-38, which is in turn inactivated by the enzyme UGT1A1 by glucuronidation.

The systematic name of this enzyme class is (6S)-6-hydroxyhyoscyamine,2-oxoglutarate oxidoreductase (epoxide-forming). This enzyme is also called hydroxyhyoscyamine dioxygenase.

This enzyme participates in alkaloid biosynthesis ii. This enzyme is important in the synthesis of many plant alkaloids. It evolved from spermidine synthase.

This enzyme is also called 2-halobenzoate 1,2-dioxygenase. This enzyme participates in benzoate degradation via coa ligation. It employs one cofactor, iron.

This enzyme participates in biosynthesis of steroids. It employs one cofactor, FAD. At least one compound, Dicumarol is known to inhibit this enzyme.

This would help speed up the overall rate since it yields the same results as adding an enzyme but without necessitating enzyme use.

Thyrotropin releasing hormone degrading enzyme is a protein, specifically a pyroglutamyl-peptidase II enzyme, that in humans is encoded by the TRHDE gene.

In enzymology, an alkylglycerophosphoethanolamine phosphodiesterase () is an enzyme that catalyzes the chemical reaction :1-alkyl-sn- glycero-3-phosphoethanolamine + H2O \rightleftharpoons 1-alkyl-sn-glycerol 3-phosphate + ethanolamine Thus, the two substrates of this enzyme are 1-alkyl-sn-glycero-3-phosphoethanolamine and H2O, whereas its two products are 1-alkyl-sn-glycerol 3-phosphate and ethanolamine. This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric diester bonds. The systematic name of this enzyme class is 1-alkyl-sn- glycero-3-phosphoethanolamine ethanolaminehydrolase. This enzyme is also called lysophospholipase D. This enzyme participates in ether lipid metabolism.

In enzymology, a reticuline oxidase () is an enzyme that catalyzes the chemical reaction :(S)-reticuline + O2 \rightleftharpoons (S)-scoulerine + H2O2 Thus, the two substrates of this enzyme are (S)-reticuline and O2, whereas its two products are (S)-scoulerine and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on X-H and Y-H to form an X-Y bond with oxygen as acceptor. The systematic name of this enzyme class is (S)-reticuline:oxygen oxidoreductase (methylene-bridge-forming). Other names in common use include BBE, berberine bridge enzyme, berberine- bridge-forming enzyme, and tetrahydroprotoberberine synthase.

In enzymology, a glycine dehydrogenase (cytochrome) () is an enzyme that catalyzes the chemical reaction :glycine + H2O + 2 ferricytochrome c \rightleftharpoons glyoxylate + NH3 \+ 2 ferrocytochrome c + 2 H+ The 3 substrates of this enzyme are glycine, H2O, and ferricytochrome c, whereas its 4 products are glyoxylate, NH3, ferrocytochrome c, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with a cytochrome as acceptor. The systematic name of this enzyme class is glycine:ferricytochrome-c oxidoreductase (deaminating). This enzyme is also called glycine---cytochrome c reductase. This enzyme participates in glycine, serine and threonine metabolism.

In enzymology, a 1,2-dehydroreticulinium reductase (NADPH) () is an enzyme that catalyzes the chemical reaction :(R)-reticuline + NADP \rightleftharpoons 1,2-dehydroreticulinium + NADPH + H Thus, the two substrates of this enzyme are (R)-reticuline and NADP, whereas its 3 products are 1,2-dehydroreticulinium, NADPH, and H. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (R)-reticuline:NADP+ oxidoreductase. This enzyme is also called 1,2-dehydroreticulinium ion reductase. This enzyme participates in alkaloid biosynthesis i.

In enzymology, a 4-hydroxybenzaldehyde dehydrogenase () is an enzyme that catalyzes the chemical reaction :4-hydroxybenzaldehyde + NAD+ \+ H2O \rightleftharpoons 4-hydroxybenzoate + NADH + 2 H+ The 3 substrates of this enzyme are 4-hydroxybenzaldehyde, NAD+, and H2O, whereas its 3 products are 4-hydroxybenzoate, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 3-hydroxybenzaldehyde:NAD+ oxidoreductase. This enzyme is also called p-hydroxybenzaldehyde dehydrogenase. This enzyme participates in toluene and xylene degradation in bacteria.

In enzymology, a 4-hydroxyphenylacetaldehyde dehydrogenase () is an enzyme that catalyzes the chemical reaction :4-hydroxyphenylacetaldehyde + NAD+ \+ H2O \rightleftharpoons 4-hydroxyphenylacetate + NADH + 2 H+ The 3 substrates of this enzyme are 4-hydroxyphenylacetaldehyde, NAD+, and H2O, whereas its 3 products are 4-hydroxyphenylacetate, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 4-hydroxyphenylacetaldehyde:NAD+ oxidoreductase. This enzyme is also called 4-HPAL dehydrogenase. This enzyme participates in tyrosine metabolism.

In enzymology, a methylenetetrahydrofolate dehydrogenase (NAD+) () is an enzyme that catalyzes the chemical reaction :5,10-methylenetetrahydrofolate + NAD+ \rightleftharpoons 5,10-methenyltetrahydrofolate + NADH + H+ Thus, the two substrates of this enzyme are 5,10-methylenetetrahydrofolate and NAD+, whereas its 3 products are 5,10-methenyltetrahydrofolate, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 5,10-methylenetetrahydrofolate:NAD+ oxidoreductase. This enzyme is also called methylenetetrahydrofolate dehydrogenase (NAD+). This enzyme participates in one carbon pool by folate.

In enzymology, a chloromuconate cycloisomerase () is an enzyme that catalyzes the chemical reaction :2-chloro-2,5-dihydro-5-oxofuran-2-acetate \rightleftharpoons 3-chloro-cis,cis-muconate Hence, this enzyme has one substrate, 2-chloro-2,5-dihydro-5-oxofuran-2-acetate, and one product, 3-chloro-cis,cis-muconate. This enzyme belongs to the family of isomerases, specifically the class of intramolecular lyases. The systematic name of this enzyme class is 2-chloro-2,5-dihydro-5-oxofuran-2-acetate lyase (decyclizing). This enzyme is also called muconate cycloisomerase II. This enzyme participates in gamma-hexachlorocyclohexane degradation and 1,4-dichlorobenzene degradation.

In enzymology, a 4-oxoproline reductase () is an enzyme that catalyzes the chemical reaction :4-hydroxy-L-proline + NAD+ \rightleftharpoons 4-oxoproline + NADH + H+ Thus, the two substrates of this enzyme are 4-hydroxy-L-proline and NAD+, whereas its 3 products are 4-oxoproline, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH- OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 4-hydroxy-L-proline:NAD+ oxidoreductase. This enzyme is also called hydroxy-L-proline oxidase. This enzyme participates in arginine and proline metabolism.

In enzymology, a hydroxyphenylpyruvate reductase () is an enzyme that catalyzes the chemical reaction :3-(4-hydroxyphenyl)lactate + NAD+ \rightleftharpoons 3-(4-hydroxyphenyl)pyruvate + NADH + H+ Thus, the two substrates of this enzyme are 3-(4-hydroxyphenyl)lactate and NAD+, whereas its 3 products are 3-(4-hydroxyphenyl)pyruvate, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 4-hydroxyphenyllactate:NAD+ oxidoreductase. This enzyme is also called HPRP. This enzyme participates in tyrosine metabolism and phenylalanine metabolism.

In enzymology, an indolelactate dehydrogenase () is an enzyme that catalyzes the chemical reaction :(indol-3-yl)lactate + NAD+ \rightleftharpoons (indol-3-yl)pyruvate + NADH + H+ Thus, the two substrates of this enzyme are (indol-3-yl)lactate and NAD+, whereas its 3 products are (indol-3-yl)pyruvate, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (indol-3-yl)lactate:NAD+ oxidoreductase. This enzyme is also called indolelactate:NAD+ oxidoreductase. This enzyme participates in tryptophan metabolism.

In enzymology, a mannitol 2-dehydrogenase (NADP+) () is an enzyme that catalyzes the chemical reaction :D-mannitol + NADP+ \rightleftharpoons D-fructose + NADPH + H+ Thus, the two substrates of this enzyme are D-mannitol and NADP+, whereas its 3 products are D-fructose, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH- OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is D-mannitol:NADP+ 2-oxidoreductase. This enzyme is also called mannitol 2-dehydrogenase (NADP+). This enzyme participates in fructose and mannose metabolism.

In enzymology, a (+)-trans-carveol dehydrogenase () is an enzyme that catalyzes the chemical reaction :(+)-trans-carveol + NAD \rightleftharpoons (+)-(S)-carvone + NADH + H Thus, the two substrates of this enzyme are (+)-trans-carveol and NAD, whereas its 3 products are (+)-(S)-carvone, NADH, and H. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD or NADP as acceptor. The systematic name of this enzyme class is (+)-trans-carveol:NAD oxidoreductase. This enzyme is also called carveol dehydrogenase. This enzyme participates in monoterpenoid biosynthesis and the degradation of the terpenes limonene and pinene.

In enzymology, a 4-hydroxybutyrate dehydrogenase () is an enzyme that catalyzes the chemical reaction :4-hydroxybutanoate + NAD+ \rightleftharpoons succinate semialdehyde + NADH + H+ The two substrates of this enzyme are therefore 4-hydroxybutanoic acid, and NAD+, whereas its 3 products are succinate semialdehyde, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 4-hydroxybutanoate:NAD+ oxidoreductase. This enzyme is also called gamma- hydroxybutyrate dehydrogenase. This enzyme participates in butanoate metabolism and the degradation of the neurotransmitter 4-hydroxybutanoic acid.

In enzymology, a 3-dehydroquinate dehydratase () is an enzyme that catalyzes the chemical reaction :3-dehydroquinate \rightleftharpoons 3-dehydroshikimate + H2O Hence, this enzyme has one substrate, 3-dehydroquinate, and two products, 3-dehydroshikimate and H2O. This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. This enzyme participates in phenylalanine, tyrosine and tryptophan biosynthesis.

In enzymology, a phosphoserine phosphatase () is an enzyme that catalyzes the following chemical reaction: :O-phospho-L(or D)-serine + H2O \rightleftharpoons L(or D)-serine + phosphate ion This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name of this enzyme class is O-phosphoserine phosphohydrolase. This enzyme participates in glycine, serine and threonine metabolism.

In enzymology, an actinomycin lactonase () is an enzyme that catalyzes the chemical reaction :actinomycin + H2O \rightleftharpoons actinomycinic monolactone Thus, the two substrates of this enzyme are actinomycin and H2O, whereas its product is actinomycinic monolactone. This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is actinomycin lactonohydrolase.

Upon binding to an enzyme substrate (ES) complex, an enzyme substrate inhibitor (ESI) complex is formed. Similar to competitive inhibitors, the rate at product formation is decreased also. Lastly, mixed inhibitors are able to bind to both the free enzyme and the enzyme-substrate complex. However, in contrast to competitive and uncompetitive inhibitors, mixed inhibitors bind to the allosteric site.

Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase, mitochondrial is an enzyme that in humans is encoded by the MTHFD2 gene. This gene encodes a nuclear-encoded mitochondrial bifunctional enzyme with methylenetetrahydrofolate dehydrogenase and methenyltetrahydrofolate cyclohydrolase activities. The enzyme functions as a homodimer and is unique in its absolute requirement for magnesium and inorganic phosphate. Formation of the enzyme-magnesium complex allows binding of NAD.

In enzymology, a 16-hydroxysteroid epimerase () is an enzyme that catalyzes the chemical reaction :16alpha-hydroxysteroid \rightleftharpoons 16beta- hydroxysteroid Hence, this enzyme has one substrate, 16alpha-hydroxysteroid, and one product, 16beta-hydroxysteroid. This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on other compounds. The systematic name of this enzyme class is 16-hydroxysteroid 16-epimerase.

In enzymology, an UDP-glucosamine 4-epimerase () is an enzyme that catalyzes the chemical reaction :UDP-glucosamine \rightleftharpoons UDP-galactosamine Hence, this enzyme has one substrate, UDP-glucosamine, and one product, UDP- galactosamine. This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on carbohydrates and derivatives. The systematic name of this enzyme class is UDP-glucosamine 4-epimerase.

In enzymology, a maltose epimerase () is an enzyme that catalyzes the chemical reaction :alpha-maltose \rightleftharpoons beta-maltose Hence, this enzyme has one substrate, alpha-maltose, and one product, beta-maltose. This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on carbohydrates and derivatives. The systematic name of this enzyme class is maltose 1-epimerase.

The enzyme is glycosylated. Different cell types contribute to the differences in the nature of the carbohydrate chain. A high mannose-type oligosaccharide is observed in the proenzyme in fibroblasts, however the mature enzyme can be seen with a complex-type oligosaccharide. In the membranes of erythrocytes, the mature enzyme and the pro-enzyme both have a complex-type oligosaccharide.

Enzyme Replacement Therapy has been used to treat Pompe disease. Since Pompe disease is caused by the deficiency of the enzyme acid alpha-glucosidase, the injection of the enzyme would alleviate the symptoms caused the disease. The functional enzyme is produced by genetically modified cells in the laboratory. It is then harvested, purified and eventually injected into the patient's body.

In enzymology, a tetrahydroxypteridine cycloisomerase () is an enzyme that catalyzes the chemical reaction :tetrahydroxypteridine \rightleftharpoons xanthine-8-carboxylate Hence, this enzyme has one substrate, tetrahydroxypteridine, and one product, xanthine-8-carboxylate. This enzyme belongs to the family of isomerases, specifically the class of intramolecular lyases. The systematic name of this enzyme class is tetrahydroxypteridine lyase (isomerizing). It employs one cofactor, NAD+.

In enzymology, a threonine racemase () is an enzyme that catalyzes the chemical reaction :L-threonine \rightleftharpoons D-threonine Hence, this enzyme has one substrate, L-threonine, and one product, D-threonine. This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on amino acids and derivatives. The systematic name of this enzyme class is threonine racemase.

Fumigaclavine B O-acetyltransferase (, FgaAT) is an enzyme with systematic name acetyl-CoA:fumigaclavine B O-acetyltransferase. This enzyme catalyses the following chemical reaction : acetyl-CoA + fumigaclavine B \rightleftharpoons CoA + fumigaclavine A The enzyme participates in the biosynthesis of fumigaclavine C, an ergot alkaloid.

2-oxoglutaramate amidase (, omega-amidase) is an enzyme with systematic name 5-amino-2,5-dioxopentanoate amidohydrolase. This enzyme catalyses the following chemical reaction : 2-oxoglutaramate + H2O \rightleftharpoons 2-oxoglutarate + ammonia The enzyme participates in the nicotine degradation pathway of several Gram-positive bacteria.

ADAMTS-4 endopeptidase (, aggrecanase-1) is an enzyme. This enzyme catalyses the following chemical reaction : Glutamyl endopeptidase; bonds cleaved include -Thr-Glu-Gly-Glu373-Ala-Arg-Gly-Ser- in the interglobular domain of mammalian aggrecan This enzyme belongs to the peptidase family M12.

2-Formylbenzoate dehydrogenase (, 2-carboxybenzaldehyde dehydrogenase, 2CBAL dehydrogenase, PhdK) is an enzyme with systematic name 2-formylbenzoate:NAD+ oxidoreductase. This enzyme catalyses the following chemical reaction : 2-formylbenzoate + NAD+ \+ H2O \rightleftharpoons o-phthalic acid + NADH + H+ The enzyme is involved in phenanthrene degradation.

Geranylgeranyl diphosphate reductase (, geranylgeranyl reductase, CHL P) is an enzyme with systematic name geranylgeranyl-diphosphate:NADP+ oxidoreductase. This enzyme catalises the following chemical reaction : phytyl diphosphate + 3 NADP+ \rightleftharpoons geranylgeranyl diphosphate + 3 NADPH + 3 H+ This enzyme also acts on geranylgeranyl-chlorophyll a.

This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D- amino-acid ligases (peptide syntheses). The systematic name of this enzyme class is (R)-4'-phosphopantothenate:L-cysteine ligase. This enzyme is also called phosphopantothenoylcysteine synthetase.

6-oxocamphor hydrolase (, OCH, camK (gene)) is an enzyme with systematic name bornane-2,6-dione hydrolase. This enzyme catalyses the following chemical reaction : bornane-2,6-dione + H2O \rightleftharpoons [(1S)-4-hydroxy-2,2,3-trimethylcyclopent-3-enyl]acetate This enzyme is isolated from Rhodococcus sp.

Valine dehydrogenase (NAD+) () is an enzyme with systematic name L-valine:NAD+ oxidoreductase (deaminating). This enzyme catalyses the following chemical reaction : L-valine + H2O + NAD+ \rightleftharpoons 3-methyl-2-oxobutanoate + NH3 \+ NADH + H+ The enzyme from Streptomyces spp. has no activity with NADP+.

FAD reductase (NADH) (, NADH-FAD reductase, NADH-dependent FAD reductase) is an enzyme with systematic name FADH2:NAD+ oxidoreductase. This enzyme catalyses the following chemical reaction : FADH2 \+ NAD+ \rightleftharpoons FAD + NADH + H+ The enzyme from Burkholderia phenoliruptrix has a preference for FAD.

Plant seed peroxygenase (, plant peroxygenase, soybean peroxygenase) is an enzyme with systematic name substrate:hydroperoxide oxidoreductase (RH- hydroxylating or epoxidising). This enzyme catalyses the following chemical reaction : R1H + R2OOH \rightleftharpoons R1OH + R2OH This enzyme is a heme protein that contains calcium binding motif.

This enzyme is involved in shikonin biosynthesis. It can be found in Lithospermum erythrorhizon. The enzyme 3-hydroxybenzoate—CoA ligase uses ATP, 3-hydroxybenzoate and CoA to produce AMP, diphosphate and 3-hydroxybenzoyl-CoA. The enzyme works equally well with 4-hydroxybenzoate.

4-hydroxybutanoyl-CoA dehydratase () is an enzyme with systematic name 4-hydroxybutanoyl-CoA hydro-lyase. This enzyme catalyses the following chemical reaction : 4-hydroxybutanoyl-CoA \rightleftharpoons but-3-enoyl-CoA + H2O This enzyme contains FAD and a [4Fe-4S] iron-sulfur cluster.

Viridiflorene synthase (, TPS31) is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate diphosphate-lyase (viridiflorene-forming). This enzyme catalyses the following chemical reaction : (2E,6E)-farnesyl diphosphate \rightleftharpoons viridiflorene + diphosphate Viridiflorene is the only product of this enzyme from Solanum lycopersicum.

Beta-selinene cyclase () is an enzyme with systematic name (2E,6E)-farnesyl- diphosphate diphosphate-lyase (beta-selinene-forming). This enzyme catalyses the following chemical reaction : (2E,6E)-farnesyl diphosphate \rightleftharpoons beta-selinene + diphosphate Initial cyclization gives (+)-germacrene A in an enzyme bound form.

Alpha-gurjunene synthase () is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate diphosphate-lyase ((-)-alpha-gurjunene-forming). This enzyme catalyses the following chemical reaction : (2E,6E)-farnesyl diphosphate \rightleftharpoons (-)-alpha-gurjunene + diphosphate Initial cyclization probably gives biyclogermacrene in an enzyme bound form.

Alpha-copaene synthase () is an enzyme with systematic name (2E,6E)-farnesyl- diphosphate diphosphate-lyase (cyclizing, alpha-copaene-forming). This enzyme catalyses the following chemical reaction : (2E,6E)-farnesyl diphosphate \rightleftharpoons (-)-alpha-copaene + diphosphate This enzyme is isolated from Helianthus annuus (sunflower).

Sesquithujene synthase (, TPS5-Del1) is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate diphosphate-lyase (sesquithujene-forming). This enzyme catalyses the following chemical reaction : (2E,6E)-farnesyl diphosphate \rightleftharpoons sesquithujene + diphosphate The enzyme from Zea mays, variety Delprim, gives mainly sesquithujene.

L-lysine cyclodeaminase (, rapL (gene), fkbL (gene), tubZ (gene), visC (gene)) is an enzyme with systematic name L-lysine ammonia-lyase (cyclizing; ammonia- forming). This enzyme catalyses the following chemical reaction : L-lysine \rightleftharpoons L-pipecolate + NH3 This enzyme requires bound NAD+.

Polyvinyl alcohol dehydrogenase (cytochrome) (, PVA dehydrogenase, PVADH) is an enzyme with systematic name polyvinyl alcohol:ferricytochrome-c oxidoreductase. This enzyme catalyses the following chemical reaction : polyvinyl alcohol + ferricytochrome c \rightleftharpoons oxidized polyvinyl alcohol + ferrocytochrome c + H+ This enzyme participates in bacterial polyvinyl alcohol degradation.

Glutinol synthase () is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualene mutase (cyclizing, glutinol-forming). This enzyme catalyses the following chemical reaction : (3S)-2,3-epoxy-2,3-dihydrosqualene \rightleftharpoons glutinol The enzyme from Kalanchoe daigremontiana also gives traces of other triterpenoids.

Friedelin synthase () is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualene mutase (cyclizing, friedelin-forming). This enzyme catalyses the following chemical reaction : (3S)-2,3-epoxy-2,3-dihydrosqualene \rightleftharpoons friedelin The enzyme from Kalanchoe daigremontiana also gives traces of other triterpenoids.

Methylornithine synthase (, PylB) is an enzyme with systematic name L-lysine carboxy-aminomethylmutase. This enzyme catalyses the conversion of L-lysine into (3R)-3-methyl-D-ornithine. The enzyme is a member of the superfamily of S-adenosyl-L-methionine-dependent radical enzymes.

Alcohol dehydrogenase (azurin) (, type II quinoprotein alcohol dehydrogenase, quinohaemoprotein ethanol dehydrogenase, QHEDH, ADHIIB) is an enzyme with systematic name alcohol:azurin oxidoreductase. This enzyme catalyses the following chemical reaction : primary alcohol + azurin \rightleftharpoons aldehyde + reduced azurin This enzyme is a periplasmic PQQ-containing quinohemoprotein.

Heme ligase (, heme detoxification protein, HDP, hemozoin synthase) is an enzyme with systematic name Fe3+:ferriprotoporphyrin IX ligase (beta-hematin- forming). This enzyme catalyses the following chemical reaction : 2 ferriprotoporphyrin IX \rightleftharpoons beta-hematin This heme detoxifying enzyme is found in Plasmodium parasites.

23S rRNA pseudouridine2604 synthase (, RluF, YjbC) is an enzyme with systematic name 23S rRNA-uridine2604 uracil mutase. This enzyme catalyses the following chemical reaction : 23S rRNA uridine2604 \rightleftharpoons 23S rRNA pseudouridine2604 The enzyme can, to a small extent, also react with uridine2605.

Catechol 2,3-dioxygenase (, 2,3-pyrocatechase, catechol 2,3-oxygenase, catechol oxygenase, metapyrocatechase, pyrocatechol 2,3-dioxygenase) is an enzyme with systematic name catechol:oxygen 2,3-oxidoreductase (decyclizing). This enzyme catalyses the following chemical reaction : 200px : catechol + O2 \rightleftharpoons 2-hydroxymuconate semialdehyde This enzyme contains Fe(II).

Alcohol dehydrogenase (nicotinoprotein) (, NDMA-dependent alcohol dehydrogenase, nicotinoprotein alcohol dehydrogenase, np-ADH, ethanol:N,N-dimethyl-4-nitrosoaniline oxidoreductase) is an enzyme with systematic name ethanol:acceptor oxidoreductase. This enzyme catalyses the following chemical reaction : ethanol + acceptor \rightleftharpoons acetaldehyde + reduced acceptor This enzyme contains Zn2+.

Methanol dehydrogenase (nicotinoprotein) (, NDMA-dependent methanol dehydrogenase, nicotinoprotein methanol dehydrogenase, methanol:N,N-dimethyl-4-nitrosoaniline oxidoreductase) is an enzyme with systematic name methanol:acceptor oxidoreductase. This enzyme catalyses the following chemical reaction : methanol + acceptor \rightleftharpoons formaldehyde + reduced acceptor This enzyme contains Zn2+ and Mg2+.

Polymannuronate hydrolase (, polymannuronic acid polymerase) is an enzyme with systematic name poly(mannuronide) mannuronohydrolase. This enzyme catalyses the following chemical reaction : Endohydrolysis of the D-mannuronide linkages of polymannuronate This enzyme does not act on alginic acid, which is a copolymer of polymannuronate.

Non-stereospecific dipeptidase (, peptidyl-D-amino acid hydrolase, D-(or L-)aminoacyl-dipeptidase) is an enzyme. This enzyme catalyses the following chemical reaction : Hydrolysis of dipeptides containing either D- or L-amino acids or both This is a digestive enzyme of cephalopods.

These proteins include methionine aminopeptidase 2, an enzyme that occurs in humans and other mammals that does not use the corrin ring of B12, but binds cobalt directly. Another non-corrin cobalt enzyme is nitrile hydratase, an enzyme in bacteria that metabolizes nitriles.

This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L- methionine:(RS)-1-benzyl-1,2,3,4-tetrahydroisoquinoline N-methyltransferase. This enzyme is also called norreticuline N-methyltransferase.

SUMO-conjugating enzyme UBC9 is an enzyme that in humans is encoded by the UBE2I gene. It is also sometimes referred to as "ubiquitin conjugating enzyme E2I" or "ubiquitin carrier protein 9", even though these names do not accurately describe its function.

Farnesyl diphosphatase (, FPP phosphatase) is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate diphosphohydrolase. This enzyme catalyses the following chemical reaction : (2E,6E)-farnesyl diphosphate + H2O \rightleftharpoons (2E,6E)-farnesol + diphosphate The enzyme is involved in the biosynthesis of acyclic sesquiterpenoids.

Mechanism of NSAIs is a reversible binding process where NSAIs binds to the aromatase enzyme through non-covalent interactions . NSAIs do not destroy the enzyme like SAIs do. An interaction occurs with a heme group of cytochrome P450 in the aromatase enzyme .

The systematic name of this enzyme class is phosphoenolpyruvate:protein-L-histidine Npi-phosphotransferase. Other names in common use include phosphoenolpyruvate sugar phosphotransferase enzyme I, phosphopyruvate-protein factor phosphotransferase, phosphopyruvate-protein phosphotransferase, sugar-PEP phosphotransferase enzyme I, and phosphoenolpyruvate:protein-L-histidine N-pros-phosphotransferase.

Leukotriene-B(4) omega-hydroxylase 1 is an enzyme involved in the metabolism various endogenous substrates and xenobiotics. Most notable substrate of the enzyme is leukotriene B4, a potent mediator of inflammation. The enzyme is encoded by the CYP4F2 gene in humans.

However the gastric lipase activity against phospholipids and cholesterol esters is poor. Gastric lipase is composed of 379 amino acids. Fully glycosylated protein is 50kDa and unglycosylated enzyme is 43kDa. However deglycosylation of the enzyme does not affect the activity of the enzyme.

Gamma-renin () is an enzyme. This enzyme catalyses the following chemical reaction : Cleavage of the Leu-Leu bond in synthetic renin substrate (horse), to produce angiotensin I, but not active on natural angiotensinogen This enzyme is present in submandibular glands of male mice.

Metridin (, Metridium proteinase A, sea anemone protease A, sea anemone proteinase A) is an enzyme. This enzyme catalyses the following chemical reaction : Preferential cleavage: Tyr-, Phe-, Leu-; little action on Trp- This digestive enzyme is isolated from the sea anemone Metridium senile.

A similar five-subunit enzyme has been isolated from Methanolobus tindarius. The sulfate-reducing Archaeoglobus fulgidus (and several other archaea) also have this enzyme.

In the Biochemistry program, each team isolates and models an enzyme from a fungal crop pathogen, then designs a molecule to inhibit that enzyme.

A magnesium may be used to help the enzyme function, although the amount it helps the enzyme can vary between different classes of aldehydes.

This is followed by a second phosphoryl transfer from the substrate back to enzyme, producing product and regenerating the active form of the enzyme.

Some antimicrobial defensins also have enzyme inhibitory activity, and some DLPs function primarily as enzyme inhibitors, acting as antifeedants (discouraging animals from eating them).

This enzyme is also called hydroxyquinol dioxygenase. This enzyme participates in benzoate degradation via hydroxylation and 1,4-dichlorobenzene degradation. It employs one cofactor, iron.

The serine/threonine-protein kinase/endoribonuclease inositol-requiring enzyme 1 α (IRE1α) is an enzyme that in humans is encoded by the ERN1 gene.

This enzyme participates in 3 metabolic pathways: purine metabolism, selenoamino acid metabolism, and sulfur metabolism. This enzyme contains an ATP binding P-loop motif.

As of late 2007, the structure has only been solved for this enzyme. Part of the enzyme was crystallized with its activating partner frequenin.

In enzymology, a pentalenene synthase () is an enzyme that catalyzes the chemical reaction :2-trans,6-trans-farnesyl diphosphate \rightleftharpoons pentalenene + diphosphate Hence, this enzyme has one substrate, 2-trans,6-trans-farnesyl diphosphate, and two products, pentalenene and diphosphate. This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on phosphates. The systematic name of this enzyme class is 2-trans,6-trans-farnesyl-diphosphate diphosphate-lyase (cyclizing, pentalenene-forming). This enzyme is also called pentalenene synthetase.

In enzymology, a sabinene-hydrate synthase () is an enzyme that catalyzes the chemical reaction :geranyl diphosphate + H2O \rightleftharpoons sabinene hydrate + diphosphate Thus, the two substrates of this enzyme are geranyl diphosphate and H2O, whereas its two products are sabinene hydrate and diphosphate. This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on phosphates. The systematic name of this enzyme class is geranyl-diphosphate diphosphate-lyase (cyclizing, sabinene-hydrate- forming). This enzyme is also called sabinene hydrate cyclase.

In enzymology, a dimethylmaleate hydratase () is an enzyme that catalyzes the chemical reaction :(2R,3S)-2,3-dimethylmalate \rightleftharpoons dimethylmaleate + H2O Hence, this enzyme has one substrate, (2R,3S)-2,3-dimethylmalate, and two products, dimethylmaleate and H2O. This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is (2R,3S)-2,3-dimethylmalate hydro-lyase (dimethylmaleate-forming). This enzyme is also called (2R,3S)-2,3-dimethylmalate hydro-lyase.

In enzymology, a Hydroxyacylglutathione hydrolase () is an enzyme that catalyzes the chemical reaction :(R)-S-lactoylglutathione + water \rightleftharpoons glutathione + a 2-hydroxy carboxylate Hence, this enzyme has two substrates, (R)-S-lactoylglutathione and water, and two products, glutathione and a 2-hydroxy carboxylate. With the common substrate methylglyoxal, the product is D-lactate. This enzyme belongs to the family of hydrolases, specifically the class of thioester lyases. This enzyme is commonly known as glyoxalase II. This enzyme participates in pyruvate metabolism.

In enzymology, a molybdate-transporting ATPase () is an enzyme that catalyzes the chemical reaction :ATP + H2O + molybdateout \rightleftharpoons ADP + phosphate + molybdatein The 3 substrates of this enzyme are ATP, H2O, and molybdate, whereas its 3 products are ADP, phosphate, and molybdate. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (molybdate-importing). This enzyme participates in abc transporters - general.

In enzymology, a monosaccharide-transporting ATPase () is an enzyme that catalyzes the chemical reaction :ATP + H2O + monosaccharideout \rightleftharpoons ADP + phosphate + monosaccharidein The 3 substrates of this enzyme are ATP, H2O, and monosaccharide, whereas its 3 products are ADP, phosphate, and monosaccharide. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (monosaccharide-importing). This enzyme participates in abc transporters - general.

In enzymology, a maltose-transporting ATPase () is an enzyme that catalyzes the chemical reaction :ATP + H2O + maltoseout \rightleftharpoons ADP + phosphate + maltosein The 3 substrates of this enzyme are ATP, H2O, and maltose, whereas its 3 products are ADP, phosphate, and maltose. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (maltose-importing). This enzyme is a member of the ABC Transporter family.

In enzymology, a Fe3+-transporting ATPase () is an enzyme that catalyzes the chemical reaction :ATP + H2O + Fe3+out \rightleftharpoons ADP + phosphate + Fe3+in The 3 substrates of this enzyme are ATP, H2O, and Fe3+, whereas its 3 products are ADP, phosphate, and Fe3+. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (ferric-ion-transporting). This enzyme participates in abc transporters - general.

In enzymology, a heme-transporting ATPase () is an enzyme that catalyzes the chemical reaction :ATP + H2O + hemein \rightleftharpoons ADP + phosphate + hemeout The 3 substrates of this enzyme are ATP, H2O, and heme, whereas its 3 products are ADP, phosphate, and heme. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (heme-exporting). This enzyme participates in abc transporters - general.

In enzymology, an oligopeptide-transporting ATPase () is an enzyme that catalyzes the chemical reaction :ATP + H2O + oligopeptide(out) \rightleftharpoons ADP + phosphate + oligopeptide(in) The 3 substrates of this enzyme are ATP, H2O, and oligopeptide, whereas its 3 products are ADP, phosphate, and oligopeptide. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (oligopeptide-importing). This enzyme is also called oligopeptide permease.

In enzymology, an oligosaccharide-diphosphodolichol diphosphatase () is an enzyme that catalyzes the chemical reaction :oligosaccharide-diphosphodolichol + H2O \rightleftharpoons oligosaccharide phosphate + dolichyl phosphate Thus, the two substrates of this enzyme are oligosaccharide-diphosphodolichol and H2O, whereas its two products are oligosaccharide phosphate and dolichyl phosphate. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides in phosphorus-containing anhydrides. The systematic name of this enzyme class is oligosaccharide-diphosphodolichol phosphodolichohydrolase. This enzyme is also called oligosaccharide- diphosphodolichol pyrophosphatase.

In enzymology, a sulfate-transporting ATPase () is an enzyme that catalyzes the chemical reaction :ATP + H2O + sulfateout \rightleftharpoons ADP + phosphate + sulfatein The 3 substrates of this enzyme are ATP, H2O, and sulfate, whereas its 3 products are ADP, phosphate, and sulfate. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (sulfate-importing). This enzyme participates in abc transporters - general.

In enzymology, a phosphate-transporting ATPase () is an enzyme that catalyzes the chemical reaction :ATP + H2O + phosphate(out) \rightleftharpoons ADP + phosphate + phosphate(in) The 3 substrates of this enzyme are ATP, H2O, and phosphate, whereas its two products are ADP and phosphate. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (phosphate-importing). This enzyme is also called ABC phosphate transporter.

In enzymology, a polyamine-transporting ATPase () is an enzyme that catalyzes the chemical reaction :ATP + H2O + polyamineout \rightleftharpoons ADP + phosphate + polyaminein The 3 substrates of this enzyme are ATP, H2O, and polyamine, whereas its 3 products are ADP, phosphate, and polyamine. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (polyamine-importing). This enzyme participates in abc transporters - general.

In enzymology, a sugar-terminal-phosphatase () is an enzyme that catalyzes the chemical reaction :D-glucose 6-phosphate + H2O \rightleftharpoons D-glucose + phosphate Thus, the two substrates of this enzyme are D-glucose 6-phosphate and H2O, whereas its two products are D-glucose and phosphate. This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name of this enzyme class is sugar-omega- phosphate phosphohydrolase. This enzyme is also called xylitol-5-phosphatase.

In enzymology, a feruloyl esterase () is an enzyme that catalyzes the chemical reaction :feruloyl-polysaccharide + H2O \rightleftharpoons ferulate + polysaccharide Thus, the two substrates of this enzyme are feruloyl- polysaccharide and H2O, whereas its two products are ferulate and polysaccharide. This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is feruloyl esterase. Other names in common use include ferulic acid esterase (FAE), hydroxycinnamoyl esterase, hemicellulase accessory enzyme, cinnamoyl ester hydrolase (cinnAE).

In enzymology, a glycerophosphocholine cholinephosphodiesterase () is an enzyme that catalyzes the chemical reaction :sn-glycero-3-phosphocholine + H2O \rightleftharpoons glycerol + choline phosphate Thus, the two substrates of this enzyme are sn-glycero-3-phosphocholine and H2O, whereas its two products are glycerol and choline phosphate. This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric diester bonds. The systematic name of this enzyme class is sn-glycero-3-phosphocholine cholinephosphohydrolase. This enzyme is also called L-3-glycerylphosphinicocholine cholinephosphohydrolase.

In enzymology, a methylumbelliferyl-acetate deacetylase (, esterase D) is an enzyme that catalyzes the chemical reaction :4-methylumbelliferyl acetate + H2O \rightleftharpoons 4-methylumbelliferone + acetate Thus, the two substrates of this enzyme are 4-methylumbelliferyl acetate and H2O, whereas its two products are 4-methylumbelliferone and acetate. This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is 4-methylumbelliferyl-acetate acylhydrolase. This enzyme is also called esterase D.

In enzymology, a mannitol-1-phosphatase () is an enzyme that catalyzes the chemical reaction :D-mannitol 1-phosphate + H2O \rightleftharpoons D-mannitol + phosphate Thus, the two substrates of this enzyme are D-mannitol 1-phosphate and H2O, whereas its two products are D-mannitol and phosphate. This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name of this enzyme class is D-mannitol-1-phosphate phosphohydrolase. This enzyme is also called mannitol-1-phosphate phosphatase.

In enzymology, a [pyruvate kinase]-phosphatase () is an enzyme that catalyzes the chemical reaction :[pyruvate kinase] phosphate + HO \rightleftharpoons [pyruvate kinase] + phosphate Thus, the two substrates of this enzyme are pyruvate kinase phosphate and HO, whereas its two products are pyruvate kinase and phosphate. This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name of this enzyme class is [ATP:pyruvate 2-O-phosphotransferase]-phosphate phosphohydrolase. This enzyme is also called pyruvate kinase phosphatase.

In enzymology, a 6-acetylglucose deacetylase () is an enzyme that catalyzes the chemical reaction :6-acetyl-D-glucose + H2O \rightleftharpoons D-glucose + acetate Thus, the two substrates of this enzyme are 6-acetyl-D-glucose and H2O, whereas its two products are D-glucose and acetate. This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is 6-acetyl-D-glucose acetylhydrolase. This enzyme is also called 6-O-acetylglucose deacetylase.

In enzymology, a glutaconate CoA-transferase () is an enzyme that catalyzes the chemical reaction :acetyl-CoA + (E)-glutaconate \rightleftharpoons acetate + glutaconyl-1-CoA Thus, the two substrates of this enzyme are acetyl-CoA and (E)-glutaconate, whereas its two products are acetate and glutaconyl-1-CoA. This enzyme belongs to the family of transferases, specifically the CoA- transferases. The systematic name of this enzyme class is acetyl- CoA:(E)-glutaconate CoA-transferase. This enzyme participates in styrene degradation and butanoate metabolism.

In enzymology, a lysine carbamoyltransferase () is an enzyme that catalyzes the chemical reaction :carbamoyl phosphate + L-lysine \rightleftharpoons phosphate + L-homocitrulline Thus, the two substrates of this enzyme are carbamoyl phosphate and L-lysine, whereas its two products are phosphate and L-homocitrulline. This enzyme belongs to the family of transferases that transfer one-carbon groups, specifically the carboxy- and carbamoyltransferases. The systematic name of this enzyme class is carbamoyl- phosphate:L-lysine carbamoyltransferase. This enzyme is also called lysine transcarbamylase.

In enzymology, a beta-diketone hydrolase () is an enzyme that catalyzes the chemical reaction :nonane-4,6-dione + H2O \rightleftharpoons pentan-2-one + butanoate Thus, the two substrates of this enzyme are nonane-4,6-dione and H2O, whereas its two products are 2-pentanone and butanoate. This enzyme belongs to the family of hydrolases, specifically those acting on carbon- carbon bonds in ketonic substances. The systematic name of this enzyme class is nonane-4,6-dione acylhydrolase. This enzyme is also called oxidized PVA hydrolase.

In enzymology, a cyclohexane-1,3-dione hydrolase () is an enzyme that catalyzes the chemical reaction :cyclohexane-1,3-dione + H2O \rightleftharpoons 5-oxohexanoate Thus, the two substrates of this enzyme are cyclohexane-1,3-dione and H2O, whereas its product is 5-oxohexanoate. This enzyme belongs to the family of hydrolases, specifically those acting on carbon-carbon bonds in ketonic substances. The systematic name of this enzyme class is cyclohexane-1,3-dione acylhydrolase (decyclizing). This enzyme is also called 1,3-cyclohexanedione hydrolase.

In enzymology, an acetoacetate-CoA ligase () is an enzyme that catalyzes the chemical reaction :ATP + acetoacetate + CoA \rightleftharpoons AMP + diphosphate + acetoacetyl-CoA The 3 substrates of this enzyme are ATP, acetoacetate, and CoA, whereas its 3 products are AMP, diphosphate, and acetoacetyl-CoA. This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The systematic name of this enzyme class is acetoacetate:CoA ligase (AMP-forming). This enzyme is also called acetoacetyl-CoA synthetase.

In enzymology, an arachidonate-CoA ligase () is an enzyme that catalyzes the chemical reaction :ATP + arachidonate + CoA \rightleftharpoons AMP + diphosphate + arachidonoyl-CoA The 3 substrates of this enzyme are ATP, arachidonate, and CoA, whereas its 3 products are AMP, diphosphate, and arachidonoyl-CoA. This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The systematic name of this enzyme class is arachidonate:CoA ligase (AMP-forming). This enzyme is also called arachidonoyl-CoA synthetase.

In enzymology, a phytanate-CoA ligase () is an enzyme that catalyzes the chemical reaction :ATP + phytanate + CoA \rightleftharpoons AMP + diphosphate + phytanoyl-CoA The 3 substrates of this enzyme are ATP, phytanate, and CoA, whereas its 3 products are AMP, diphosphate, and phytanoyl-CoA. This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The systematic name of this enzyme class is phytanate:CoA ligase (AMP-forming). This enzyme is also called phytanoyl-CoA ligase.

In enzymology, a dethiobiotin synthase () is an enzyme that catalyzes the chemical reaction :ATP + 7,8-diaminononanoate + CO2 \rightleftharpoons ADP + phosphate + dethiobiotin The 3 substrates of this enzyme are ATP, 7,8-diaminononanoate, and CO2, whereas its 3 products are ADP, phosphate, and dethiobiotin. This enzyme belongs to the family of ligases, specifically the cyclo-ligases, which form carbon-nitrogen bonds. The systematic name of this enzyme class is 7,8-diaminononanoate:carbon-dioxide cyclo-ligase (ADP- forming). This enzyme is also called desthiobiotin synthase.

In enzymology, a propionate-CoA ligase () is an enzyme that catalyzes the chemical reaction :ATP + propanoate + CoA \rightleftharpoons AMP + diphosphate + propanoyl-CoA The 3 substrates of this enzyme are ATP, propanoate, and CoA, whereas its 3 products are AMP, diphosphate, and propanoyl-CoA. This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The systematic name of this enzyme class is propanoate:CoA ligase (AMP-forming). This enzyme is also called propionyl-CoA synthetase.

In enzymology, a citryl-CoA lyase () is an enzyme that catalyzes the chemical reaction :(3S)-citryl-CoA \rightleftharpoons acetyl-CoA + oxaloacetate Hence, this enzyme has one substrate, (3S)-citryl-CoA, and two products, acetyl-CoA and oxaloacetate. This enzyme belongs to the family of lyases, specifically the oxo-acid-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is (3S)-citryl-CoA oxaloacetate-lyase (acetyl-CoA-forming). This enzyme is also called (3S)-citryl-CoA oxaloacetate-lyase.

In enzymology, a 4-oxalocrotonate decarboxylase () is an enzyme that catalyzes the chemical reaction :4-oxalocrotonate \rightleftharpoons 2-oxopent-4-enoate + CO2 Hence, this enzyme has one substrate, 4-oxalocrotonate, and two products, 2-oxopent-4-enoate and CO2. This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is 4-oxalocrotonate carboxy-lyase (2-oxopent-4-enoate-forming). This enzyme is also called 4-oxalocrotonate carboxy-lyase.

In enzymology, an octadecanal decarbonylase () is an enzyme that catalyzes the chemical reaction :octadecanal \rightleftharpoons heptadecane + CO Hence, this enzyme has one substrate, octadecanal, and two products, heptadecane and CO. This enzyme belongs to the family of lyases, specifically in the "catch-all" class of carbon-carbon lyases. The systematic name of this enzyme class is octadecanal alkane-lyase. Other names in common use include decarbonylase, and aldehyde decarbonylase. At least one compound, EDTA is known to inhibit this enzyme.

In enzymology, a phenylserine aldolase () is an enzyme that catalyzes the chemical reaction :L-threo-3-phenylserine \rightleftharpoons glycine + benzaldehyde Hence, this enzyme has one substrate, L-threo-3-phenylserine, and two products, glycine and benzaldehyde. This enzyme belongs to the family of lyases, specifically the aldehyde-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is L-threo-3-phenylserine benzaldehyde-lyase (glycine-forming). This enzyme is also called L-threo-3-phenylserine benzaldehyde-lyase.

In enzymology, a 1,3-alpha-L-fucosidase () is an enzyme that catalyzes the chemical reaction of cleaving the 1,3-linkages between alpha-L-fucose and N-acetylglucosamine residues in glycoproteins. This enzyme belongs to the family of hydrolases, specifically those glycosidases that hydrolyse O- and S-glycosyl compounds. The systematic name of this enzyme class is 3-alpha-L- fucosyl-N-acetylglucosaminyl-glycoprotein fucohydrolase. This enzyme is also called almond emulsin fucosidase I. This enzyme participates in the degradation of glycan structures.

In enzymology, a 3-deoxyoctulosonase () is an enzyme that catalyzes the chemical reaction :3-deoxyoctulosonyl-lipopolysaccharide + H2O \rightleftharpoons 3-deoxyoctulosonic acid + lipopolysaccharide Thus, the two substrates of this enzyme are 3-deoxyoctulosonyl-lipopolysaccharide and H2O, whereas its two products are 3-deoxyoctulosonic acid and lipopolysaccharide. This enzyme belongs to the family of hydrolases, specifically those glycosidases that hydrolyse O- and S-glycosyl compounds. The systematic name of this enzyme class is 3-deoxyoctulosonyl-lipopolysaccharide hydrolase. This enzyme is also called alpha-Kdo-ase.

In enzymology, an alpha-L-fucosidase () is an enzyme that catalyzes the chemical reaction :an alpha-L-fucoside + H2O \rightleftharpoons L-fucose + an alcohol Thus, the two substrates of this enzyme are alpha-L-fucoside and H2O, whereas its two products are L-fucose and alcohol. This enzyme belongs to the family of hydrolases, specifically those glycosidases that hydrolyse O- and S-glycosyl compounds. The systematic name of this enzyme class is alpha-L- fucoside fucohydrolase. This enzyme is also called alpha-fucosidase.

In enzymology, a beta-L-arabinosidase () is an enzyme that catalyzes the chemical reaction :a beta-L-arabinoside + H2O \rightleftharpoons L-arabinose + an alcohol Thus, the two substrates of this enzyme are beta-L-arabinoside and H2O, whereas its two products are L-arabinose and alcohol. This enzyme belongs to the family of hydrolases, specifically those glycosidases that hydrolyse O- and S-glycosyl compounds. The systematic name of this enzyme class is beta-L- arabinoside arabinohydrolase. This enzyme is also called vicianosidase.

In enzymology, an ureidoglycolate hydrolase () is an enzyme that catalyzes the chemical reaction :(S)-ureidoglycolate + H2O \rightleftharpoons glyoxylate + 2 NH3 \+ CO2 Thus, the two substrates of this enzyme are (S)-ureidoglycolate and H2O, whereas its 3 products are glyoxylate, NH3, and CO2. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amidines. The systematic name of this enzyme class is (S)-ureidoglycolate amidohydrolase (decarboxylating). This enzyme participates in purine metabolism.

In enzymology, a riboflavinase () is an enzyme that catalyzes the chemical reaction :riboflavin + H2O \rightleftharpoons ribitol + lumichrome Thus, the two substrates of this enzyme are riboflavin and H2O, whereas its two products are ribitol and lumichrome. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in compounds that have not been otherwise categorized within EC number 3.5. The systematic name of this enzyme class is riboflavin hydrolase. This enzyme participates in riboflavin metabolism.

In enzymology, a N-carbamoylsarcosine amidase () is an enzyme that catalyzes the chemical reaction :N-carbamoylsarcosine + H2O \rightleftharpoons sarcosine + CO2 \+ NH3 Thus, the two substrates of this enzyme are N-carbamoylsarcosine and H2O, whereas its 3 products are sarcosine, CO2, and NH3. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N-carbamoylsarcosine amidohydrolase. This enzyme is also called carbamoylsarcosine amidase.

In enzymology, a N-feruloylglycine deacylase () is an enzyme that catalyzes the chemical reaction :N-feruloylglycine + H2O \rightleftharpoons ferulate + glycine Thus, the two substrates of this enzyme are N-feruloylglycine and H2O, whereas its two products are ferulate and glycine. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N-feruloylglycine amidohydrolase. This enzyme is also called N-feruloylglycine hydrolase.

In enzymology, a biuret amidohydrolase () is an enzyme that catalyzes the chemical reaction :biuret + H2O \rightleftharpoons urea(CH₄N₂O) + CO2 \+ NH3 Thus, the two substrates of this enzyme are biuret and H2O, whereas its 3 products are urea, CO2, and NH3. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is biuret amidohydrolase. This enzyme participates in atrazine degradation.

In enzymology, an aminoimidazolase () is an enzyme that catalyzes the chemical reaction :4-aminoimidazole + H2O \rightleftharpoons unidentified product + NH3 Thus, the two substrates of this enzyme are 4-aminoimidazole and H2O, whereas its two products are unidentified product and NH3. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is 4-aminoimidazole aminohydrolase. This enzyme is also called 4-aminoimidazole hydrolase.

In enzymology, a carboxymethylhydantoinase () is an enzyme that catalyzes the chemical reaction :L-5-carboxymethylhydantoin + H2O \rightleftharpoons N-carbamoyl-L-aspartate Thus, the two substrates of this enzyme are L-5-carboxymethylhydantoin and H2O, whereas its product is N-carbamoyl-L- aspartate. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amides. The systematic name of this enzyme class is L-5-carboxymethylhydantoin amidohydrolase. This enzyme is also called hydantoin hydrolase.

In enzymology, a mandelamide amidase () is an enzyme that catalyzes the chemical reaction :(R)-mandelamide + H2O \rightleftharpoons (R)-mandelate + NH3 Thus, the two substrates of this enzyme are (R)-mandelamide and H2O, whereas its two products are (R)-mandelate and NH3. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is mandelamide hydrolase. This enzyme is also called Pseudomonas mandelamide hydrolase.

In enzymology, an acetylputrescine deacetylase () is an enzyme that catalyzes the chemical reaction :N-acetylputrescine + H2O \rightleftharpoons acetate + putrescine Thus, the two substrates of this enzyme are N-acetylputrescine and H2O, whereas its two products are acetate and putrescine. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N-acetylputrescine acetylhydrolase. This enzyme participates in urea cycle and metabolism of amino groups.

In enzymology, a dCTP deaminase (dUMP-forming) () is an enzyme that catalyzes the chemical reaction :dCTP + 2 H2O \rightleftharpoons dUMP + diphosphate + NH3 Thus, the two substrates of this enzyme are dCTP and H2O, whereas its 3 products are dUMP, diphosphate, and NH3. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is dCTP aminohydrolase (dUMP-forming). This enzyme participates in pyrimidine metabolism.

In enzymology, a glutathionylspermidine amidase () is an enzyme that catalyzes the chemical reaction :glutathionylspermidine + H2O \rightleftharpoons glutathione + spermidine Thus, the two substrates of this enzyme are glutathionylspermidine and H2O, whereas its two products are glutathione and spermidine. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is gamma-L-glutamyl-L-cysteinyl- glycine:spermidine amidase. This enzyme is also called glutathionylspermidine amidohydrolase (spermidine-forming).

In enzymology, a carnosine N-methyltransferase () is an enzyme that catalyzes the chemical reaction :S-adenosyl-L-methionine + carnosine \rightleftharpoons S-adenosyl-L-homocysteine + anserine Thus, the two substrates of this enzyme are S-adenosyl methionine and carnosine, whereas its two products are S-adenosylhomocysteine and anserine. This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L- methionine:carnosine N-methyltransferase. This enzyme participates in histidine metabolism.

In enzymology, a columbamine O-methyltransferase () is an enzyme that catalyzes the chemical reaction :S-adenosyl-L-methionine + columbamine \rightleftharpoons S-adenosyl-L-homocysteine + palmatine Thus, the two substrates of this enzyme are S-adenosyl methionine and columbamine, whereas its two products are S-adenosylhomocysteine and palmatine. This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:columbamine O-methyltransferase. This enzyme participates in alkaloid biosynthesis i.

In enzymology, a geissoschizine dehydrogenase () is an enzyme that catalyzes the chemical reaction :geissoschizine + NADP+ \rightleftharpoons 4,21-didehydrogeissoschizine + NADPH Thus, the two substrates of this enzyme are geissoschizine and NADP+, whereas its two products are 4,21-didehydrogeissoschizine and NADPH. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is geissoschizine:NADP+ 4,21-oxidoreductase. This enzyme participates in indole and ipecac alkaloid biosynthesis.

In enzymology, a phloroglucinol reductase () is an enzyme that catalyzes the chemical reaction :dihydrophloroglucinol + NADP+ \rightleftharpoons phloroglucinol + NADPH + H+ Thus, the two substrates of this enzyme are dihydrophloroglucinol and NADP+, whereas its 3 products are phloroglucinol, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is dihydrophloroglucinol:NADP+ oxidoreductase. This enzyme participates in benzoate degradation via coa ligation.

In enzymology, a bilirubin oxidase, BOD or BOx, () is an enzyme encoded by a gene in various organisms that catalyzes the chemical reaction :2 bilirubin + O2 \rightleftharpoons 2 biliverdin + 2 H2O This enzyme belongs to the family of oxidoreductases, to be specific those acting on the CH-CH group of donor with oxygen as acceptor. The systematic name of this enzyme class is bilirubin:oxygen oxidoreductase. This enzyme is also called bilirubin oxidase M-1. This enzyme participates in porphyrin and chlorophyll metabolism.

In enzymology, a phenol O-methyltransferase () is an enzyme that catalyzes the chemical reaction :S-adenosyl-L-methionine + phenol \rightleftharpoons S-adenosyl-L-homocysteine + anisole Thus, the two substrates of this enzyme are S-adenosyl methionine and phenol, whereas its two products are S-adenosylhomocysteine and anisole. This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L- methionine:phenol O-methyltransferase. This enzyme is also called PMT.

In enzymology, a naringenin 8-dimethylallyltransferase () is an enzyme that catalyzes the chemical reaction :dimethylallyl diphosphate + (-)-(2S)-naringenin \rightleftharpoons diphosphate + sophoraflavanone B Thus, the two substrates of this enzyme are dimethylallyl diphosphate and (-)-(2S)-naringenin, whereas its two products are diphosphate and sophoraflavanone B. This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is dimethylallyl- diphosphate:naringenin 8-dimethylallyltransferase. This enzyme is also called N8DT.

In enzymology, a biphenyl synthase () is an enzyme that catalyzes the chemical reaction: :3 malonyl-CoA + benzoyl-CoA \rightleftharpoons 4 CoA + 3,5-dihydroxybiphenyl + 4 CO2 Thus, the two substrates of this enzyme are malonyl-CoA and benzoyl-CoA, whereas its three products are CoA, 3,5-dihydroxybiphenyl, and CO2. This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is malonyl- CoA:benzoyl-CoA malonyltransferase. This enzyme is also called BIS.

In enzymology, an alcohol O-acetyltransferase () is an enzyme that catalyzes the chemical reaction :acetyl-CoA + an alcohol \rightleftharpoons CoA + an acetyl ester Thus, the two substrates of this enzyme are acetyl-CoA and alcohol, whereas its two products are CoA and acetyl ester. This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acetyl-CoA:alcohol O-acetyltransferase. This enzyme is also called alcohol acetyltransferase.

In prokaryotic proline biosynthesis, GSA is synthesized from γ-glutamyl phosphate by the enzyme γ-glutamyl phosphate reductase. In most eukaryotes, GSA is synthesised from the amino acid glutamate by the bifunctional enzyme 1-pyrroline-5-carboxylate synthase(P5CS). The human P5CS is encoded by the ALDH18A1 gene. The enzyme pyrroline-5-carboxylate reductase converts P5C into proline In proline degradation, the enzyme proline dehydrogenase produces P5C from proline, and the enzyme 1-pyrroline-5-carboxylate dehydrogenase converts GSA to glutamate.

In enzymology, a kynurenine-glyoxylate transaminase () is an enzyme that catalyzes the chemical reaction :L-kynurenine + glyoxylate \rightleftharpoons 4-(2-aminophenyl)-2,4-dioxobutanoate + glycine Thus, the two substrates of this enzyme are L-kynurenine and glyoxylate, whereas its two products are 4-(2-aminophenyl)-2,4-dioxobutanoate and glycine. This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-kynurenine:glyoxylate aminotransferase (cyclizing). This enzyme is also called kynurenine-glyoxylate aminotransferase.

In enzymology, a vinorine synthase () is an enzyme that catalyzes the chemical reaction :acetyl-CoA + 16-epivellosimine \rightleftharpoons CoA + vinorine Thus, the two substrates of this enzyme are acetyl-CoA and 16-epivellosimine, whereas its two products are CoA and vinorine. This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acyl-CoA:16-epivellosimine O-acetyltransferase (cyclizing). This enzyme participates in indole and ipecac alkaloid biosynthesis.

In enzymology, a shikimate O-hydroxycinnamoyltransferase () is an enzyme that catalyzes the chemical reaction :4-coumaroyl-CoA + shikimate \rightleftharpoons CoA + 4-coumaroylshikimate Thus, the two substrates of this enzyme are 4-coumaroyl-CoA and shikimate, whereas its two products are CoA and 4-coumaroylshikimate. This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is 4-coumaroyl-CoA:shikimate O-(hydroxycinnamoyl)transferase. This enzyme is also called shikimate hydroxycinnamoyltransferase.

In enzymology, a quinate O-hydroxycinnamoyltransferase () is an enzyme that catalyzes the chemical reaction :feruloyl-CoA + quinate \rightleftharpoons CoA + O-feruloylquinate Thus, the two substrates of this enzyme are feruloyl-CoA and quinate, whereas its two products are CoA and O-feruloylquinate. This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is feruloyl-CoA:quinate O-(hydroxycinnamoyl)transferase. This enzyme is also called hydroxycinnamoyl coenzyme A-quinate transferase.

In enzymology, a salutaridinol 7-O-acetyltransferase () is an enzyme that catalyzes the chemical reaction :acetyl-CoA + salutaridinol \rightleftharpoons CoA + 7-O-acetylsalutaridinol Thus, the two substrates of this enzyme are acetyl-CoA and salutaridinol, whereas its two products are CoA and 7-O-acetylsalutaridinol. This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acetyl-CoA:salutaridinol 7-O-acetyltransferase. This enzyme participates in alkaloid biosynthesis i.

In enzymology, a monoterpenol O-acetyltransferase () is an enzyme that catalyzes the chemical reaction :acetyl-CoA + a monoterpenol \rightleftharpoons CoA + a monoterpenol acetate ester Thus, the two substrates of this enzyme are acetyl-CoA and monoterpenol, whereas its two products are CoA and monoterpenol acetate ester. This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acetyl- CoA:monoterpenol O-acetyltransferase. This enzyme is also called menthol transacetylase.

In enzymology, a glycoprotein N-palmitoyltransferase () is an enzyme that catalyzes the chemical reaction :palmitoyl-CoA + glycoprotein \rightleftharpoons CoA + N-palmitoylglycoprotein Thus, the two substrates of this enzyme are palmitoyl-CoA and glycoprotein, whereas its two products are CoA and N-palmitoylglycoprotein. This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is palmitoyl- CoA:glycoprotein N-palmitoyltransferase. This enzyme is also called mucus glycoprotein fatty acyltransferase.

In enzymology, a glycoprotein O-fatty-acyltransferase () is an enzyme that catalyzes the chemical reaction :palmitoyl-CoA + mucus glycoprotein \rightleftharpoons CoA + O-palmitoylglycoprotein Thus, the two substrates of this enzyme are palmitoyl-CoA and mucus glycoprotein, whereas its two products are CoA and O-palmitoylglycoprotein. This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is fatty-acyl- CoA:mucus-glycoprotein fatty-acyltransferase. This enzyme is also called protein acyltransferase.

In enzymology, a hydrogen-sulfide S-acetyltransferase () is an enzyme that catalyzes the chemical reaction :acetyl-CoA + hydrogen sulfide \rightleftharpoons CoA + thioacetate Thus, the two substrates of this enzyme are acetyl-CoA and hydrogen sulfide, whereas its two products are CoA and thioacetate. This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acetyl-CoA:hydrogen-sulfide S-acetyltransferase. This enzyme is also called hydrogen-sulfide acetyltransferase.

In enzymology, a dimethylallylcistransferase () is an enzyme that catalyzes the chemical reaction :dimethylallyl diphosphate + isopentenyl diphosphate \rightleftharpoons diphosphate + neryl diphosphate Thus, the two substrates of this enzyme are dimethylallyl diphosphate and isopentenyl diphosphate, whereas its two products are diphosphate and neryl diphosphate. This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is dimethylallyl-diphosphate:isopentenyl-diphosphate dimethylallylcistransferase. This enzyme is also called neryl-diphosphate synthase.

In enzymology, an adenosylmethionine cyclotransferase () is an enzyme that catalyzes the chemical reaction :S-adenosyl-L-methionine \rightleftharpoons 5'-methylthioadenosine + 2-aminobutan-4-olide Hence, this enzyme has one substrate, S-adenosyl-L-methionine, and two products, 5'-methylthioadenosine and 2-aminobutan-4-olide. This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is S-adenosyl-L-methionine alkyltransferase (cyclizing). This enzyme is also called adenosylmethioninase.

In enzymology, a chlorate reductase () is an enzyme that catalyzes the chemical reaction :AH2 \+ chlorate \rightleftharpoons A + H2O + chlorite Thus, the two substrates of this enzyme are a reduced electron acceptor (denoted AH2) and chlorate, whereas its 3 products are an oxidized electron acceptor (denoted A), water, and chlorite. It is closely related to the enzyme perchlorate reductase which reduces both chlorate and perchlorate. This enzyme belongs to the family of oxidoreductases. The systematic name of this enzyme class is chlorite:acceptor oxidoreductase.

In enzymology, a rifamycin-B oxidase () is an enzyme that catalyzes the chemical reaction :rifamycin B + O2 \rightleftharpoons rifamycin O + H2O2 Thus, the two substrates of this enzyme are rifamycin B and O2, whereas its two products are rifamycin O and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on diphenols and related substances as donor with oxygen as acceptor. The systematic name of this enzyme class is rifamycin-B:oxygen oxidoreductase. This enzyme is also called rifamycin B oxidase.

In enzymology, a glutathione—homocystine transhydrogenase () is an enzyme that catalyzes the chemical reaction :2 glutathione + homocystine \rightleftharpoons glutathione disulfide + 2 homocysteine Thus, the two substrates of this enzyme are glutathione and homocystine, whereas its two products are glutathione disulfide and homocysteine. This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with a disulfide as acceptor. The systematic name of this enzyme class is glutathione:homocystine oxidoreductase. This enzyme participates in methionine metabolism and glutathione metabolism.

In enzymology, a retinal oxidase () is an enzyme that catalyzes the chemical reaction :retinal + O2 \+ H2O \rightleftharpoons retinoic acid + H2O2 The 3 substrates of this enzyme are retinal, O2, and H2O, whereas its two products are retinoic acid and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with oxygen as acceptor. The systematic name of this enzyme class is retinal:oxygen oxidoreductase. This enzyme is also called retinene oxidase.

In enzymology, a vanillin dehydrogenase () is an enzyme that catalyzes the chemical reaction :100px + NAD+ \+ H2O \rightleftharpoons 100px + NADH + H+ The 3 substrates of this enzyme are vanillin, NAD+, and H2O, whereas its 3 products are vanillate, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is vanillin:NAD+ oxidoreductase. This enzyme participates in 2,4-dichlorobenzoate degradation.

In enzymology, a carboxylate reductase () is an enzyme that catalyzes the chemical reaction :an aldehyde + acceptor + H2O \rightleftharpoons a carboxylate + reduced acceptor The 3 substrates of this enzyme are aldehyde, acceptor, and H2O, whereas its two products are carboxylate and reduced acceptor. This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with other acceptors. The systematic name of this enzyme class is aldehyde:acceptor oxidoreductase. This enzyme is also called aldehyde:(acceptor) oxidoreductase.

In enzymology, a glycerol dehydrogenase (acceptor) () is an enzyme that catalyzes the chemical reaction :glycerol + acceptor \rightleftharpoons glycerone + reduced acceptor Thus, the two substrates of this enzyme are glycerol and acceptor, whereas its two products are glycerone and reduced acceptor. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other acceptors. The systematic name of this enzyme class is glycerol:acceptor 1-oxidoreductase. This enzyme is also called glycerol:(acceptor) 1-oxidoreductase.

In enzymology, an alcohol oxidase () is an enzyme that catalyzes the chemical reaction :a primary alcohol + O2 \rightleftharpoons an aldehyde + H2O2 Thus, the two substrates of this enzyme are primary alcohol and O2, whereas its two products are aldehyde and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of the donor with oxygen as the acceptor. The systematic name of this enzyme class is alcohol:oxygen oxidoreductase. This enzyme is also called ethanol oxidase.

In enzymology, a vanillyl-alcohol oxidase () is an enzyme that catalyzes the chemical reaction :110px + O2 \rightleftharpoons 115px + H2O2 Thus, the two substrates of this enzyme are vanillyl alcohol and O2, whereas its two products are vanillin and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. The systematic name of this enzyme class is vanillyl alcohol:oxygen oxidoreductase. This enzyme is also called 4-hydroxy-2-methoxybenzyl alcohol oxidase.

In enzymology, a lactate—malate transhydrogenase () is an enzyme that catalyzes the chemical reaction :(S)-lactate + oxaloacetate \rightleftharpoons pyruvate + malate Thus, the two substrates of this enzyme are (S)-lactate and oxaloacetate, whereas its two products are pyruvate and malate. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH- OH group of donor with other acceptors. The systematic name of this enzyme class is (S)-lactate:oxaloacetate oxidoreductase. This enzyme is also called malate-lactate transhydrogenase.

In enzymology, a choline oxidase () is an enzyme that catalyzes the chemical reaction :choline + O2 \rightleftharpoons betaine aldehyde + H2O2 Thus, the two substrates of this enzyme are choline and O2, whereas its two products are betaine aldehyde and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. The systematic name of this enzyme class is choline:oxygen 1-oxidoreductase. This enzyme participates in glycine, serine, and threonine metabolism.

In enzymology, a fatty-acid peroxidase () is an enzyme that catalyzes the chemical reaction :palmitate + 2 H2O2 \rightleftharpoons pentadecanal + CO2 \+ 3 H2O Thus, the two substrates of this enzyme are palmitate and H2O2, whereas its 3 products are pentadecanal, CO2, and H2O. This enzyme belongs to the family of oxidoreductases, specifically those acting on a peroxide as acceptor (peroxidases). The systematic name of this enzyme class is hexadecanoate:hydrogen-peroxide oxidoreductase. This enzyme is also called long chain fatty acid peroxidase.

In enzymology, a methylarsonate reductase () is an enzyme that catalyzes the chemical reaction :methylarsonate + 2 glutathione \rightleftharpoons methylarsonite + glutathione disulfide + H2O Thus, the two substrates of this enzyme are methylarsonate and glutathione, whereas its 3 products are methylarsonite, glutathione disulfide, and H2O. This enzyme belongs to the family of oxidoreductases, specifically those acting on phosphorus or arsenic in donor with disulfide as acceptor. The systematic name of this enzyme class is gluthathione:methylarsonate oxidoreductase. This enzyme is also called MMA(V) reductase.

In enzymology, a p-benzoquinone reductase (NADPH) () is an enzyme that catalyzes the chemical reaction :NADPH + H+ \+ p-benzoquinone \rightleftharpoons NADP+ \+ hydroquinone The 3 substrates of this enzyme are NADPH, H+, and p-benzoquinone, whereas its two products are NADP+ and hydroquinone. This enzyme belongs to the family of oxidoreductases, specifically those acting on NADH or NADPH with a quinone or similar compound as acceptor. The systematic name of this enzyme class is NADPH:p-benzoquinone oxidoreductase. This enzyme participates in gamma-hexachlorocyclohexane degradation.

In enzymology, a taurine dehydrogenase () is an enzyme that catalyzes the chemical reaction :taurine + H2O + acceptor \rightleftharpoons sulfoacetaldehyde + NH3 \+ reduced acceptor The 3 substrates of this enzyme are taurine, H2O, and acceptor, whereas its 3 products are sulfoacetaldehyde, NH3, and reduced acceptor. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with other acceptors. The systematic name of this enzyme class is taurine:acceptor oxidoreductase (deaminating). This enzyme is also called taurine:(acceptor) oxidoreductase (deaminating).

In enzymology, an alpha-pinene-oxide decyclase () is an enzyme that catalyzes the chemical reaction :alpha-pinene oxide \rightleftharpoons (Z)-2-methyl-5-isopropylhexa-2,5-dienal Hence, this enzyme has one substrate, alpha-pinene oxide, and one product, (Z)-2-methyl-5-isopropylhexa-2,5-dienal. This enzyme belongs to the family of isomerases, specifically the class of intramolecular lyases. The systematic name of this enzyme class is alpha- pinene-oxide lyase (decyclizing). This enzyme is also called alpha-pinene oxide lyase.

In enzymology, an arginine racemase () is an enzyme that catalyzes the chemical reaction :L-arginine \rightleftharpoons D-arginine Hence, this enzyme has one substrate, L-arginine, and one product, D-arginine. This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on amino acids and derivatives. The systematic name of this enzyme class is arginine racemase. This enzyme participates in 3 metabolic pathways: lysine degradation, D-glutamine and D-glutamate metabolism, and D-arginine and D-ornithine metabolism.

In enzymology, a beta-phosphoglucomutase () is an enzyme that catalyzes the chemical reaction :beta-D-glucose 1-phosphate \rightleftharpoons beta-D- glucose 6-phosphate Hence, this enzyme has one substrate, beta-D-glucose 1-phosphate, and one product, beta-D-glucose 6-phosphate. This enzyme belongs to the family of isomerases, specifically the phosphotransferases (phosphomutases), which transfer phosphate groups within a molecule. The systematic name of this enzyme class is beta-D-glucose 1,6-phosphomutase. This enzyme participates in starch and sucrose metabolism.

In enzymology, a phosphoglucosamine mutase () is an enzyme that catalyzes the chemical reaction :alpha-D-glucosamine 1-phosphate \rightleftharpoons D-glucosamine 6-phosphate Hence, this enzyme has one substrate, alpha-D- glucosamine 1-phosphate, and one product, D-glucosamine 6-phosphate. This enzyme belongs to the family of isomerases, specifically the phosphotransferases (a-D-phosphohexomutases), which transfer phosphate groups within a molecule. The systematic name of this enzyme class is alpha-D- glucosamine 1,6-phosphomutase. This enzyme participates in aminosugars metabolism.

In enzymology, a farnesol 2-isomerase () is an enzyme that catalyzes the chemical reaction :2-trans,6-trans-farnesol \rightleftharpoons 2-cis,6-trans- farnesol Hence, this enzyme has one substrate, 2-trans,6-trans-farnesol, and one product, 2-cis,6-trans-farnesol. This enzyme belongs to the family of isomerases, specifically cis-trans isomerases. The systematic name of this enzyme class is 2-trans,6-trans-farnesol 2-cis-trans-isomerase. This enzyme is also called farnesol isomerase.

In enzymology, a beta-alanyl-CoA ammonia-lyase () is an enzyme that catalyzes the chemical reaction :beta-alanyl-CoA \rightleftharpoons acryloyl-CoA + NH3 Hence, this enzyme has one substrate, beta-alanyl-CoA, and two products, acryloyl-CoA and NH3. This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic name of this enzyme class is beta-alanyl-CoA ammonia-lyase (acryloyl-CoA-forming). This enzyme is also called beta-alanyl coenzyme A ammonia-lyase.

In enzymology, a pyrimidine-nucleoside phosphorylase () is an enzyme that catalyzes the chemical reaction :a pyrimidine nucleoside + phosphate \rightleftharpoons a pyrimidine base + alpha-D-ribose 1-phosphate Thus, the two substrates of this enzyme are pyrimidine nucleoside and phosphate, whereas its two products are pyrimidine base and alpha-D-ribose 1-phosphate. This enzyme belongs to the family of glycosyltransferases, specifically the pentosyltransferases. The systematic name of this enzyme class is pyrimidine- nucleoside:phosphate alpha-D-ribosyltransferase. This enzyme is also called Py-NPase.

In enzymology, an erythrulose reductase () is an enzyme that catalyzes the chemical reaction :erythritol + NADP+ \rightleftharpoons D-erythrulose + NADPH + H+ Thus, the two substrates of this enzyme are erythritol and NADP+, whereas its 3 products are D-erythrulose, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is erythritol:NADP+ oxidoreductase. This enzyme is also called D-erythrulose reductase.

In enzymology, a chlordecone reductase () is an enzyme that catalyzes the chemical reaction :chlordecone alcohol + NADP+ \rightleftharpoons chlordecone + NADPH + H+ Thus, the two substrates of this enzyme are chlordecone alcohol and NADP+, whereas its 3 products are chlordecone, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH- OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is chlordecone-alcohol:NADP+ 2-oxidoreductase. This enzyme is also called CDR.

In enzymology, a codeinone reductase (NADPH) () is an enzyme that catalyzes the chemical reaction :codeine + NADP+ \rightleftharpoons codeinone + NADPH + H+ Thus, the two substrates of this enzyme are codeine and NADP+, whereas its 3 products are codeinone, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is codeine:NADP+ oxidoreductase. This enzyme participates in alkaloid biosynthesis i.

In enzymology, an isopiperitenol dehydrogenase () is an enzyme that catalyzes the chemical reaction :(-)-trans-isopiperitenol + NAD+ \rightleftharpoons (-)-isopiperitenone + NADH + H+ Thus, the two substrates of this enzyme are (-)-trans-isopiperitenol and NAD+, whereas its 3 products are (-)-isopiperitenone, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (-)-trans-isopiperitenol:NAD+ oxidoreductase. This enzyme participates in monoterpenoid biosynthesis.

In enzymology, a pantetheine kinase () is an enzyme that catalyzes the chemical reaction :ATP + pantetheine \rightleftharpoons ADP + pantetheine 4'-phosphate Thus, the two substrates of this enzyme are ATP and pantetheine, whereas its two products are ADP and pantetheine 4'-phosphate. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:pantetheine 4'-phosphotransferase. This enzyme is also called pantetheine kinase (phosphorylating).

In enzymology, a phenylalanine adenylyltransferase () is an enzyme that catalyzes the chemical reaction :ATP + L-phenylalanine \rightleftharpoons diphosphate + N-adenylyl-L-phenylalanine Thus, the two substrates of this enzyme are ATP and L-phenylalanine, whereas its two products are diphosphate and N-adenylyl-L-phenylalanine. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is ATP:L-phenylalanine adenylyltransferase. This enzyme is also called L-phenylalanine adenylyltransferase.

In enzymology, a pseudouridine kinase () is an enzyme that catalyzes the chemical reaction :ATP + pseudouridine \rightleftharpoons ADP + pseudouridine 5'-phosphate Thus, the two substrates of this enzyme are ATP and pseudouridine, whereas its two products are ADP and pseudouridine 5'-phosphate. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:pseudouridine 5'-phosphotransferase. This enzyme is also called pseudouridine kinase (phosphorylating).

In enzymology, a selenide, water dikinase () is an enzyme that catalyzes the chemical reaction :ATP + selenide + H2O \rightleftharpoons AMP + selenophosphate + phosphate The 3 substrates of this enzyme are ATP, selenide, and H2O, whereas its 3 products are AMP, selenophosphate, and phosphate. This enzyme belongs to the family of transferases, to be specific, those transferring phosphorus-containing groups (phosphotransferases) with paired acceptors (dikinases). The systematic name of this enzyme class is ATP:selenide, water phosphotransferase. This enzyme is also called selenophosphate synthetase.

In enzymology, a ribosylnicotinamide kinase () is an enzyme that catalyzes the chemical reaction :ATP + N-ribosylnicotinamide \rightleftharpoons ADP + nicotinamide ribonucleotide Thus, the two substrates of this enzyme are ATP and N-ribosylnicotinamide, whereas its two products are ADP and nicotinamide ribonucleotide. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:N-ribosylnicotinamide 5'-phosphotransferase. This enzyme is also called ribosylnicotinamide kinase (phosphorylating).

In enzymology, a farnesyl-diphosphate kinase () is an enzyme that catalyzes the chemical reaction :ATP + farnesyl diphosphate \rightleftharpoons ADP + farnesyl triphosphate Thus, the two substrates of this enzyme are ATP and farnesyl diphosphate, whereas its two products are ADP and farnesyl triphosphate. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. The systematic name of this enzyme class is ATP:farnesyl-diphosphate phosphotransferase. This enzyme is also called farnesyl pyrophosphate kinase.

In enzymology, a dolichol kinase () is an enzyme that catalyzes the chemical reaction :CTP + dolichol \rightleftharpoons CDP + dolichyl phosphate Thus, the two substrates of this enzyme are CTP and dolichol, whereas its two products are CDP and dolichyl phosphate. This enzyme belongs to the family of transferases, to be specific, those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is CTP:dolichol O-phosphotransferase. This enzyme is also called dolichol phosphokinase.

In enzymology, an erythritol kinase () is an enzyme that catalyzes the chemical reaction :ATP + erythritol \rightleftharpoons ADP + D-erythritol 4-phosphate Thus, the two substrates of this enzyme are ATP and erythritol, whereas its two products are ADP and D-erythritol 4-phosphate. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:erythritol 4-phosphotransferase. This enzyme is also called erythritol kinase (phosphorylating).

In enzymology, a salutaridine reductase (NADPH) () is an enzyme that catalyzes the chemical reaction :salutaridinol + NADP+ \rightleftharpoons salutaridine + NADPH + H+ Thus, the two substrates of this enzyme are salutaridinol and NADP+, whereas its 3 products are salutaridine, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH- OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is salutaridinol:NADP+ 7-oxidoreductase. This enzyme participates in alkaloid biosynthesis i.

In enzymology, a (2,3-dihydroxybenzoyl)adenylate synthase () is an enzyme that catalyzes the chemical reaction :ATP + 2,3-dihydroxybenzoate \rightleftharpoons diphosphate + (2,3-dihydroxybenzoyl)adenylate Thus, the two substrates of this enzyme are ATP and 2,3-dihydroxybenzoate, whereas its two products are diphosphate and (2,3-dihydroxybenzoyl)adenylate. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is ATP:2,3-dihydroxybenzoate adenylyltransferase. This enzyme is also called 2,3-dihydroxybenzoate-AMP ligase.

In enzymology, a mevaldate reductase () is an enzyme that catalyzes the chemical reaction :(R)-mevalonate + NAD+ \rightleftharpoons mevaldate + NADH + H+ Thus, the two substrates of this enzyme are (R)-mevalonate and NAD+, whereas its 3 products are mevaldate, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (R)-mevalonate:NAD+ oxidoreductase. This enzyme is also called mevalonic dehydrogenase.

In enzymology, an AMP—thymidine kinase () is an enzyme that catalyzes the chemical reaction :AMP + thymidine \rightleftharpoons adenosine + thymidine 5'-phosphate Thus, the two substrates of this enzyme are AMP and thymidine, whereas its two products are adenosine and thymidine 5'-phosphate. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is AMP:thymidine 5'-phosphotransferase. This enzyme is also called adenylate-nucleoside phosphotransferase.

In enzymology, an alpha,alpha-trehalose phosphorylase () is an enzyme that catalyzes the chemical reaction :alpha,alpha-trehalose + phosphate \rightleftharpoons D-glucose + beta-D-glucose 1-phosphate Thus, the two substrates of this enzyme are trehalose and phosphate, whereas its two products are D-glucose and beta-D-glucose 1-phosphate. This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is alpha,alpha-trehalose:phosphate beta- D-glucosyltransferase. This enzyme is also called trehalose phosphorylase.

CcrM in complex with a dsDNA structure was resolved, showing that the enzyme presents a novel DNA interaction mechanism, opening a bubble in the DNA recognition site (The concerted mechanism of Methyltransferases relies in the flip of the target base), the enzyme interacts with DNA forming an homodimer with differential monomer interactions. CcrM is a highly efficient enzyme capable of methylating a high number of 5'-GANTC-3' sites in low time, however if the enzyme is processive (the enzyme binds to the DNA and methylate several methylation sites before dissociation) or distributive (the enzyme dissociates from DNA after each methylation) it is still in discussion. First reports indicated the second case, however more recent characterisation of CcrM indicate that it is a processive enzyme.

The precursor to asparagine is oxaloacetate. Oxaloacetate is converted to aspartate using a transaminase enzyme. The enzyme transfers the amino group from glutamate to oxaloacetate producing α-ketoglutarate and aspartate. The enzyme asparagine synthetase produces asparagine, AMP, glutamate, and pyrophosphate from aspartate, glutamine, and ATP.

Acetoacetyl-CoA synthase (, NphT7) is an enzyme with systematic name acetyl- CoA:malonyl-CoA C-acetyltransferase (decarboxylating). This enzyme catalyses the following chemical reaction : acetyl-CoA + malonyl-CoA \rightleftharpoons acetoacetyl-CoA + CoA + CO2 The enzyme from the soil bacterium Streptomyces sp. CL190 produces acetoacetyl-CoA.

Mitochondrial intermediate peptidase (, mitochondrial intermediate precursor- processing proteinase, MIP) is an enzyme. This enzyme catalyses the following chemical reaction : Release of an N-terminal octapeptide as second stage of processing of some proteins imported into the mitochondrion This enzyme is a homologue of thimet oligopeptidase.

Stromelysin 2 (, matrix metalloproteinase 10, transin 2, proteoglycanase 2) is an enzyme. This enzyme catalyses the following chemical reaction : Similar to stromelysin 1, but action on collagen types III, IV and V is weak This enzyme belongs to the peptidase family M10 (interstitial collagenase family).

8-oxo-dGDP phosphatase (, NUDT5) is an enzyme with systematic name 8-oxo-dGDP phosphohydrolase. This enzyme catalyses the following chemical reaction : 8-oxo-dGDP + H2O \rightleftharpoons 8-oxo-dGMP + phosphate The enzyme catalyses the hydrolysis of both 8-oxo-dGDP and 8-oxo-GDP.

Protoporphyrinogen IX dehydrogenase (menaquinone) (, HemG) is an enzyme with systematic name protoporphyrinogen IX:menaquinone oxidoreductase. This enzyme catalyses the following chemical reaction : protoporphyrinogen IX + 3 menaquinone \rightleftharpoons protoporphyrin IX + 3 menaquinol This enzyme enables Escherichia coli to synthesize heme in both aerobic and anaerobic environments.

4-methylaminobutanoate oxidase (methylamine-forming) (, mao (gene)) is an enzyme with systematic name 4-methylaminobutanoate methylamidohydrolase. This enzyme catalyses the following chemical reaction : 4-methylaminobutanoate + O2 \+ H2O \rightleftharpoons succinate semialdehyde + methylamine + H2O2 The enzyme participates in the nicotine degradation in soil bacterium Arthrobacter nicotinovorans.

Baicalein 7-O-glucuronosyltransferase (, UBGAT) is an enzyme with systematic name UDP-D-glucuronate:5,6,7-trihydroxyflavone 7-O-glucuronosyltransferase . This enzyme catalyses the following chemical reaction : UDP-D-glucuronate + baicalein \rightleftharpoons UDP + baicalin The enzyme is specific for UDP-D- glucuronate as a sugar donor.

Catalase-peroxidase (, katG (gene)) is an enzyme with systematic name donor:hydrogen-peroxide oxidoreductase. This enzyme catalyses the following chemical reaction # donor + H2O2 oxidized donor + 2 H2O # 2 H2O2 O2 \+ 2 H2O This enzyme is a strong catalase with H2O2 as donor which releases O2.

Pentalenic acid synthase (, CYP105D7, sav7469 (gene)) is an enzyme with systematic name 1-deoxypentalenate,reduced ferredoxin:O2 oxidoreductase. This enzyme catalyses the following chemical reaction : 1-deoxypentalenate + reduced ferredoxin + O2 \rightleftharpoons pentalenate + oxidized ferredoxin + H2O Pentalenic acid synthase is a heme-thiolate enzyme (P-450).

Terpentetriene synthase (, Cyc2) is an enzyme with systematic name terpentedienyl-diphosphate diphosphate-lyase (terpentetriene-forming). This enzyme catalyses the following chemical reaction : terpentedienyl diphosphate \rightleftharpoons terpentetriene + diphosphate This enzyme requires Mg2+ for maximal activity but can use Mn2+, Fe2+ or Co2+ to a lesser extent.

Tryptophan synthase (indole-salvaging) (, tryptophan synthase beta2) is an enzyme with systematic name L-serine hydro-lyase (adding indole, L-tryptophan- forming). This enzyme catalyses the following chemical reaction : L-serine + indole \rightleftharpoons L-tryptophan + H2O This enzyme salvages the lost indole to L-tryptophan.

Thujopsene synthase () is an enzyme with systematic name (2E,6E)-farnesyl diphosphate lyase (cyclizing, (+)-thujopsene-forming). This enzyme catalyses the following chemical reaction : (2E,6E)-farnesyl diphosphate \rightleftharpoons (+)-thujopsene + diphosphate The recombinant enzyme from the plant Arabidopsis thaliana produces (+)-alpha-barbatene, (+)-thujopsene and (+)-beta-chamigrene.

Alpha-longipinene synthase () is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate diphosphate-lyase (alpha-longipinene-forming). This enzyme catalyses the following chemical reaction : (2E,6E)-farnesyl diphosphate \rightleftharpoons alpha-longipinene + diphosphate The enzyme from Norway spruce produces longifolene as the main product.

Beta-santalene synthase () is an enzyme with systematic name (2E,6E)-farnesyl diphosphate lyase (cyclizing, (-)-beta-santalene-forming). This enzyme catalyses the following chemical reaction : (2E,6E)-farnesyl diphosphate \rightleftharpoons (-)-beta-santalene + diphosphate The enzyme synthesizes a mixture of sesquiterpenoids from (2E,6E)-farnesyl diphosphate.

Alpha-muurolene synthase (, Cop3) is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate diphosphate-lyase (cyclizing, alpha-muurolene- forming). This enzyme catalyses the following chemical reaction : (2E,6E)-farnesyl diphosphate \rightleftharpoons alpha-muurolene + diphosphate The enzyme has been characterized from the fungus Coprinus cinereus.

Gamma-muurolene synthase (, Cop3) is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate diphosphate-lase (cyclizing, gamma-muurolene- forming). This enzyme catalyses the following chemical reaction : (2E,6E)-farnesyl diphosphate \rightleftharpoons gamma-muurolene + diphosphate The enzyme has been characterized from the fungus Coprinus cinereus.

Beta-copaene synthase (, cop4) is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate diphosphate-lyase (cyclizing, beta-copaene- forming). This enzyme catalyses the following chemical reaction : (2E,6E)-farnesyl diphosphate \rightleftharpoons beta-copaene + diphosphate This enzyme is isolated from the fungus Coprinus cinereus.

Tricyclene synthase (, TPS3) is an enzyme with systematic name geranyl- diphosphate diphosphate-lyase (cyclizing; tricyclene-forming). This enzyme catalyses the following chemical reaction : geranyl diphosphate \rightleftharpoons tricyclene + diphosphate The enzyme from Solanum lycopersicum (tomato) gives a mixture of tricyclene, camphene, beta-myrcene and limonene.

Baccharis oxide synthase () is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualene mutase (cyclizing, baccharis-oxide- forming). This enzyme catalyses the following chemical reaction : (3S)-2,3-epoxy-2,3-dihydrosqualene \rightleftharpoons baccharis oxide The enzyme from Stevia rebaudiana also gives traces of other triterpenoids.

Alpha-seco-amyrin synthase () is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualene mutase (cyclizing, alpha-seco-amyrin- forming). This enzyme catalyses the following chemical reaction : (3S)-2,3-epoxy-2,3-dihydrosqualene \rightleftharpoons alpha-seco-amyrin The enzyme from Arabidopsis thaliana is multifunctional.

Beta-seco-amyrin synthase () is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualene mutase (cyclizing, beta-seco-amyrin- forming). This enzyme catalyses the following chemical reaction : (3S)-2,3-epoxy-2,3-dihydrosqualene \rightleftharpoons beta-seco-amyrin The enzyme from Arabidopsis thaliana is multifunctional.

Baruol synthase (, BARS1) is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualene mutase (cyclizing, baruol-forming). This enzyme catalyses the following chemical reaction : (3S)-2,3-epoxy-2,3-dihydrosqualene \rightleftharpoons baruol The enzyme from Arabidopsis thaliana also produces traces of 22 other triterpenoids.

5-exo-hydroxycamphor dehydrogenase (, F-dehydrogenase, FdeH) is an enzyme with systematic name 5-exo-hydroxycamphor:NAD+ oxidoreductase. This enzyme catalyses the following chemical reaction : 5-exo-hydroxycamphor + NAD+ \rightleftharpoons bornane-2,5-dione + NADH + H+ This enzyme contains Zn2+. It is isolated from Pseudomonas putida.

Methylecgonone reductase (, MecgoR (gene name)) is an enzyme with systematic name ecgonine methyl ester:NADP+ oxidoreductase. This enzyme catalyses the following chemical reaction : ecgonine methyl ester + NADP+ \rightleftharpoons ecgonone methyl ester + NADPH + H+ The enzyme from the plant Erythroxylum coca participates in the biosynthesis of cocaine.

Beta-carotene isomerase (, DWARF27 (gene)) is an enzyme with systematic name beta-carotene 9-cis-all-trans isomerase. This enzyme catalyses the following chemical reaction : all-trans-beta-carotene \rightleftharpoons 9-cis-beta- carotene The enzyme participates in a pathway leading to biosynthesis of strigolactones.

23S rRNA pseudouridine2457 synthase (, RluE, YmfC) is an enzyme with systematic name 23S rRNA-uridine2457 uracil mutase. This enzyme catalyses the following chemical reaction : 23S rRNA uridine2457 \rightleftharpoons 23S rRNA pseudouridine2457 The enzyme modifies uridine2457 in a stem of 23S RNA in Escherichia coli.

Capsanthin/capsorubin synthase (, CCS, ketoxanthophyll synthase, capsanthin- capsorubin synthase) is an enzyme with systematic name violaxanthin—capsorubin isomerase (ketone-forming). This enzyme catalyses the following chemical reaction : (1) violaxanthin \rightleftharpoons capsorubin : (2) antheraxanthin \rightleftharpoons capsanthin This multifunctional enzyme is induced during chromoplast differentiation in plants.

Low-specificity L-threonine aldolase (, LtaE) is an enzyme with systematic name L-threonine/L-allo-threonine acetaldehyde-lyase (glycine-forming). This enzyme catalyses the following chemical reaction : (1) L-threonine \rightleftharpoons glycine + acetaldehyde : (2) L-allothreonine \rightleftharpoons glycine + acetaldehyde This enzyme requires pyridoxal phosphate.

Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase () is an enzyme with systematic name ATP:methylphosphonate 5-triphosphoribosyltransferase. This enzyme catalyses the following chemical reaction : ATP + methylphosphonate \rightleftharpoons alpha-D-ribose 1-methylphosphonate 5-triphosphate + adenine This enzyme is isolated from the bacterium Escherichia coli.

Tripeptide aminopeptidase (, tripeptidase, aminotripeptidase, aminoexotripeptidase, lymphopeptidase, imidoendopeptidase, peptidase B, alanine-phenylalanine-proline arylamidase, peptidase T) is an enzyme. This enzyme catalyses the following chemical reaction: : Release of the N-terminal residue from a tripeptide This is a zinc enzyme, widely distributed in mammalian tissues.

Aminopeptidase Ey () is an enzyme. This enzyme catalyses differs from other aminopeptidases in broad specificity for amino acids in the P1 position and the ability to hydrolyse peptides of four or five residues that contain Pro in the P1' position This enzyme is zinc glycoprotein.

An uncompetitive inhibitor cannot bind to the free enzyme, only to the enzyme- substrate complex; hence, these types of inhibitors are most effective at high substrate concentration. In the presence of the inhibitor, the enzyme- substrate complex is inactive. This type of inhibition is rare.

Acetophenone carboxylase () is an enzyme with systematic name acetophenone:carbon-dioxide ligase (ADP-forming). This enzyme catalyses the following chemical reaction : 2 ATP + acetophenone + HCO3− \+ H2O + H+ \rightleftharpoons 2 ADP + 2 phosphate + 3-oxo-3-phenylpropanoate The enzyme is involved in anaerobic degradation of ethylbenzene.

Tetrahydrosarcinapterin synthase (, H4MPT:alpha-L-glutamate ligase, MJ0620, MptN protein) is an enzyme with systematic name tetrahydromethanopterin:alpha- L-glutamate ligase (ADP-forming). This enzyme catalyses the following chemical reaction : ATP + tetrahydromethanopterin + L-glutamate \rightleftharpoons ADP + phosphate + 5,6,7,8-tetrahydrosarcinapterin This enzyme catalyses the biosynthesis of 5,6,7,8-tetrahydrosarcinapterin.

5-phosphoribostamycin phosphatase (, btrP (gene), neoI (gene)) is an enzyme with systematic name 5-phosphoribostamycin phosphohydrolase. This enzyme catalyses the following chemical reaction : 5-phosphoribostamycin + H2O \rightleftharpoons ribostamycin + phosphate This enzyme is involved in the biosynthesis of several aminocyclitol antibiotics, including ribostamycin, neomycin and butirosin.

Deoxyribonuclease (pyrimidine dimer) (, endodeoxyribonuclease (pyrimidine dimer), bacteriophage T4 endodeoxyribonuclease V, T4 endonuclease V) is an enzyme. This enzyme catalyses the following chemical reaction : Endonucleolytic cleavage near pyrimidine dimers to products with 5'-phosphate This enzyme acts on a damaged strand, 5' from the damaged site.

Ribonuclease IV (, endoribonuclease IV, poly(A)-specific ribonuclease) is an enzyme. This enzyme catalyses the following chemical reaction : Endonucleolytic cleavage of poly(A) to fragments terminated by 3'-hydroxy and 5'-phosphate groups This enzyme forms oligonucleotides with an average chain length of 10.

Sclareol cyclase (, geranylgeranyl pyrophosphate:sclareol cyclase, geranylgeranyl pyrophosphate-sclareol cyclase, GGPP:sclareol cyclase) is an enzyme with systematic name geranylgeranyl-diphosphate diphosphohydrolase (sclareol-forming). This enzyme catalyses the following chemical reaction : geranylgeranyl diphosphate + 2 H2O \rightleftharpoons sclareol + diphosphate This enzyme requires Mg2+ or Mn2+ for activity.

Geranyl diphosphate diphosphatase (, geraniol synthase, geranyl pyrophosphate pyrophosphatase, GES, CtGES) is an enzyme with systematic name geranyl- diphosphate diphosphohydrolase. This enzyme catalyses the following chemical reaction : geranyl diphosphate + H2O \rightleftharpoons geraniol + diphosphate This enzyme is isolated from Ocimum basilicum (basil) and Cinnamomum tenuipile (camphor tree).

Exodeoxyribonuclease III (, Escherichia coli exonuclease III, E. coli exonuclease III, endoribonuclease III) is an enzyme. This enzyme catalyses the following chemical reaction : Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates This enzyme has a preference for double-stranded DNA.

Oxalate oxidase （Enzyme Commission number ）occurs mainly in plants. It can degrade oxalic acid into carbon dioxide and hydrogen peroxide. Oxalate decarboxylase (OXDC，) is a kind of oxalate degrading enzyme containing Mn2+,ENZYME entry: EC 4.1.1.2, ExPASy Bioinformatics Resource Portal, accessed 19 March 2017.

Snake venom factor V activator () is an enzyme. This enzyme catalyses the following chemical reaction : Fully activates human clotting factor V by a single cleavage at the Trp-Tyr-Leu-Arg1545-Ser-Asn-Asn-Gly bond. This enzyme is present in venom of Vipera russelli.

Ananain (, stem bromelain, fruit bromelain) is an enzyme. This enzyme catalyses the following chemical reaction : Hydrolysis of proteins with broad specificity for peptide bonds. Best reported small molecule substrate Bz-Phe- Val-Arg-NHMec This enzyme is isolated from stem of pineapple plant, Ananas comosus.

The enzyme phosphorylase kinase plays a role in phosphorylating glycogen phosphorylase to activate it and another enzyme, protein phosphatase-1, inactivates glycogen phosphorylase through dephosphorylation.

The specific activity of an enzyme is another common unit. This is the activity of an enzyme per milligram of total protein (expressed in μmol min−1 mg−1). Specific activity gives a measurement of enzyme purity in the mixture. It is the micro moles of product formed by an enzyme in a given amount of time (minutes) under given conditions per milligram of total proteins.

In enzymology, a choline-sulfatase () is an enzyme that catalyzes the chemical reaction :choline sulfate + H2O \rightleftharpoons choline + sulfate Thus, the two substrates of this enzyme are choline sulfate and H2O, whereas its two products are choline and sulfate. This enzyme belongs to the family of hydrolases, specifically those acting on sulfuric ester bonds. The systematic name of this enzyme class is choline-sulfate sulfohydrolase.

In enzymology, a S-succinylglutathione hydrolase () is an enzyme that catalyzes the chemical reaction :S-succinylglutathione + H2O \rightleftharpoons glutathione + succinate Thus, the two substrates of this enzyme are S-succinylglutathione and H2O, whereas its two products are glutathione and succinate. This enzyme belongs to the family of hydrolases, specifically those acting on thioester bonds. The systematic name of this enzyme class is S-succinylglutathione hydrolase.

In enzymology, a sugar-phosphatase () is an enzyme that catalyzes the chemical reaction :sugar phosphate + H2O \rightleftharpoons sugar + phosphate Thus, the two substrates of this enzyme are sugar phosphate and H2O, whereas its two products are sugar and phosphate. This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name of this enzyme class is sugar-phosphate phosphohydrolase.

In enzymology, a monomethyl-sulfatase () is an enzyme that catalyzes the chemical reaction :monomethyl sulfate + H2O \rightleftharpoons methanol + sulfate Thus, the two substrates of this enzyme are monomethyl sulfate and H2O, whereas its two products are methanol and sulfate. This enzyme belongs to the family of hydrolases, specifically those acting on sulfuric ester bonds. The systematic name of this enzyme class is monomethyl-sulfate sulfohydrolase.

In enzymology, a phenylacetyl-CoA hydrolase () is an enzyme that catalyzes the chemical reaction :phenylglyoxylyl-CoA + H2O \rightleftharpoons phenylglyoxylate + CoA Thus, the two substrates of this enzyme are phenylglyoxylyl-CoA and H2O, whereas its two products are phenylglyoxylate and CoA. This enzyme belongs to the family of hydrolases, specifically those acting on thioester bonds. The systematic name of this enzyme class is phenylglyoxylyl-CoA hydrolase.

In enzymology, a bile-acid-CoA hydrolase () is an enzyme that catalyzes the chemical reaction :deoxycholoyl-CoA + H2O \rightleftharpoons CoA + deoxycholate Thus, the two substrates of this enzyme are deoxycholoyl-CoA and H2O, whereas its two products are CoA and deoxycholate. This enzyme belongs to the family of hydrolases, specifically those acting on thioester bonds. The systematic name of this enzyme class is deoxycholoyl-CoA hydrolase.

In enzymology, an acetylpyruvate hydrolase () is an enzyme that catalyzes the chemical reaction :acetylpyruvate + H2O \rightleftharpoons acetate + pyruvate Thus, the two substrates of this enzyme are acetylpyruvate and H2O, whereas its two products are acetate and pyruvate. This enzyme belongs to the family of hydrolases, specifically those acting on carbon-carbon bonds in ketonic substances. The systematic name of this enzyme class is 2,4-dioxopentanoate acetylhydrolase.

They succeeded in detecting the enzyme activity from the microsomal fraction. This was the crucial step in the serendipitous discovery of lysosomes. To estimate this enzyme activity, they used that of the standardized enzyme acid phosphatase and found that the activity was only 10% of the expected value. One day, the enzyme activity of purified cell fractions which had been refrigerated for five days was measured.

D-arabitol-phosphate dehydrogenase (, APDH, D-arabitol 1-phosphate dehydrogenase, D-arabitol 5-phosphate dehydrogenase) is an enzyme with systematic name D-arabitol-phosphate:NAD+ oxidoreductase. This enzyme catalyses the following chemical reaction : D-arabitol 1-phosphate + NAD+ \rightleftharpoons D-xylulose 5-phosphate + NADH + H+ This enzyme participates in arabitol catabolism. The enzyme also converts D-arabitol 5-phosphate to D-ribulose 5-phosphate at a lower rate.

Acetolactate synthase is catalytic enzyme involved in the biosynthesis of various amino acids. This enzyme has the Enzyme Commission Code is 2.2.1.6, which means that the enzyme is a transketolase or a transaldolase, which is classified under the transferases that transfer aldehyde or ketone residues. In this case, acetolactase synthase is a transketolase, which moves back and forth, having both catabolic and anabolic forms.

Enzyme kinetics is the investigation of how enzymes bind substrates and turn them into products. The rate data used in kinetic analyses are commonly obtained from enzyme assays. In 1913 Leonor Michaelis and Maud Leonora Menten proposed a quantitative theory of enzyme kinetics, which is referred to as Michaelis–Menten kinetics.; The major contribution of Michaelis and Menten was to think of enzyme reactions in two stages.

Cyanophycinase (, cyanophycin degrading enzyme, beta-Asp-Arg hydrolysing enzyme, CGPase, CphB, CphE, cyanophycin granule polypeptidase, extracellular CGPase) is an enzyme. It catalyses the following chemical reaction : [L-Asp(4-L-Arg)]n \+ H2O \rightleftharpoons [L-Asp(4-L-Arg)]n-1 \+ L-Asp(4-L-Arg) The enzyme is highly specific for the branched polypeptide cyanophycin. It is similar to Dipeptidase E, another S51 family serine protease.

This enzyme belongs to the family of transferases, specifically acyltransferases that convert acyl groups into alkyl groups on transfer. The systematic name of this enzyme class is acetyl-CoA:glyoxylate C-acetyltransferase (thioester-hydrolysing, carboxymethyl-forming). Other names in common use include L-malate glyoxylate-lyase (CoA-acetylating), glyoxylate transacetylase, glyoxylate transacetase, glyoxylic transacetase, malate condensing enzyme, malate synthetase, malic synthetase, and malic- condensing enzyme.

In enzymology, an ent-copalyl diphosphate synthase () is an enzyme that catalyzes the chemical reaction: The partial cyclization of geranylgeranyl pyrophosphate to ent-copalyl pyrophosphate is catalyzed by ent-copalyl diphosphate synthase. Hence, this enzyme has one substrate, geranylgeranyl pyrophosphate, and one product, ent-copalyl pyrophosphate. This enzyme participates in gibberellin biosynthesis. This enzyme belongs to the family of isomerases, specifically the class of intramolecular lyases.

In enzymology, a methionine racemase () is an enzyme that catalyzes the chemical reaction :L-methionine \rightleftharpoons D-methionine Hence, this enzyme has one substrate, L-methionine, and one product, D-methionine. This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on amino acids and derivatives. The systematic name of this enzyme class is methionine racemase. It employs one cofactor, pyridoxal phosphate.

General asparagine self-cleaving mechanism in asparagine peptide lyases These enzymes are synthesized as precursors or propeptides, which cleave themselves by an autoproteolytic reaction. The self-cleaving nature of asparagine peptide lyases contradicts the general definition of an enzyme given that the enzymatic activity destroys the enzyme. However, the self-processing is the action of a proteolytic enzyme, notwithstanding the enzyme is not recoverable from the reaction.

In enzymology, a DNA beta-glucosyltransferase () is an enzyme that catalyzes the chemical reaction in which a beta-D-glucosyl residue is transferred from UDP-glucose to an hydroxymethylcytosine residue in DNA. It is analogous to the enzyme DNA alpha-glucosyltransferase. This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-glucose:DNA beta-D-glucosyltransferase.

In enzymology, a limonoid glucosyltransferase () is an enzyme that catalyzes the chemical reaction :UDP-glucose + limonin \rightleftharpoons glucosyl- limonin + UDP Thus, the two substrates of this enzyme are UDP-glucose and limonin, whereas its two products are glucosyl-limonin and UDP. This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is uridine diphosphoglucose-limonoid glucosyltransferase.

Citrus juice inhibits the enzyme only within the intestines if consumed in small amounts. Intestinal enzyme inhibition will only affect the potency of orally administrated drugs. When larger amounts are consumed they may also inhibit the enzyme in the liver. The hepatic enzyme inhibition may cause an additional increase in potency and a prolonged metabolic half-life (prolonged metabolic half-life for all ways of drug administration).

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is ribitol:NAD+ 2-oxidoreductase. Other names in common use include adonitol dehydrogenase, ribitol dehydrogenase A (wild type), ribitol dehydrogenase B (mutant enzyme with different properties), and ribitol dehydrogenase D (mutant enzyme with different properties).

Folylpolyglutamate synthase, mitochondrial is an enzyme that in humans is encoded by the FPGS gene. This gene encodes the folylpolyglutamate synthetase enzyme. This enzyme has a central role in establishing and maintaining both cytosolic and mitochondrial folylpolyglutamate concentrations and, therefore, is essential for folate homeostasis and the survival of proliferating cells. This enzyme catalyzes the ATP-dependent addition of glutamate moieties to folate and folate derivatives.

Zinc D-Ala-D-Ala carboxypeptidase (, Zn2+ G peptidase, D-alanyl-D-alanine hydrolase, D-alanyl-D-alanine-cleaving carboxypeptidase, DD-carboxypeptidase, G enzyme, DD-carboxypeptidase-transpeptidase) is an enzyme. This enzyme catalyses the following chemical reaction : Cleavage of the bond: (Ac)2-L-lysyl-D-alanyl--D-alanine This is a zinc enzyme. Catalyses carboxypeptidation but not transpeptidation reactions involved in bacterial cell wall metabolism.

The secretin-induced rapid flow of water results in lower and often unreliable enzyme concentrations. CCK also induces gallbladder contraction and the release of bile, which may further dilute enzyme concentrations. As a result, the quantification of total enzyme output (units/min) must be determined through continuous collection of duodenal fluid with or without the use of perfusion markers. Measurement of more than one enzyme (i.e.

In enzymology, an arabinonate dehydratase () is an enzyme that catalyzes the chemical reaction :D-arabinonate \rightleftharpoons 2-dehydro-3-deoxy-D- arabinonate + H2O Hence, this enzyme has one substrate, D-arabinonate, and two products, 2-dehydro-3-deoxy-D-arabinonate and H2O. This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is D-arabinonate hydro-lyase (2-dehydro-3-deoxy-D-arabinonate-forming). This enzyme is also called D-arabinonate hydro-lyase.

In enzymology, a D-glutamate cyclase () is an enzyme that catalyzes the chemical reaction :D-glutamate \rightleftharpoons 5-oxo-D-proline + H2O Hence, this enzyme has one substrate, D-glutamate, and two products, 5-oxo-D-proline and H2O. This enzyme belongs to the family of lyases, specifically the hydro- lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is D-glutamate hydro-lyase (cyclizing; 5-oxo-D-proline-forming). This enzyme is also called D-glutamate hydro-lyase (cyclizing).

In enzymology, a galactarate dehydratase () is an enzyme that catalyzes the chemical reaction :D-galactarate \rightleftharpoons 5-dehydro-4-deoxy-D- glucarate + H2O Hence, this enzyme has one substrate, D-galactarate, and two products, 5-dehydro-4-deoxy-D-glucarate and H2O. This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is D-galactarate hydro-lyase (5-dehydro-4-deoxy-D-glucarate-forming). This enzyme is also called D-galactarate hydro-lyase.

In enzymology, a carnitine dehydratase () is an enzyme that catalyzes the chemical reaction :L-carnitine \rightleftharpoons 4-(trimethylammonio)but-2-enoate + H2O Hence, this enzyme has one substrate, L-carnitine, and two products, 4-(trimethylammonio)but-2-enoate and H2O. This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is L-carnitine hydro-lyase [4-(trimethylammonio)but-2-enoate-forming]. This enzyme is also called L-carnitine hydro-lyase.

In enzymology, an altronate dehydratase () is an enzyme that catalyzes the chemical reaction :D-altronate \rightleftharpoons 2-dehydro-3-deoxy-D- gluconate + H2O Hence, this enzyme has one substrate, D-altronate, and two products, 2-dehydro-3-deoxy-D-gluconate and H2O. This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is D-altronate hydro-lyase (2-dehydro-3-deoxy-D-gluconate-forming). This enzyme is also called D-altronate hydro-lyase.

However, CLECs have an inherent disadvantage: enzyme crystallization is a laborious procedure requiring enzyme of high purity, which translates to prohibitively high costs. The more recently developed cross-linked enzyme aggregates (CLEAs), on the other hand, are produced by simple precipitation of the enzyme from aqueous solution, as physical aggregates of protein molecules, by the addition of salts, or water miscible organic solvents or non-ionic polymers.Sheldon, R.A.; Schoevaart, R.; van Langen, L.; A novel method for enzyme immobilization; Biocat. Biotrans, 2005, 23(3/4), 141-147.

In enzymology, an iron-chelate-transporting ATPase () is an enzyme that catalyzes the chemical reaction :ATP + H2O + iron chelateout \rightleftharpoons ADP + phosphate + iron chelatein The 3 substrates of this enzyme are ATP, H2O, and iron chelate, whereas its 3 products are ADP, phosphate, and iron chelate. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (iron-chelate-importing). This enzyme participates in abc transporters - general.

In enzymology, a manganese-transporting ATPase () is an enzyme that catalyzes the chemical reaction :ATP + H2O + Mn2+out \rightleftharpoons ADP + phosphate + Mn2+in The 3 substrates of this enzyme are ATP, H2O, and Mn2+, whereas its 3 products are ADP, phosphate, and Mn2+. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is called ATP phosphohydrolase (manganese-importing). This enzyme is also known as ABC-type manganese permease complex.

In enzymology, a teichoic-acid-transporting ATPase () is an enzyme that catalyzes the chemical reaction :ATP + H2O + teichoic acidin \rightleftharpoons ADP + phosphate + teichoic acidout The 3 substrates of this enzyme are ATP, H2O, and teichoic acid, whereas its 3 products are ADP, phosphate, and teichoic acid. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (teichoic-acid-exporting). This enzyme participates in abc transporters - general.

In enzymology, a vitamin B12-transporting ATPase () is an enzyme that catalyzes the chemical reaction :ATP + H2O + vitamin B12out \rightleftharpoons ADP + phosphate + vitamin B12in The 3 substrates of this enzyme are ATP, H2O, and vitamin B12, whereas its 3 products are ADP, phosphate, and vitamin B12. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (vitamin B12-importing). This enzyme participates in abc transporters - general.

In enzymology, a quaternary-amine-transporting ATPase () is an enzyme that catalyzes the chemical reaction :ATP + H2O + quaternary amineout \rightleftharpoons ADP + phosphate + quaternary aminein The 3 substrates of this enzyme are ATP, H2O, and quaternary amine, whereas its 3 products are ADP, phosphate, and quaternary amine. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (quaternary-amine-importing). This enzyme participates in abc transporters - general.

In enzymology, a dolichylphosphate-mannose phosphodiesterase () is an enzyme that catalyzes the chemical reaction :dolichyl beta-D-mannosyl phosphate + H2O \rightleftharpoons dolichyl phosphate + D-mannose Thus, the two substrates of this enzyme are dolichyl beta-D-mannosyl phosphate and H2O, whereas its two products are dolichyl phosphate and D-mannose. This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric diester bonds. The systematic name of this enzyme class is dolichyl-beta-D-mannosyl-phosphate dolichylphosphohydrolase. This enzyme is also called mannosylphosphodolichol phosphodiesterase.

In enzymology, a glucose-1-phosphatase () is an enzyme that catalyzes the chemical reaction :alpha-D-glucose 1-phosphate + H2O \rightleftharpoons D-glucose + phosphate Thus, the two substrates of this enzyme are alpha-D- glucose 1-phosphate and H2O, whereas its two products are D-glucose and phosphate. This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name of this enzyme class is alpha-D-glucose-1-phosphate phosphohydrolase. This enzyme participates in glycolysis and gluconeogenesis.

In enzymology, an ADP-phosphoglycerate phosphatase () is an enzyme that catalyzes the chemical reaction :3-(ADP)-2-phosphoglycerate + H2O \rightleftharpoons 3-(ADP)-glycerate + phosphate Thus, the two substrates of this enzyme are 3-(ADP)-2-phosphoglycerate and H2O, whereas its two products are 3-(ADP)-glycerate and phosphate. This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name of this enzyme class is 3-(ADP)-2-phosphoglycerate phosphohydrolase. This enzyme is also called adenosine diphosphate phosphoglycerate phosphatase.

In enzymology, an all-trans-retinyl-palmitate hydrolase () is an enzyme that catalyzes the chemical reaction :all-trans-retinyl palmitate + H2O \rightleftharpoons all-trans-retinol + palmitate Thus, the two substrates of this enzyme are all-trans-retinyl palmitate and H2O, whereas its two products are all-trans-retinol and palmitate. This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is all-trans-retinyl-palmitate acylhydrolase. This enzyme participates in retinol metabolism.

In enzymology, a choline sulfotransferase () is an enzyme that catalyzes the chemical reaction :3'-phosphoadenylyl sulfate + choline \rightleftharpoons adenosine 3',5'-bisphosphate + choline sulfate Thus, the two substrates of this enzyme are 3'-phosphoadenylyl sulfate and choline, whereas its two products are adenosine 3',5'-bisphosphate and choline sulfate. This enzyme belongs to the family of transferases, specifically the sulfotransferases, which transfer sulfur-containing groups. The systematic name of this enzyme class is 3'-phosphoadenylyl-sulfate:choline sulfotransferase. This enzyme is also called choline sulphokinase.

In enzymology, a D-alanine 2-hydroxymethyltransferase () is an enzyme that catalyzes the chemical reaction :5,10-methylenetetrahydrofolate + D-alanine + H2O \rightleftharpoons tetrahydrofolate + 2-methylserine The 3 substrates of this enzyme are 5,10-methylenetetrahydrofolate, D-alanine, and H2O, whereas its two products are tetrahydrofolate and 2-methylserine. This enzyme belongs to the family of transferases that transfer one-carbon groups, specifically the hydroxymethyl-, formyl- and related transferases. The systematic name of this enzyme class is 5,10-methylenetetrahydrofolate:D-alanine 2-hydroxymethyltransferase. This enzyme is also called 2-methylserine hydroxymethyltransferase.

In enzymology, a 4-chlorobenzoyl-CoA dehalogenase () is an enzyme that catalyzes the chemical reaction :4-chlorobenzoyl-CoA + H2O \rightleftharpoons 4-hydroxybenzoyl CoA + chloride Thus, the two substrates of this enzyme are 4-chlorobenzoyl-CoA and H2O, whereas its two products are 4-hydroxybenzoyl CoA and chloride. This enzyme belongs to the family of hydrolases, specifically those acting on halide bonds in carbon-halide compounds. The systematic name of this enzyme class is 4-chlorobenzoyl CoA chlorohydrolase. This enzyme participates in 2,4-dichlorobenzoate degradation.

In enzymology, a 4-chlorobenzoate—CoA ligase () is an enzyme that catalyzes the chemical reaction :4-chlorobenzoate + CoA + ATP \rightleftharpoons 4-chlorobenzoyl-CoA + AMP + diphosphate The 3 substrates of this enzyme are 4-chlorobenzoate, CoA, and ATP, whereas its 3 products are 4-chlorobenzoyl- CoA, AMP, and diphosphate. This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The systematic name of this enzyme class is 4-chlorobenzoate:CoA ligase. This enzyme participates in 2,4-dichlorobenzoate degradation.

In enzymology, a glutamate-methylamine ligase () is an enzyme that catalyzes the chemical reaction :ATP + L-glutamate + methylamine \rightleftharpoons ADP + phosphate + N5-methyl-L-glutamine The 3 substrates of this enzyme are ATP, L-glutamate, and methylamine, whereas its 3 products are ADP, phosphate, and N5-methyl-L-glutamine. This enzyme belongs to the family of ligases, specifically those forming generic carbon-nitrogen bonds. The systematic name of this enzyme class is L-glutamate:methylamine ligase (ADP-forming). This enzyme is also called gamma-glutamylmethylamide synthetase.

In enzymology, a fucosterol-epoxide lyase () is an enzyme that catalyzes the chemical reaction :(24R,24'R)-fucosterol epoxide \rightleftharpoons desmosterol + acetaldehyde Hence, this enzyme has one substrate, (24R,24'R)-fucosterol epoxide, and two products, desmosterol and acetaldehyde. This enzyme belongs to the family of lyases, specifically the aldehyde-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is (24R,24'R)-fucosterol-epoxide acetaldehyde-lyase (desmosterol-forming). This enzyme is also called (24R,24'R)-fucosterol-epoxide acetaldehyde-lyase.

9,12-octadecadienoate 8-hydroperoxide 8R-isomerase (, 5,8-LDS (bifunctional enzyme), 5,8-linoleate diol synthase (bifunctional enzyme), 8-hydroperoxide isomerase, (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate mutase ((5S,8R,9Z,12Z)-5,8-dihydroxy-9,12-octadecadienoate-forming), PpoA) is an enzyme with systematic name (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate hydroxymutase ((5S,8R,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoate-forming). This enzyme catalyses the following chemical reaction : (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate \rightleftharpoons (5S,8R,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoate This enzyme contains heme.

In enzymology, a difructose-anhydride synthase () is an enzyme that catalyzes the chemical reaction :bis-D-fructose 2',1:2,1'-dianhydride + H2O \rightleftharpoons inulobiose Thus, the two substrates of this enzyme are bis- D-fructose 2',1:2,1'-dianhydride and H2O, whereas its product is inulobiose. This enzyme belongs to the family of hydrolases, specifically those glycosidases that hydrolyse O- and S-glycosyl compounds. The systematic name of this enzyme class is bis-D-fructose 2',1:2,1'-dianhydride fructohydrolase. This enzyme is also called inulobiose hydrolase.

In enzymology, a pterin deaminase () is an enzyme that catalyzes the chemical reaction :2-amino-4-hydroxypteridine + H2O \rightleftharpoons 2,4-dihydroxypteridine + NH3 Thus, the two substrates of this enzyme are 2-amino-4-hydroxypteridine and H2O, whereas its two products are 2,4-dihydroxypteridine and NH3. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is 2-amino-4-hydroxypteridine aminohydrolase. This enzyme is also called acrasinase.

In enzymology, a N-substituted formamide deformylase () is an enzyme that catalyzes the chemical reaction :N-benzylformamide + H2O \rightleftharpoons formate + benzylamine Thus, the two substrates of this enzyme are N-benzylformamide and H2O, whereas its two products are formate and benzylamine. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N-benzylformamide amidohydrolase and is also called NfdA. The enzyme is produced by Arthrobacter pascens bacteria.

In enzymology, an amidinoaspartase () is an enzyme that catalyzes the chemical reaction :N-amidino-L-aspartate + H2O \rightleftharpoons L-aspartate + urea Thus, the two substrates of this enzyme are N-amidino-L-aspartate and H2O, whereas its two products are L-aspartate and urea. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amidines. The systematic name of this enzyme class is N-amidino-L-aspartate amidinohydrolase. This enzyme is also called amidinoaspartic amidinohydrolase.

In enzymology, a D-glutaminase () is an enzyme that catalyzes the chemical reaction :D-glutamine + H2O \rightleftharpoons D-glutamate + NH3 Thus, the two substrates of this enzyme are D-glutamine and H2O, whereas its two products are D-glutamate and NH3. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is D-glutamine amidohydrolase. This enzyme participates in d-glutamine and d-glutamate metabolism and nitrogen metabolism.

In enzymology, a formyltetrahydrofolate deformylase () is an enzyme that catalyzes the chemical reaction :10-formyltetrahydrofolate + H2O \rightleftharpoons formate + tetrahydrofolate Thus, the two substrates of this enzyme are 10-formyltetrahydrofolate and H2O, whereas its two products are formate and tetrahydrofolate. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is 10-formyltetrahydrofolate amidohydrolase. This enzyme participates in glyoxylate and dicarboxylate metabolism and one carbon pool by folate.

In enzymology, an anthranilate N-methyltransferase () is an enzyme that catalyzes the chemical reaction :S-adenosyl-L-methionine + anthranilate \rightleftharpoons S-adenosyl-L-homocysteine + N-methylanthranilate Thus, the two substrates of this enzyme are S-adenosyl methionine and anthranilate, whereas its two products are S-adenosylhomocysteine and N-methylanthranilate. This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:anthranilate N-methyltransferase. This enzyme is also called anthranilic acid N-methyltransferase.

In enzymology, a quinaldate 4-oxidoreductase () is an enzyme that catalyzes the chemical reaction :quinaldate + acceptor + H2O \rightleftharpoons kynurenate + reduced acceptor The 3 substrates of this enzyme are quinaldate, acceptor, and H2O, whereas its two products are kynurenate and reduced acceptor. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with other acceptors. The systematic name of this enzyme class is quinoline-2-carboxylate:acceptor 4-oxidoreductase (hydroxylating). This enzyme is also called quinaldic acid 4-oxidoreductase.

In enzymology, a cyclohexanone dehydrogenase () is an enzyme that catalyzes a chemical reaction :cyclohexanone + acceptor \rightleftharpoons cyclohex-2-enone + reduced acceptor Thus, the two substrates of this enzyme are cyclohexanone and acceptor, whereas its two products are cyclohex-2-enone and reduced acceptor. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with other acceptors. The systematic name of this enzyme class is cyclohexanone:acceptor 2-oxidoreductase. This enzyme is also called cyclohexanone:(acceptor) 2-oxidoreductase.

In enzymology, a biochanin-A reductase () is an enzyme that catalyzes the chemical reaction :dihydrobiochanin A + NADP+ \rightleftharpoons biochanin A + NADPH + H+ Thus, the two substrates of this enzyme are dihydrobiochanin A and NADP+, whereas its 3 products are biochanin A, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH- CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is dihydrobiochanin-A:NADP+ Delta2-oxidoreductase. This enzyme participates in isoflavonoid biosynthesis.

In enzymology, a putrescine N-methyltransferase () is an enzyme that catalyzes the chemical reaction :S-adenosyl-L-methionine + putrescine \rightleftharpoons S-adenosyl-L-homocysteine + N-methylputrescine Thus, the two substrates of this enzyme are S-adenosyl methionine and putrescine, whereas its two products are S-adenosylhomocysteine and N-methylputrescine. This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L- methionine:putrescine N-methyltransferase. This enzyme is also called putrescine methyltransferase.

In enzymology, a pyridine N-methyltransferase () is an enzyme that catalyzes the chemical reaction :S-adenosyl-L-methionine + pyridine \rightleftharpoons S-adenosyl-L-homocysteine + N-methylpyridinium Thus, the two substrates of this enzyme are S-adenosyl methionine and pyridine, whereas its two products are S-adenosylhomocysteine and N-methylpyridinium. This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L- methionine:pyridine N-methyltransferase. This enzyme is also called pyridine methyltransferase.

In enzymology, a 1-alkenylglycerophosphocholine O-acyltransferase () is an enzyme that catalyzes the chemical reaction :acyl-CoA + 1-alkenylglycerophosphocholine \rightleftharpoons CoA + 1-alkenyl-2-acylglycerophosphocholine Thus, the two substrates of this enzyme are acyl-CoA and 1-alkenylglycerophosphocholine, whereas its two products are CoA and 1-alkenyl-2-acylglycerophosphocholine. This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acyl-CoA:1-alkenylglycerophosphocholine O-acyltransferase. This enzyme participates in ether lipid metabolism.

In enzymology, a 1-alkenylglycerophosphoethanolamine O-acyltransferase () is an enzyme that catalyzes the chemical reaction :acyl-CoA + 1-alkenylglycerophosphoethanolamine \rightleftharpoons CoA + 1-alkenyl-2-acylglycerophosphoethanolamine Thus, the two substrates of this enzyme are acyl-CoA and 1-alkenylglycerophosphoethanolamine, whereas its two products are CoA and 1-alkenyl-2-acylglycerophosphoethanolamine. This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acyl-CoA:1-alkenylglycerophosphoethanolamine O-acyltransferase. This enzyme participates in ether lipid metabolism.

In enzymology, a 10-deacetylbaccatin III 10-O-acetyltransferase () is an enzyme that catalyzes the chemical reaction :acetyl-CoA + 10-deacetylbaccatin III \rightleftharpoons CoA + baccatin III Thus, the two substrates of this enzyme are acetyl-CoA and 10-deacetylbaccatin III, whereas its two products are CoA and baccatin III. This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acetyl-CoA:taxan-10beta-ol O-acetyltransferase. This enzyme participates in diterpenoid biosynthesis.

In enzymology, a D-4-hydroxyphenylglycine transaminase () is an enzyme that catalyzes the chemical reaction :D-4-hydroxyphenylglycine + 2-oxoglutarate \rightleftharpoons 4-hydroxyphenylglyoxylate + L-glutamate Thus, the two substrates of this enzyme are D-4-hydroxyphenylglycine and 2-oxoglutarate, whereas its two products are 4-hydroxyphenylglyoxylate and L-glutamate. This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is D-4-hydroxyphenylglycine:2-oxoglutarate aminotransferase. This enzyme is also called D-hydroxyphenylglycine aminotransferase.

In enzymology, a tryptophan-phenylpyruvate transaminase () is an enzyme that catalyzes the chemical reaction :L-tryptophan + phenylpyruvate \rightleftharpoons (indol-3-yl)pyruvate + L-phenylalanine Thus, the two substrates of this enzyme are L-tryptophan and phenylpyruvate, whereas its two products are (indol-3-yl)pyruvate and L-phenylalanine. This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-tryptophan:phenylpyruvate aminotransferase. This enzyme is also called L-tryptophan-alpha-ketoisocaproate aminotransferase.

In enzymology, a formaldehyde transketolase () is an enzyme that catalyzes the chemical reaction :D-xylulose 5-phosphate + formaldehyde \rightleftharpoons glyceraldehyde 3-phosphate + glycerone Thus, the two substrates of this enzyme are D-xylulose 5-phosphate and formaldehyde, whereas its two products are glyceraldehyde 3-phosphate and glycerone. This enzyme belongs to the family of transferases, specifically those transferring aldehyde or ketonic groups (transaldolases and transketolases, respectively). The systematic name of this enzyme class is D-xylulose-5-phosphate:formaldehyde glycolaldehydetransferase. This enzyme is also called dihydroxyacetone synthase.

In enzymology, a sulfoacetaldehyde acetyltransferase () is an enzyme that catalyzes the chemical reaction :acetyl phosphate + sulfite \rightleftharpoons 2-sulfoacetaldehyde + phosphate Thus, the two substrates of this enzyme are acetyl phosphate and sulfite, whereas its two products are 2-sulfoacetaldehyde and phosphate. This enzyme belongs to the family of transferases, specifically those acyltransferases that convert acyl groups into alkyl groups on transfer. The systematic name of this enzyme class is acetyl-phosphate:sulfite S-acetyltransferase (acyl-phosphate hydrolysing, 2-oxoethyl-forming). This enzyme is also called Xsc.

In enzymology, a triacylglycerol---sterol O-acyltransferase () is an enzyme that catalyzes the chemical reaction :triacylglycerol + a 3beta-hydroxysterol \rightleftharpoons diacylglycerol + a 3beta-hydroxysterol ester Thus, the two substrates of this enzyme are triacylglycerol and 3beta-hydroxysterol, whereas its two products are diacylglycerol and 3beta-hydroxysterol ester. This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is triacylglycerol:3beta-hydroxysterol O-acyltransferase. This enzyme is also called triacylglycerol:sterol acyltransferase.

In enzymology, a leucine N-acetyltransferase () is an enzyme that catalyzes the chemical reaction :acetyl-CoA + L-leucine \rightleftharpoons CoA + N-acetyl-L-leucine Thus, the two substrates of this enzyme are acetyl-CoA and L-leucine, whereas its two products are CoA and N-acetyl-L-leucine. This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acetyl-CoA:L-leucine N-acetyltransferase. This enzyme is also called leucine acetyltransferase.

In enzymology, an aspulvinone dimethylallyltransferase () is an enzyme that catalyzes the chemical reaction :2 dimethylallyl diphosphate + aspulvinone E \rightleftharpoons 2 diphosphate + aspulvinone H Thus, the two substrates of this enzyme are dimethylallyl diphosphate and aspulvinone E, whereas its two products are diphosphate and aspulvinone H. This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is dimethylallyl- diphosphate:aspulvinone-E dimethylallyltransferase. This enzyme is also called dimethylallyl pyrophosphate:aspulvinone dimethylallyltransferase.

In enzymology, a 3-oxoadipyl-CoA thiolase () is an enzyme that catalyzes the chemical reaction :succinyl-CoA + acetyl-CoA \rightleftharpoons CoA + 3-oxoadipyl-CoA Thus, the two substrates of this enzyme are succinyl-CoA and acetyl-CoA, whereas its two products are CoA and 3-oxoadipyl-CoA. This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is succinyl-CoA:acetyl-CoA C-succinyltransferase. This enzyme participates in benzoate degradation via hydroxylation.

In enzymology, a columbamine oxidase () is an enzyme that catalyzes the chemical reaction :2 columbamine + O2 \rightleftharpoons 2 berberine + 2 H2O Thus, the two substrates of this enzyme are columbamine and O2, whereas its two products are berberine and H2O. This enzyme belongs to the family of oxidoreductases, specifically those acting on X-H and Y-H to form an X-Y bond with oxygen as acceptor. The systematic name of this enzyme class is columbamine:oxygen oxidoreductase (cyclizing). This enzyme is also called berberine synthase.

In enzymology, a phenylacetaldehyde dehydrogenase () is an enzyme that catalyzes the chemical reaction :phenylacetaldehyde + NAD+ \+ H2O \rightleftharpoons phenylacetate + NADH + 2 H+ The 3 substrates of this enzyme are phenylacetaldehyde, NAD+, and H2O, whereas its 3 products are phenylacetate, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is phenylacetaldehyde:NAD+ oxidoreductase. This enzyme participates in phenylalanine metabolism and styrene degradation.

In enzymology, a pyruvate oxidase (CoA-acetylating) () is an enzyme that catalyzes the chemical reaction :pyruvate + CoA + O2 \rightleftharpoons acetyl-CoA + CO2 \+ H2O2 The 3 substrates of this enzyme are pyruvate, CoA, and O2, whereas its 3 products are acetyl-CoA, CO2, and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with oxygen as acceptor. The systematic name of this enzyme class is pyruvate:oxygen 2-oxidoreductase (CoA-acetylating). This enzyme participates in pyruvate metabolism.

In enzymology, a hexose oxidase () is an enzyme that catalyzes the chemical reaction :D-glucose + O2 \rightleftharpoons D-glucono-1,5-lactone + H2O2 Thus, the two substrates of this enzyme are D-glucose and O2, whereas its two products are D-glucono-1,5-lactone and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. The systematic name of this enzyme class is D-hexose:oxygen 1-oxidoreductase. This enzyme participates in pentose phosphate pathway.

In enzymology, a 4-hydroxyphenylpyruvate oxidase () is an enzyme that catalyzes the chemical reaction :4-hydroxyphenylpyruvate + 1/2 O2 \rightleftharpoons 4-hydroxyphenylacetate + CO2 Thus, the two substrates of this enzyme are 4-hydroxyphenylpyruvate and O2, whereas its two products are 4-hydroxyphenylacetate and CO2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with oxygen as acceptor. The systematic name of this enzyme class is 4-hydroxyphenylpyruvate:oxygen oxidoreductase (decarboxylating). This enzyme participates in tyrosine metabolism.

In enzymology, a 6-oxohexanoate dehydrogenase () is an enzyme that catalyzes the chemical reaction :6-oxohexanoate + NADP+ \+ H2O \rightleftharpoons adipate + NADPH + 2 H+ The 3 substrates of this enzyme are 6-oxohexanoate, NADP+, and H2O, whereas its 3 products are adipate, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 6-oxohexanoate:NADP+ oxidoreductase. This enzyme participates in caprolactam degradation.

In enzymology, an aldehyde dehydrogenase (pyrroloquinoline-quinone) () is an enzyme that catalyzes the chemical reaction :an aldehyde + acceptor + H2O \rightleftharpoons a carboxylate + reduced acceptor The 3 substrates of this enzyme are aldehyde, acceptor, and H2O, whereas its two products are carboxylate and reduced acceptor. This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with other acceptors. The systematic name of this enzyme class is aldehyde:(pyrroloquinoline-quinone) oxidoreductase. This enzyme is also called aldehyde dehydrogenase (acceptor).

In enzymology, an ecdysone oxidase () is an enzyme that catalyzes the chemical reaction :ecdysone + O2 \rightleftharpoons 3-dehydroecdysone + H2O2 Thus, the two substrates of this enzyme are ecdysone and O2, whereas its two products are 3-dehydroecdysone and H2O2. This enzyme may or may not belong to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. The systematic name of this enzyme class is ecdysone:oxygen 3-oxidoreductase. This enzyme might also called beta-ecdysone oxidase.

In enzymology, a putrescine oxidase () is an enzyme that catalyzes the chemical reaction :putrescine + O2 \+ H2O \rightleftharpoons 4-aminobutanal + NH3 \+ H2O2 The 3 substrates of this enzyme are putrescine, O2, and H2O, whereas its 3 products are 4-aminobutanal, NH3, and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with oxygen as acceptor. The systematic name of this enzyme class is putrescine:oxygen oxidoreductase (deaminating). This enzyme participates in urea cycle and metabolism of amino groups.

In enzymology, a leghemoglobin reductase () is an enzyme that catalyzes the chemical reaction :NAD(P)H + H+ \+ 2 ferrileghemoglobin \rightleftharpoons NAD(P)+ + 2 ferroleghemoglobin The 4 substrates of this enzyme are NADH, NADPH, H+, and ferrileghemoglobin, whereas its 3 products are NAD+, NADP+, and ferroleghemoglobin. This enzyme belongs to the family of oxidoreductases, specifically those acting on NADH or NADPH with a heme protein as acceptor. The systematic name of this enzyme class is NAD(P)H:ferrileghemoglobin oxidoreductase. This enzyme is also called ferric leghemoglobin reductase.

In enzymology, a vomilenine reductase () is an enzyme that catalyzes the chemical reaction :1,2-dihydrovomilenine + NADP+ \rightleftharpoons vomilenine + NADPH + H+ Thus, the two substrates of this enzyme are 1,2-dihydrovomilenine and NADP+, whereas its 3 products are vomilenine, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH- NH group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 1,2-dihydrovomilenine:NADP+ oxidoreductase. This enzyme participates in indole and ipecac alkaloid biosynthesis.

The condition is inherited in an autosomal recessive pattern: mutated copies of the gene GCDH must be provided by both parents to cause glutaric acidemia type 1. The GCDH gene encodes the enzyme glutaryl-CoA dehydrogenase. This enzyme is involved in degrading the amino acids lysine, hydroxylysine and tryptophan. Mutations in the GCDH' gene prevent production of the enzyme or result in the production of a defective enzyme with very low residual activity, or an enzyme with relatively high residual activity but still phenotypic consequences.

This enzyme belongs to the family of isomerases, specifically the racemases and epimerases which act on other compounds. The systematic name of this enzyme class is 2-methylacyl-CoA 2-epimerase. In vitro experiments with the human enzyme AMACR 1A show that both (2S)- and (2R)-methyldecanoyl- CoA esters are substrates and are converted by the enzyme with very similar efficiency. Prolonged incubation of either substrate with the enzyme establishes an equilibrium with both substrates or products present in a near 1:1 ratio.

In enzymology, a cholestenol Delta-isomerase () is an enzyme that catalyzes the chemical reaction :5alpha-cholest-7-en-3beta-ol \rightleftharpoons 5alpha- cholest-8-en-3beta-ol Hence, this enzyme has one substrate, 5alpha- cholest-7-en-3beta-ol, and one product, 5alpha-cholest-8-en-3beta-ol. This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases transposing C=C bonds. The systematic name of this enzyme class is Delta7-cholestenol Delta7-Delta8-isomerase. This enzyme participates in biosynthesis of steroids.

An endoenzyme, or intracellular enzyme, is an enzyme that functions within the cell in which it was produced. Because the majority of enzymes fall within this category, the term is used primarily to differentiate a specific enzyme from an exoenzyme. It is possible for a single enzyme to have both endoenzymatic and exoenzymatic functions; for example, glycolytic enzymes of Kreb's Cycle. In most cases the term endoenzyme refers to an enzyme that binds to a bond 'within the body' of a large molecule - usually a polymer.

In enzymology, a glucose-6-phosphate 1-epimerase () is an enzyme that catalyzes the chemical reaction :alpha-D-glucose 6-phosphate \rightleftharpoons beta-D-glucose 6-phosphate Hence, this enzyme has one substrate, alpha-D-glucose 6-phosphate, and one product, beta-D-glucose 6-phosphate. This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on carbohydrates and derivatives. The systematic name of this enzyme class is D-glucose-6-phosphate 1-epimerase. This enzyme participates in glycolysis / gluconeogenesis.

In enzymology, a (+)-delta-cadinene synthase () is an enzyme that catalyzes the chemical reaction :2-trans,6-trans-farnesyl diphosphate \rightleftharpoons (+)-delta-cadinene + diphosphate Hence, this enzyme has one substrate, 2-trans,6-trans-farnesyl diphosphate, and two products, (+)-delta-cadinene and diphosphate. This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on phosphates. The systematic name of this enzyme class is 2-trans,6-trans-farnesyl-diphosphate diphosphate-lyase (cyclizing, (+)-delta-cadinene-forming). This enzyme participates in terpenoid biosynthesis.

In enzymology, a serine-sulfate ammonia-lyase () is an enzyme that catalyzes the chemical reaction :L-serine O-sulfate + H2O \rightleftharpoons pyruvate + NH3 \+ sulfate Thus, the two substrates of this enzyme are L-serine O-sulfate and H2O, whereas its 3 products are pyruvate, NH3, and sulfate. This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic name of this enzyme class is L-serine-O- sulfate ammonia-lyase (pyruvate-forming). This enzyme is also called (L-SOS)lyase.

In enzymology, a S-(hydroxymethyl)glutathione synthase () is an enzyme that catalyzes the chemical reaction :S-(hydroxymethyl)glutathione \rightleftharpoons glutathione + formaldehyde Hence, this enzyme has one substrate, S-(hydroxymethyl)glutathione, and two products, glutathione and formaldehyde. This enzyme belongs to the family of lyases, specifically the class of carbon-sulfur lyases. The systematic name of this enzyme class is S-(hydroxymethyl)glutathione formaldehyde-lyase (glutathione-forming). Other names in common use include glutathione-dependent formaldehyde-activating enzyme, Gfa, and S-(hydroxymethyl)glutathione formaldehyde-lyase.

Christian de Duve and his team continued studying the insulin mechanism-of-action in liver cells, focusing on the enzyme glucose 6-phosphatase, the key enzyme in sugar metabolism (glycolysis) and the target of insulin. They found that G6P was the principal enzyme in regulating blood sugar levels, but, they could not, even after repeated experiments, purify and isolate the enzyme from the cellular extracts. So they tried the more laborious procedure of cell fractionation to detect the enzyme activity. This was the moment of serendipitous discovery.

In enzymology, an isoorientin 3'-O-methyltransferase () is an enzyme that catalyzes the chemical reaction :S-adenosyl-L-methionine + isoorientin \rightleftharpoons S-adenosyl-L-homocysteine + isoscoparin Thus, the two substrates of this enzyme are S-adenosyl methionine and isoorientin, whereas its two products are S-adenosylhomocysteine and isoscoparin. This enzyme belongs to the family of transferases, specifically those transferring one- carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:isoorientin 3'-O-methyltransferase. This enzyme is also called isoorientin 3'-methyltransferase.

In enzymology, a jasmonate O-methyltransferase () is an enzyme that catalyzes the chemical reaction :S-adenosyl-L-methionine + jasmonate \rightleftharpoons S-adenosyl-L-homocysteine + methyl jasmonate Thus, the two substrates of this enzyme are S-adenosyl methionine and jasmonate, whereas its two products are S-adenosylhomocysteine and methyl jasmonate. This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L- methionine:jasmonate O-methyltransferase. This enzyme is also called jasmonic acid carboxyl methyltransferase.

In enzymology, an isovitexin beta-glucosyltransferase () is an enzyme that catalyzes the chemical reaction :UDP-glucose + isovitexin \rightleftharpoons UDP + isovitexin 2"-O-beta-D-glucoside Thus, the two substrates of this enzyme are UDP-glucose and isovitexin, whereas its two products are UDP and isovitexin 2"-O-beta-D-glucoside. This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-glucose:isovitexin 2"-O-beta-D- glucosyltransferase. This enzyme is also called uridine diphosphoglucose- isovitexin 2"-glucosyltransferase.

In enzymology, a coniferyl-alcohol dehydrogenase () is an enzyme that catalyzes the chemical reaction :coniferyl alcohol + NADP+ \rightleftharpoons coniferyl aldehyde + NADPH + H+ Thus, the two substrates of this enzyme are coniferyl alcohol and NADP+, whereas its 3 products are coniferyl aldehyde, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is coniferyl-alcohol:NADP+ oxidoreductase. This enzyme is also called CAD.

In enzymology, a spermidine dehydrogenase () is an enzyme that catalyzes the chemical reaction :spermidine + acceptor + H2O \rightleftharpoons propane-1,3-diamine + 4-aminobutanal + reduced acceptor The 3 substrates of this enzyme are spermidine, acceptor, and H2O, whereas its 3 products are propane-1,3-diamine, 4-aminobutanal, and reduced acceptor. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donor with other acceptors. The systematic name of this enzyme class is spermidine:acceptor oxidoreductase. This enzyme is also called spermidine:(acceptor) oxidoreductase.

In enzymology, a vellosimine dehydrogenase () is an enzyme that catalyzes the chemical reaction :10-deoxysarpagine + NADP+ \rightleftharpoons vellosimine + NADPH + H+ Thus, the two substrates of this enzyme are 10-deoxysarpagine and NADP+, whereas its 3 products are vellosimine, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH- OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 10-deoxysarpagine:NADP+ oxidoreductase. This enzyme participates in indole and ipecac alkaloid biosynthesis.

In enzymology, a salicylaldehyde dehydrogenase () is an enzyme that catalyzes the chemical reaction :salicylaldehyde + NAD+ \+ H2O \rightleftharpoons salicylate + NADH + 2 H+ The 3 substrates of this enzyme are salicylaldehyde, NAD+, and H2O, whereas its 3 products are salicylate, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is salicylaldehyde:NAD+ oxidoreductase. This enzyme participates in naphthalene and anthracene degradation.

In enzymology, a triokinase () is an enzyme that catalyzes the chemical reaction :ATP + D-glyceraldehyde \rightleftharpoons ADP + D-glyceraldehyde 3-phosphate Thus, the two substrates of this enzyme are ATP and D-glyceraldehyde, whereas its two products are ADP and D-glyceraldehyde 3-phosphate. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:D-glyceraldehyde 3-phosphotransferase. This enzyme is also called triose kinase.

In enzymology, a L-xylulokinase () is an enzyme that catalyzes the chemical reaction :ATP + L-xylulose \rightleftharpoons ADP + L-xylulose 5-phosphate Thus, the two substrates of this enzyme are ATP and L-xylulose, whereas its two products are ADP and L-xylulose 5-phosphate. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:L-xylulose 5-phosphotransferase. This enzyme is also called L-xylulokinase (phosphorylating).

In enzymology, a [protein-PII] uridylyltransferase () is an enzyme that catalyzes the chemical reaction :UTP + [protein-PII] \rightleftharpoons diphosphate + uridylyl-[protein-PII] Thus, the two substrates of this enzyme are UTP and protein-PII, whereas its two products are diphosphate and uridylyl-[protein-PII]. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is UTP:[protein-PII] uridylyltransferase. Other names in common use include PII uridylyl-transferase, and uridyl removing enzyme.

In enzymology, a nucleoside-phosphate kinase () is an enzyme that catalyzes the chemical reaction :ATP + nucleoside phosphate \rightleftharpoons ADP + nucleoside diphosphate Thus, the two substrates of this enzyme are ATP and nucleoside monophosphate, whereas its two products are ADP and nucleoside diphosphate. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. The systematic name of this enzyme class is ATP:nucleoside-phosphate phosphotransferase. This enzyme is also called NMP- kinase, or nucleoside-monophosphate kinase.

Figure B. The Human succinyl-CoA-Transferase enzyme is represented by the two joint blue and green bars at the top of the image. The alpha subunit of the Acetate-CoA- Transferase enzyme is homologous with the first half of the enzyme, represents by the blue bar. The beta subunit of the Acetate-CoA-Transferase enzyme is homologous with the second half of the enzyme, represents by the green bar. This mage was adapted from Uetz, P. & Pohl, E. (2018) Protein-Protein and Protein-DNA Interactions.

In enzymology, a sorbose reductase () is an enzyme that catalyzes the chemical reaction :D-glucitol + NADP+ \rightleftharpoons L-sorbose + NADPH + H+ Thus, the two substrates of this enzyme are D-glucitol and NADP+, whereas its 3 products are L-sorbose, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is D-glucitol:NADP+ oxidoreductase. This enzyme is also called Sou1p.

In enzymology, a D-ribulokinase () is an enzyme that catalyzes the chemical reaction :ATP + D-ribulose \rightleftharpoons ADP + D-ribulose 5-phosphate Thus, the two substrates of this enzyme are ATP and D-ribulose, whereas its two products are ADP and D-ribulose 5-phosphate. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:D-ribulose 5-phosphotransferase. This enzyme is also called D-ribulokinase (phosphorylating).

In enzymology, a diphosphate-purine nucleoside kinase () is an enzyme that catalyzes the chemical reaction :diphosphate + a purine nucleoside \rightleftharpoons phosphate + a purine mononucleotide Thus, the two substrates of this enzyme are diphosphate and purine nucleoside, whereas its two products are phosphate and purine mononucleotide. This enzyme belongs to the family of transferases, specifically those transferring phosphorus- containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is diphosphate:purine nucleoside phosphotransferase. This enzyme is also called pyrophosphate-purine nucleoside kinase.

In enzymology, a D-arabinokinase () is an enzyme that catalyzes the chemical reaction :ATP + D-arabinose \rightleftharpoons ADP + D-arabinose 5-phosphate Thus, the two substrates of this enzyme are ATP and D-arabinose, whereas its two products are ADP and D-arabinose 5-phosphate. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:D-arabinose 5-phosphotransferase. This enzyme is also called D-arabinokinase (phosphorylating).

In enzymology, a ceramide kinase, also abbreviated as CERK, () is an enzyme that catalyzes the chemical reaction: :ATP + ceramide \rightleftharpoons ADP + ceramide 1-phosphate Thus, the two substrates of this enzyme are ATP and ceramide, whereas its two products are ADP and ceramide-1-phosphate. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:ceramide 1-phosphotransferase. This enzyme is also called acylsphingosine kinase.

In enzymology, a hygromycin-B kinase () is an enzyme that catalyzes the chemical reaction :ATP + hygromycin B \rightleftharpoons ADP + 7"-O-phosphohygromycin Thus, the two substrates of this enzyme are ATP and hygromycin B, whereas its two products are ADP and 7-O-phosphohygromycin. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:hygromycin-B 7"-O-phosphotransferase. This enzyme is also called hygromycin B phosphotransferase.

In enzymology, a 6-hydroxyhexanoate dehydrogenase () is an enzyme that catalyzes the chemical reaction :6-hydroxyhexanoate + NAD+ \rightleftharpoons 6-oxohexanoate + NADH + H+ Thus, the two substrates of this enzyme are 6-hydroxyhexanoate and NAD+, whereas its 3 products are 6-oxohexanoate, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 6-hydroxyhexanoate:NAD+ oxidoreductase. This enzyme participates in caprolactam degradation.

In enzymology, a 8-oxocoformycin reductase () is an enzyme that catalyzes the chemical reaction :coformycin + NADP+ \rightleftharpoons 8-oxocoformycin + NADPH + H+ Thus, the two substrates of this enzyme are coformycin and NADP+, whereas its 3 products are 8-oxocoformycin, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is coformycin:NADP+ 8-oxidoreductase. This enzyme is also called 8-ketodeoxycoformycin reductase.

In enzymology, a (+)-borneol dehydrogenase () is an enzyme that increases the rate of, or catalyzes, the chemical reaction :(+)-borneol + NAD \rightleftharpoons (+)-camphor + NADH + H Thus, the two substrates of this enzyme are (+)-borneol and NAD, whereas its 3 products are (+)-camphor, NADH, and H. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD or NADP as acceptor. The systematic name of this enzyme class is (+)-borneol:NAD oxidoreductase. This enzyme is also called bicyclic monoterpenol dehydrogenase.

In enzymology, a (+)-sabinol dehydrogenase () is an enzyme that catalyzes the chemical reaction :(+)-cis-sabinol + NAD \rightleftharpoons (+)-sabinone + NADH + H Thus, the two substrates of this enzyme are (+)-cis-sabinol and NAD, whereas its 3 products are (+)-sabinone, NADH, and H. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD or NADP as acceptor. The systematic name of this enzyme class is (+)-cis-sabinol:NAD oxidoreductase. This enzyme is also called (+)-cis- sabinol dehydrogenase.

In enzymology, an ureidoglycolate dehydrogenase () is an enzyme that catalyzes the chemical reaction :(S)-ureidoglycolate + NAD(P)+ \rightleftharpoons oxalureate + NAD(P)H + H+ The 3 substrates of this enzyme are (S)-ureidoglycolate, NAD+, and NADP+, whereas its 4 products are oxalureate, NADH, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (S)-ureidoglycolate:NAD(P)+ oxidoreductase. This enzyme participates in purine metabolism.

In enzymology, an octanol dehydrogenase () is an enzyme that catalyzes the chemical reaction :1-octanol + NAD+ \rightleftharpoons 1-octanal + NADH + H+ Thus, the two substrates of this enzyme are 1-octanol and NAD+, whereas its 3 products are 1-octanal, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is octanol:NAD+ oxidoreductase. This enzyme is also called 1-octanol dehydrogenase.

Venombin A (, alpha-fibrinogenase, habutobin, zinc metalloproteinase Cbfib1.1, zinc metalloproteinase Cbfib1.2, zinc metalloproteinase Cbfib2, ancrod) is an enzyme. This enzyme catalyses the following chemical reaction : Selective cleavage of Arg- bond in fibrinogen, to form fibrin, and release fibrinopeptide A. The specificity of further degradation of fibrinogen varies with species origin of the enzyme This enzyme is a thrombin-like enzyme from venoms of snakes of the viper/rattlesnake group. Examples include ancrod and batroxobin, two serine proteases from snakes that have been used in medical preparations.

However, unlike uncatalysed chemical reactions, enzyme-catalysed reactions display saturation kinetics. For a given enzyme concentration and for relatively low substrate concentrations, the reaction rate increases linearly with substrate concentration; the enzyme molecules are largely free to catalyse the reaction, and increasing substrate concentration means an increasing rate at which the enzyme and substrate molecules encounter one another. However, at relatively high substrate concentrations, the reaction rate asymptotically approaches the theoretical maximum; the enzyme active sites are almost all occupied by substrates resulting in saturation, and the reaction rate is determined by the intrinsic turnover rate of the enzyme.Fromm H.J., Hargrove M.S. (2012) Enzyme Kinetics.

The primary biochemical reaction catalyzed by the adenosylcobalamin-5'-phosphate phosphatase (formerly alpha-ribazole phosphatase) () enzyme is :AdoCbl-5'-P + H2O \rightleftharpoons AdoCbl + phosphate This enzyme can also catalyze the following reaction in vitro, however it is not the biologically relevant reaction :alpha-ribazole 5'-phosphate + H2O \rightleftharpoons alpha-ribazole + phosphate Thus, the two substrates of this enzyme are adenosylcobalamin-5'-phosphate and H2O, whereas its two products are adenosylcobalamin and phosphate. This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name of this enzyme class is adenosylcobalamin-5'-phosphate phosphohydrolase. This enzyme is also called CobC.

In enzymology, a pantoate-beta-alanine ligase () is an enzyme that catalyzes the chemical reaction :ATP + (R)-pantoate + beta-alanine \rightleftharpoons AMP + diphosphate + (R)-pantothenate The 3 substrates of this enzyme are ATP, (R)-pantoate, and beta-alanine, whereas its 3 products are AMP, diphosphate, and (R)-pantothenate. This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases (peptide synthases). The systematic name of this enzyme class is (R)-pantoate:beta-alanine ligase (AMP-forming). Other names in common use include pantothenate synthetase, pantoate activating enzyme, pantoic- activating enzyme, and D-pantoate:beta-alanine ligase (AMP-forming).

Allosteric modulation is used to alter the activity of molecules and enzymes in biochemistry and pharmacology. For comparison, a typical drug is made to bind to the active site of an enzyme which thus prohibits binding of a substrate to that enzyme causing a decrease in enzyme activity. Allosteric modulation occurs when an effector binds to an allosteric site (also known as a regulatory site) of an enzyme and alters the enzyme activity. Allosteric modulators are designed to fit the allosteric site to cause a conformational change of the enzyme, in particular a change in the shape of the active site, which then causes a change in its activity.

Deoxyhypusine synthase (, spermidine:eIF5A-lysine 4-aminobutyltransferase (propane-1,3-diamine-forming)) is an enzyme with systematic name (eIF5A-precursor)-lysine:spermidine 4-aminobutyltransferase (propane-1,3-diamine-forming). This enzyme catalyses the following chemical reaction : [eIF5A-precursor]-lysine + spermidine \rightleftharpoons [eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine (overall reaction) : (1a) spermidine + NAD+ \rightleftharpoons dehydrospermidine + NADH : (1b) dehydrospermidine + [enzyme]-lysine \rightleftharpoons N-(4-aminobutylidene)-[enzyme]-lysine + propane-1,3-diamine : (1c) N-(4-aminobutylidene)-[enzyme]-lysine + [eIF5A-precursor]-lysine \rightleftharpoons N-(4-aminobutylidene)-[eIF5A-precursor]-lysine + [enzyme]-lysine : (1d) N-(4-aminobutylidene)-[eIF5A-precursor]-lysine + NADH + H+ \rightleftharpoons [eIF5A-precursor]-deoxyhypusine + NAD+ The eukaryotic initiation factor eIF5A contains a hypusine residue that is essential for activity.

In methylcobalamin-dependent forms of the enzyme, the reaction proceeds by two steps in a ping-pong reaction. The enzyme is initially primed into a reactive state by the transfer of a methyl group from N5-MeTHF to Co(I) in enzyme-bound cobalamin (Cob), forming methyl-cobalamin(Me-Cob) that now contains Me-Co(III) and activating the enzyme. Then, a Hcy that has coordinated to an enzyme-bound zinc to form a reactive thiolate reacts with the Me-Cob. The activated methyl group is transferred from Me-Cob to the Hcy thiolate, which regenerates Co(I) in Cob, and Met is released from the enzyme.

DNA ligase (NAD+) (, polydeoxyribonucleotide synthase (NAD+), polynucleotide ligase (NAD+), DNA repair enzyme, DNA joinase, polynucleotide synthetase (nicotinamide adenine dinucleotide), deoxyribonucleic-joining enzyme, deoxyribonucleic ligase, deoxyribonucleic repair enzyme, deoxyribonucleic joinase, DNA ligase, deoxyribonucleate ligase, polynucleotide ligase, deoxyribonucleic acid ligase, polynucleotide synthetase, deoxyribonucleic acid joinase, DNA-joining enzyme, polynucleotide ligase (nicotinamide adenine dinucleotide)) is an enzyme with systematic name poly(deoxyribonucleotide):poly(deoxyribonucleotide) ligase (AMP-forming, NMN- forming). This enzyme catalyses the following chemical reaction : NAD+ \+ (deoxyribonucleotide)n \+ (deoxyribonucleotide)m \rightleftharpoons AMP + beta-nicotinamide D-ribonucleotide + (deoxyribonucleotide)n+m Catalyses the formation of a phosphodiester at the site of a single-strand break in duplex DNA.

In enzymology, a maleylacetate reductase () is an enzyme that catalyzes the chemical reaction :3-oxoadipate + NAD(P)+ \rightleftharpoons 2-maleylacetate + NAD(P)H + H+ The 3 substrates of this enzyme are 3-oxoadipate, NAD+, and NADP+, whereas its 4 products are 2-maleylacetate, NADH, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 3-oxoadipate:NAD(P)+ oxidoreductase. This enzyme is also called maleolylacetate reductase. This enzyme participates in 3 metabolic pathways: gamma-hexachlorocyclohexane degradation, benzoate degradation via hydroxylation, and 1,4-dichlorobenzene degradation.

In enzymology, a trans-1,2-dihydrobenzene-1,2-diol dehydrogenase () is an enzyme that catalyzes the chemical reaction :trans-1,2-dihydrobenzene-1,2-diol + NADP+ \rightleftharpoons catechol + NADPH + H+ Thus, the two substrates of this enzyme are trans-1,2-dihydrobenzene-1,2-diol and NADP+, whereas its three products are catechol, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is trans-1,2-dihydrobenzene-1,2-diol:NADP+ oxidoreductase. This enzyme is also called dihydrodiol dehydrogenase. This enzyme participates in metabolism of xenobiotics by cytochrome p450.

In enzymology, a Delta24-sterol reductase () is an enzyme that catalyzes the chemical reaction :5alpha-cholest-7-en-3beta-ol + NADP+ \rightleftharpoons 5alpha-cholesta-7,24-dien-3beta-ol + NADPH + H+ Thus, the two substrates of this enzyme are 5alpha-cholest-7-en-3beta-ol and NADP+, whereas its 3 products are 5alpha-cholesta-7,24-dien-3beta-ol, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is sterol:NADP+ Delta24-oxidoreductase. This enzyme is also called lanosterol Delta24-reductase. This enzyme participates in biosynthesis of steroids.

In enzymology, a 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase () is an enzyme that catalyzes the chemical reaction :2,3-dihydro-2,3-dihydroxybenzoate + NAD+ \rightleftharpoons 2,3-dihydroxybenzoate + NADH + H+ Thus, the two substrates of this enzyme are 2,3-dihydro-2,3-dihydroxybenzoate and NAD+, whereas its 3 products are 2,3-dihydroxybenzoate, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH- CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 2,3-dihydro-2,3-dihydroxybenzoate:NAD+ oxidoreductase. This enzyme is also called 2,3-diDHB dehydrogenase. This enzyme participates in biosynthesis of siderophore group nonribosomal.

In enzymology, a precorrin-2 C20-methyltransferase () is an enzyme that catalyzes the chemical reaction :S-adenosyl-L-methionine + precorrin-2 \rightleftharpoons S-adenosyl-L-homocysteine + precorrin-3A precorrin-2 substrate of the enzyme The two substrates of this enzyme are S-adenosyl methionine and precorrin 2 and its two products are S-adenosylhomocysteine and precorrin 3A. This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:precorrin-4 C20-methyltransferase and another names in common use is CobI. The enzyme is part of the biosynthetic pathway to cobalamin (vitamin B12) in aerobic bacteria.

In enzymology, an enzyme-thiol transhydrogenase (glutathione-disulfide) () is an enzyme that catalyzes the chemical reaction :[xanthine dehydrogenase] + glutathione disulfide \rightleftharpoons [xanthine oxidase] + 2 glutathione Thus, the two substrates of this enzyme are xanthine dehydrogenase and glutathione disulfide, whereas its two products are xanthine oxidase and glutathione. This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with a disulfide as acceptor. The systematic name of this enzyme class is [xanthine- dehydrogenase]:glutathione-disulfide S-oxidoreductase. Other names in common use include [xanthine-dehydrogenase]:oxidized-glutathione S-oxidoreductase, enzyme-thiol transhydrogenase (oxidized-glutathione), glutathione-dependent thiol:disulfide oxidoreductase, and thiol:disulfide oxidoreductase.

In enzymology, a mycothiol-dependent formaldehyde dehydrogenase () is an enzyme that catalyzes the chemical reaction :formaldehyde + mycothiol + NAD+ \rightleftharpoons S-formylmycothiol + NADH + 2 H+ The 3 substrates of this enzyme are formaldehyde, mycothiol, and NAD+, whereas its 3 products are S-formylmycothiol, NADH, and H+. This enzyme catalyses the following chemical reaction This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is formaldehyde:NAD+ oxidoreductase (mycothiol-formylating). This enzyme is also called NAD/factor- dependent formaldehyde dehydrogenase or S-(hydroxymethyl)mycothiol dehydrogenase.

In enzymology, a leucoanthocyanidin reductase () (LAR, aka leucocyanidin reductase or LCR) is an enzyme that catalyzes the chemical reaction :(2R,3S)-catechin + NADP+ \+ H2O \rightleftharpoons 2,3-trans-3,4-cis- leucocyanidin + NADPH + H+ The 3 substrates of this enzyme are (2R,3S)-catechin, NADP+, and H2O, whereas its 3 products are 2,3-trans-3,4-cis-leucocyanidin, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on CH or CH2 groups with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (2R,3S)-catechin:NADP+ 4-oxidoreductase. This enzyme is also called leucocyanidin reductase. This enzyme participates in flavonoid biosynthesis.

In enzymology, a pyrroline-2-carboxylate reductase () is an enzyme that catalyzes the chemical reaction :L-proline + NAD(P)+ \rightleftharpoons 1-pyrroline-2-carboxylate + NAD(P)H + H+ The 3 substrates of this enzyme are L-proline, NAD+, and NADP+, whereas its 4 products are 1-pyrroline-2-carboxylate, NADH, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-proline:NAD(P)+ 2-oxidoreductase. This enzyme is also called Delta1-pyrroline-2-carboxylate reductase. This enzyme participates in lysine degradation and arginine and proline metabolism.

In enzymology, a methylenetetrahydrofolate reductase (ferredoxin) () is an enzyme that catalyzes the chemical reaction :5-methyltetrahydrofolate + 2 oxidized ferredoxin \rightleftharpoons 5,10-methylenetetrahydrofolate + 2 reduced ferredoxin + 2 H+ Thus, the two substrates of this enzyme are 5-methyltetrahydrofolate and oxidized ferredoxin, whereas its 3 products are 5,10-methylenetetrahydrofolate, reduced ferredoxin, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH- NH group of donors with an iron-sulfur protein as acceptor. The systematic name of this enzyme class is 5-methyltetrahydrofolate:ferredoxin oxidoreductase. This enzyme is also called 5,10-methylenetetrahydrofolate reductase. This enzyme participates in one carbon pool by folate.

In enzymology, a dTDP-galactose 6-dehydrogenase () is an enzyme that catalyzes the chemical reaction :dTDP-D-galactose + 2 NADP+ \+ H2O \rightleftharpoons dTDP-D-galacturonate + 2 NADPH + 2 H+ The 3 substrates of this enzyme are dTDP-D-galactose, NADP+, and H2O, whereas its 3 products are dTDP-D- galacturonate, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is dTDP-D- galactose:NADP+ 6-oxidoreductase. This enzyme is also called thymidine- diphosphate-galactose dehydrogenase. This enzyme participates in nucleotide sugars metabolism.

2-deoxy-D-gluconate 3-dehydrogenase () is an enzyme that catalyzes the chemical reaction :2-deoxy-D-gluconate + NAD+ \rightleftharpoons 3-dehydro-2-deoxy-D-gluconate + NADH + H+ Thus, the two substrates of this enzyme are 2-deoxy-D-gluconate and NAD+, whereas its 3 products are 3-dehydro-2-deoxy-D-gluconate, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 2-deoxy-D-gluconate:NAD+ 3-oxidoreductase. This enzyme is also called 2-deoxygluconate dehydrogenase. This enzyme participates in pentose and glucuronate interconversions.

In enzymology, a 2-hydroxy-3-oxopropionate reductase () is an enzyme that catalyzes the chemical reaction :(R)-glycerate + NAD(P)+ \rightleftharpoons 2-hydroxy-3-oxopropanoate + NAD(P)H + H+ The 3 substrates of this enzyme are (R)-glycerate, NAD+, and NADP+, whereas its 4 products are 2-hydroxy-3-oxopropanoate, NADH, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (R)-glycerate:NAD(P)+ oxidoreductase. This enzyme is also called tartronate semialdehyde reductase. This enzyme participates in glyoxylate and dicarboxylate metabolism.

The word ligase uses combining forms of lig- (from the Latin verb ligāre, "to bind" or "to tie together") + -ase (denoting an enzyme), yielding "binding enzyme".

Dimethylsulfone reductase () is an enzyme. This enzyme catalyses the following chemical reaction : dimethyl sulfoxide + H2O + NAD+ \rightleftharpoons dimethyl sulfone + NADH + H+ Dimethylsulfone reductase is a molybdoprotein.

The quantity or concentration of an enzyme can be expressed in molar amounts, as with any other chemical, or in terms of activity in enzyme units.

A proposed function of this form of the enzyme is matrix mineralization. However, mice that lack a functional form of this enzyme show normal skeletal development.

There is limited data to suggest that the human type II enzyme is subject to alternative splicing, as has been established for the type I enzyme.

An enzyme must be selected based upon the desired reaction. The selected enzyme defines the required operational properties, such as pH, temperature, activity, and substrate affinity.

This enzyme is also called 3-hydroxybenzoate 4-hydroxylase. This enzyme participates in benzoate degradation via hydroxylation and 2,4-dichlorobenzoate degradation. It employs one cofactor, FAD.

This enzyme is converted into its active mature form at low pH by sequential cleavage of the prosegment that is carried out by the enzyme itself.

Nitric oxide reductase (cytochrome c) () is an enzyme with systematic name nitrous oxide:ferricytochrome-c oxidoreductase. This enzyme catalyses the following chemical reaction : nitrous oxide + 2 ferricytochrome c + H2O \rightleftharpoons 2 nitric oxide + 2 ferrocytochrome c + 2 H+ The enzyme from Pseudomonas aeruginosa contains a dinuclear centre.

Pyrrole-2-carboxylate decarboxylase () is an enzyme with systematic name pyrrole-2-carboxylate carboxy-lyase. This enzyme catalyses the following chemical reaction : (1) pyrrole-2-carboxylate \rightleftharpoons pyrrole + CO2 : (2) pyrrole-2-carboxylate + H2O \rightleftharpoons pyrrole + HCO3− The enzyme catalyses both the carboxylation and decarboxylation reactions.

Carboxynorspermidine decarboxylase (, carboxyspermidine decarboxylase, CANSDC, VC1623 (gene)) is an enzyme with systematic name carboxynorspermidine carboxy- lyase (bis(3-aminopropyl)amine-forming). This enzyme catalyses the following chemical reaction : (1) carboxynorspermidine \rightleftharpoons bis(3-aminopropyl)amine + CO2 : (2) carboxyspermidine \rightleftharpoons spermidine + CO2 This enzyme contains pyridoxal 5'-phosphate.

In enzymology, an acetylxylan esterase () is an enzyme that catalyzes a chemical reaction, the deacetylation of xylans and xylo-oligosaccharides. This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is likewise acetylxylan esterase.

Phycoerythrobilin synthase (, PebS) is an enzyme with systematic name (3Z)-phycoerythrobilin:ferredoxin oxidoreductase (from biliverdin IX alpha). This enzyme catalyses the following chemical reaction : (3Z)-phycoerythrobilin + 2 oxidized ferredoxin \rightleftharpoons biliverdin IX alpha + 2 reduced ferredoxin This enzyme, from a cyanophage infecting oceanic cyanobacteria of the Prochlorococcus genus.

Oxepin-CoA hydrolase (, paaZ (gene)) is an enzyme with systematic name 2-oxepin-2(3H)-ylideneacetyl-CoA hydrolyase. This enzyme catalyses the following chemical reaction : 2-oxepin-2(3H)-ylideneacetyl-CoA + H2O \rightleftharpoons 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde The enzyme is present in bacteria Escherichia coli.

7-Chloro-L-tryptophan oxidase (, RebO) is an enzyme with systematic name 7-chloro-L-tryptophan:oxygen oxidoreductase. This enzyme catalyses the following chemical reaction : 7-chloro-L-tryptophan + O2 \rightleftharpoons 2-imino-3-(7-chloroindol-3-yl)propanoate + H2O2 This enzyme contains a noncovalently bound FAD.

D-proline dehydrogenase (, D-Pro DH, D-Pro dehydrogenase, dye-linked D-proline dehydrogenase) is an enzyme with systematic name D-proline:acceptor oxidoreductase. This enzyme catalyses the following chemical reaction : D-proline + acceptor \rightleftharpoons 1-pyrroline-2-carboxylate + reduced acceptor This enzyme is a flavoprotein (FAD).

Linolenate 9R-lipoxygenase (, NspLOX, (9R)-LOX, linoleate 9R-dioxygenase) is an enzyme with systematic name alpha-linolenate:oxygen (9R)-oxidoreductase. This enzyme catalyses the following chemical reaction : alpha-linolenate + O2 \rightleftharpoons (9R,10E,12Z,15Z)-9-hydroperoxyoctadeca-10,12,15-trienoate In cyanobacteria the enzyme is involved in oxylipin biosynthesis.

Soyasapogenol glucuronosyltransferase (, UGASGT) is an enzyme with systematic name UDP-D-glucuronate:soyasapogenol 3-O-D-glucuronosyltransferase. This enzyme catalyses the following chemical reaction : UDP-glucuronate + soyasapogenol B \rightleftharpoons UDP + soyasapogenol B 3-O-D-glucuronide This enzyme requires a divalent ion, Mg2+ or Mn2+, or Ca2+.

Plasmepsin I (, aspartic hemoglobinase I, PFAPG, malaria aspartic hemoglobinase) is an enzyme. This enzyme catalyses the following chemical reaction : Hydrolysis of the -Phe33-Leu- bond in the alpha-chain of hemoglobin, leading to denaturation of the molecule This enzyme is present in the malaria organism, Plasmodium.

Anthranilate 3-monooxygenase (FAD) (, anthranilate 3-hydroxylase, anthranilate hydroxylase) is an enzyme with systematic name anthranilate,FAD:oxygen oxidoreductase (3-hydroxylating). This enzyme catalyses the following chemical reaction : anthranilate + FADH2 \+ O2 \rightleftharpoons 3-hydroxyanthranilate + FAD + H2O The enzyme from the bacterium Geobacillus thermodenitrificans participates in tryptophan degradation.

Linalool dehydratase (, linalool hydro-lyase (myrcene-forming)) is an enzyme with systematic name (3S)-linalool hydro-lyase (myrcene-forming). This enzyme catalyses the following chemical reaction : (3S)-linalool \rightleftharpoons myrcene + H2O In absence of oxygen this enzyme can also catalyse the isomerization of (3S)-linalool to geraniol.

Epi-cedrol synthase (, 8-epicedrol synthase, epicedrol synthase) is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate diphosphate-lyase (8-epi- cedrol-forming). This enzyme catalyses the following chemical reaction : (2E,6E)-farnesyl diphosphate + H2O \rightleftharpoons 8-epi-cedrol + diphosphate This enzyme is activated by Mg2+.

Aphidicolan-16beta-ol synthase (, PbACS) is an enzyme with systematic name 9alpha-copalyl-diphosphate diphosphate-lyase (aphidicolan-16beta-ol-forming). This enzyme catalyses the following chemical reaction : 9alpha-copalyl diphosphate + H2O \rightleftharpoons aphidicolan-16beta-ol + diphosphate This is a bifunctional enzyme, which also has EC 5.5.1.14 activity.

Tetraprenyl-beta-curcumene synthase (, ytpB (gene)) is an enzyme with systematic name all-trans-heptaprenyl-diphosphate diphosphate-lyase (cyclizing, tetraprenyl-beta-curcumene-forming). This enzyme catalyses the following chemical reaction : all-trans-heptaprenyl diphosphate \rightleftharpoons tetraprenyl-beta-curcumene + diphosphate This enzyme is isolated from Bacillus subtilis.

Delta6-protoilludene synthase (, 6-protoilludene synthase) is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate diphosphate-lyase (cyclizing, Delta6-protoilludene-forming). This enzyme catalyses the following chemical reaction : (2E,6E)-farnesyl diphosphate \rightleftharpoons Delta6-protoilludene + diphosphate This enzyme is isolated from the fungus Armillaria gallica.

Bicyclogermacrene synthase (, Ov-TPS4) is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate diphosphate-lyase (bicyclogermacrene-forming). This enzyme catalyses the following chemical reaction : (2E,6E)-farnesyl diphosphate \rightleftharpoons bicyclogermacrene + diphosphate The enzyme from oregano (Origanum vulgare) gives mainly bicyclogermacrene with Mn2+ as a cofactor.

Alpha-humulene synthase (, ZSS1) is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate diphosphate-lyase (alpha-humulene-forming). This enzyme catalyses the following chemical reaction: : (2E,6E)-farnesyl diphosphate \rightleftharpoons alpha-humulene + diphosphate The enzyme from Zingiber zerumbet, shampoo ginger, also gives traces of β-caryophyllene.

Fusicocca-2,10(14)-diene synthase (, fusicoccadiene synthase, PaFS, PaDC4) is an enzyme with systematic name geranylgeranyl diphosphate-lyase (fusicocca-2,10(14)-diene-forming). This enzyme catalyses the following chemical reaction : geranylgeranyl diphosphate \rightleftharpoons fusicocca-2,10(14)-diene + diphosphate This multifunctional enzyme also has EC 2.5.1.29, farnesyltranstransferase, activity.

Isopimara-7,15-diene synthase (, PaTPS-Iso, copalyl diphosphate-lyase (isopimara-7,15-diene-forming)) is an enzyme with systematic name (+)-copalyl diphosphate-lyase (isopimara-7,15-diene-forming). This enzyme catalyses the following chemical reaction : (+)-copalyl diphosphate \rightleftharpoons isopimara-7,15-diene + diphosphate The enzyme only forms isopimara-7,15-diene.

4'-demethylrebeccamycin synthase (, arcyriaflavin A N-glycosyltransferase, RebG) is an enzyme with systematic name 4'-demethylrebeccamycin D-glucose- lyase. This enzyme catalyses the following chemical reaction : 4'-O-demethylrebeccamycin + H2O \rightleftharpoons dichloro-arcyriaflavin A + beta-D-glucose This enzyme catalyses a step in the biosynthesis of rebeccamycin.

TRNA pseudouridine38/39 synthase (, Deg1, Pus3p, pseudouridine synthase 3) is an enzyme with systematic name tRNA-uridine38/39 uracil mutase. This enzyme catalyses the following chemical reaction : tRNA uridine38/39 \rightleftharpoons tRNA pseudouridine38/39 The enzyme from Saccharomyces cerevisiae is active only towards uridine38 and uridine39.

Alcohol dehydrogenase (quinone) (, type III ADH, membrane associated quinohaemoprotein alcohol dehydrogenase) is an enzyme with systematic name alcohol:quinone oxidoreductase. This enzyme catalyses the following chemical reaction : ethanol + ubiquinone \rightleftharpoons acetaldehyde + ubiquinol This enzyme is present in acetic acid bacteria where it is involved in acetic acid production.

Pepsin B (, parapepsin I, pig gelatinase) is an enzyme. This enzyme catalyses the following chemical reaction : Degradation of gelatin, with manor activity on hemoglobin. Specificity for B chain of insulin is more restricted than that of pepsin A This enzyme is formed from pig pepsinogen B.

Chanoclavine-I dehydrogenase (, easD (gene), fgaDH (gene)) is an enzyme with systematic name chanoclavine-I:NAD+ oxidoreductase. This enzyme catalises the following chemical reaction : chanoclavine-I + NAD+ \rightleftharpoons chanoclavine-I aldehyde + NADH + H+ This enzyme catalyses a step in the pathway of ergot alkaloid biosynthesis in certain fungi.

Zeta-carotene isomerase (, Z-ISO, 15-cis-zeta-carotene isomerase) is an enzyme with systematic name 9,15,9'-tricis-zeta-carotene cis-trans-isomerase. This enzyme catalyses the following chemical reaction : 9,15,9'-tricis-zeta- carotene \rightleftharpoons 9,9'-dicis-zeta-carotene This enzyme is involved in carotenoid biosynthesis.

Germanicol synthase (, RsM1, (S)-2,3-epoxysqualene mutase (cyclizing, germanicol-forming)) is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualenee mutase (cyclizing, germanicol-forming). This enzyme catalyses the following chemical reaction : (3S)-2,3-epoxy-2,3-dihydrosqualene \rightleftharpoons germanicol The enzyme produces germanicol, beta-amyrin and lupeol.

Taraxerol synthase (, RsM2, (S)-2,3-epoxysqualene mutase (cyclizing, taraxerol-forming)) is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualene mutase (cyclizing, taraxerol-forming). This enzyme catalyses the following chemical reaction : (3S)-2,3-epoxy-2,3-dihydrosqualene \rightleftharpoons taraxerol The enzyme gives taraxerol, beta-amyrin and lupeol.

TRNA pseudouridine32 synthase (, RluA, pseudouridine synthase RluA, Pus9p, Rib2/Pus8p) is an enzyme with systematic name tRNA-uridine32 uracil mutase. This enzyme catalyses the following chemical reaction : tRNA uridine32 \rightleftharpoons tRNA pseudouridine32 The dual enzyme from Escherichia coli also catalyses the formation of pseudouridine746 in 23S rRNA.

Methionine transaminase (, methionine-oxo-acid transaminase) is an enzyme with systematic name L-methionine:2-oxo-acid aminotransferase. This enzyme catalyses the following chemical reaction : L-methionine + 2-oxo carboxylate \rightleftharpoons 2-oxo-4-methylthiobutanoate + L-amino acid The enzyme is most active with L-methionine.

GDP-L-galactose phosphorylase (, VTC2, VTC5) is an enzyme with systematic name GDP:alpha-L-galactose 1-phosphate guanylyltransferase. This enzyme catalyses the following chemical reaction : GDP-L-galactose + phosphate \rightleftharpoons alpha-L-galactose 1-phosphate + GDP The enzyme catalyses a reaction of the Smirnoff-Wheeler pathway.

Molybdenum cofactor sulfurtransferase (, molybdenum cofactor sulfurase, ABA3, HMCS, MoCo sulfurase, MoCo sulfurtransferase) is an enzyme with systematic name L-cysteine:molybdenum cofactor sulfurtransferase. This enzyme catalyses the following chemical reaction : molybdenum cofactor + L-cysteine + 2 H+ \rightleftharpoons thio-molybdenum cofactor + L-alanine + H2O This enzyme contains pyridoxal phosphate.

A preproenzyme is an enzyme with two additional characteristics: "pre" refers to a signal sequence (signal peptide) which directs the enzyme to a specific organelle or subcellular localization; "pro" indicates that the enzyme is present in an inactive form and requires modification (e.g. cleavage) for activation.

Most enzyme mimics studies are motivated by a combination of factors including factors that are unrelated to the enzyme. Several of the factors that are related to the enzyme are listed below. Defining the active site structure. A number of important active sites are still poorly defined.

Homospermidine synthase () is an enzyme with systematic name putrescine:putrescine 4-aminobutyltransferase (ammonia-forming). This enzyme catalyses the following chemical reaction : (1) 2 putrescine \rightleftharpoons sym-homospermidine + NH3 \+ H+ : (2) putrescine + spermidine \rightleftharpoons sym-homospermidine + propane-1,3-diamine The reaction of this enzyme occurs in three steps.

Beta-galactofuranosidase (, exo-beta-galactofuranosidase, exo-beta-D- galactofuranosidase, beta-D-galactofuranosidase) is an enzyme with systematic name beta-D-galactofuranoside hydrolase. This enzyme catalyses the following chemical reaction : Hydrolysis of terminal non-reducing beta-D- galactofuranosides, releasing [galactose] The enzyme from Helminthosporium sacchari detoxifies helminthosporoside.

Xaa-Pro aminopeptidase (, X-Pro aminopeptidase, proline aminopeptidase, aminopeptidase P, aminoacylproline aminopeptidase) is an enzyme. This enzyme catalyses the following chemical reaction : Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide This enzyme is Mn2+-dependent.

Nitric oxide reductase was assigned Enzyme Commission number (EC) 1.7.2.5. Enzyme Commission numbers are the standard naming system used for enzymes. The EC identifies the class, subclass, sub-subclass, and serial number of the enzyme. Nitric oxide reductase is in Class 1, therefore it is an oxidoreductases.

ADP-ribose 1-phosphate phosphatase (, POA1, Appr1p phosphatase, Poa1p) is an enzyme with systematic name ADP-ribose 1-phosphate phosphohydrolase. This enzyme catalyses the following chemical reaction : ADP-ribose 1-phosphate + H2O \rightleftharpoons ADP-ribose + phosphate The enzyme is highly specific for ADP-ribose 1-phosphate.

Ribonuclease IX (, poly(U)- and poly(C)-specific endoribonuclease) is an enzyme. This enzyme catalyses the following chemical reaction : Endonucleolytic cleavage of poly(U) or poly(C) to fragments terminated by 3'-hydroxy and 5'-phosphate groups This enzyme acts on poly(U) and poly(C).

Spleen exonuclease (, 3'-exonuclease, spleen phosphodiesterase, 3'-nucleotide phosphodiesterase, phosphodiesterase II) is an enzyme. This enzyme catalyses the following chemical reaction Exonucleolytic cleavage in the 5'- to 3'-direction to yield nucleoside 3'-phosphates (exonuclease type b) center This enzyme has a preference for single-stranded substrate.

Limit dextrinase (, R-enzyme, amylopectin-1,6-glucosidase, dextrin alpha-1,6-glucanohydrolase) is an enzyme with systematic name dextrin 6-alpha- glucanohydrolase. This enzyme catalyses the hydrolysis of (1->6)-alpha-D- glucosidic linkages in alpha- and beta-limits dextrins of amylopectin and glycogen,in amylopectin and pullulan.

Cerebroside-sulfatase (, arylsulfatase A, cerebroside sulfate sulfatase) is an enzyme with systematic name cerebroside-3-sulfate 3-sulfohydrolase. This enzyme catalyses the following chemical reaction : a cerebroside 3-sulfate + H2O \rightleftharpoons a cerebroside + sulfate This enzyme hydrolyses galactose-3-sulfate residues in a number of lipids.

Glutamyl endopeptidase II (, GluSGP) is an enzyme. This enzyme catalyses the following chemical reaction : Preferential cleavage: -Glu- >> -Asp- . Preference for Pro or Leu at P2 and Phe at P3. Cleavage of -Glu-Asp- and -Glu- Pro- bonds is slow This enzyme is isolated from Streptomyces griseus.

Hypodermin C (, Hypoderma collagenase) is an enzyme. This enzyme catalyses the following chemical reaction : Hydrolysis of proteins including native collagen at -Ala bond leaving an N-terminal (75%) and a C-terminal (25%) fragment This enzyme is isolated from the larva of a warble fly, Hypoderma lineatum.

Glycyl endopeptidase (, papaya peptidase B, papaya proteinase IV, glycine- specific proteinase, chymopapain, Papaya proteinase 4, PPIV, chymopapain M) is an enzyme. This enzyme catalyses the following chemical reaction : Preferential cleavage: Gly-, in proteins and small molecule substrates This enzyme is isolated from the papaya plant, Carica papaya.

V-cath endopeptidase (, AcNPV protease, BmNPV protease, NPV protease, baculovirus cathepsin, nucleopolyhedrosis virus protease, viral cathepsin) is an enzyme. This enzyme catalyses the following chemical reaction : Endopeptidase of broad specificity, hydrolyzing substrates of both cathepsin L and cathepsin B This enzyme belongs to the peptidase family C1.

The systematic name of this enzyme class is 3-mercaptopyruvate:cyanide sulfurtransferase. This enzyme is also called beta- mercaptopyruvate sulfurtransferase and in the older literature, human liver rhodanese.

Species in the genus Mucuna are known to carry irritant hairs. These hairs contain mucunain, an enzyme which causes itching. This enzyme can be destroyed using heat.

Debrisoquine is a derivative of guanidine. It is an antihypertensive drug similar to guanethidine. Debrisoquine is frequently used for phenotyping the CYP2D6 enzyme, a drug-metabolizing enzyme.

The enzyme formylmethanofuran:tetrahydromethanopterin formyltransferase catalyzes the transfer of the formyl group from formylmethanofuran to N5 on tetrahydromethanopterin, . This enzyme has been crystallized; it contains no prosthetic group.

In enzymology, a D-fuconate dehydratase () is an enzyme that catalyzes the chemical reaction :D-fuconate \rightleftharpoons 2-dehydro-3-deoxy-D-fuconate + H2O Hence, this enzyme has one substrate, D-fuconate, and two products, 2-dehydro-3-deoxy-D-fuconate and H2O. This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is D-fuconate hydro-lyase (2-dehydro-3-deoxy-D-fuconate-forming). This enzyme is also called D-fuconate hydro-lyase.

In enzymology, a L-fuconate dehydratase () is an enzyme that catalyzes the chemical reaction :L-fuconate \rightleftharpoons 2-dehydro-3-deoxy-L-fuconate + H2O Hence, this enzyme has one substrate, L-fuconate, and two products, 2-dehydro-3-deoxy-L-fuconate and H2O. This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is L-fuconate hydro-lyase (2-dehydro-3-deoxy-L-fuconate-forming). This enzyme is also called L-fuconate hydro-lyase.

In enzymology, a long-chain-enoyl-CoA hydratase () is an enzyme that catalyzes the chemical reaction :(3S)-3-hydroxyacyl-CoA \rightleftharpoons trans-2-enoyl-CoA + H2O Hence, this enzyme has one substrate, (3S)-3-hydroxyacyl-CoA, and two products, trans-2-enoyl-CoA and H2O. This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is long- chain-(3S)-3-hydroxyacyl-CoA hydro-lyase. This enzyme is also called long- chain enoyl coenzyme A hydratase.

In enzymology, a L-rhamnonate dehydratase () is an enzyme that catalyzes the chemical reaction :L-rhamnonate \rightleftharpoons 2-dehydro-3-deoxy-L- rhamnonate + H2O Hence, this enzyme has one substrate, L-rhamnonate, and two products, 2-dehydro-3-deoxy-L-rhamnonate and H2O. This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is L-rhamnonate hydro-lyase (2-dehydro-3-deoxy-L-rhamnonate-forming). This enzyme is also called L-rhamnonate hydro-lyase.

In enzymology, a trans-L-3-hydroxyproline dehydratase () is an enzyme that catalyzes the chemical reaction :trans-L-3-hydroxyproline \rightleftharpoons Delta1-pyrroline 2-carboxylate + H2O Hence, this enzyme has one substrate, trans-L-3-hydroxyproline, and two products, Delta1-pyrroline 2-carboxylate and H2O. This enzyme belongs to the family of lyases, specifically the hydro- lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is trans-L-3-hydroxyproline hydro-lyase (Delta1-pyrroline-2-carboxylate- forming). This enzyme is also called trans-L-3-hydroxyproline hydro-lyase.

In enzymology, a 5alpha-hydroxysteroid dehydratase () is an enzyme that catalyzes the chemical reaction :5alpha-ergosta-7,22-diene-3beta,5-diol \rightleftharpoons ergosterol + H2O Hence, this enzyme has one substrate, 5alpha-ergosta-7,22-diene-3beta,5-diol, and two products, ergosterol and H2O. This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is 5alpha-ergosta-7,22-diene-3beta,5-diol 5,6-hydro-lyase (ergosterol-forming). This enzyme is also called 5alpha-ergosta-7,22-diene-3beta,5-diol 5,6-hydro- lyase.

In enzymology, an amorpha-4,11-diene synthase (ADS) () is an enzyme that catalyzes the chemical reaction :2-trans,6-trans-farnesyl diphosphate ⇌ amorpha-4,11-diene + diphosphate Hence, this enzyme has one substrate, 2-trans,6-trans-farnesyl diphosphate, and two products, amorpha-4,11-diene and diphosphate. This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on phosphates. The systematic name of this enzyme class is 2-trans,6-trans-farnesyl-diphosphate diphosphate-lyase (amorpha-4,11-diene-forming). This enzyme is also called amorphadiene synthase.

Moreover, immobilization of an enzyme on a carrier often leads to a substantial loss of activity, especially at high enzyme loadings. Consequently, there is an increasing interest in carrier-free immobilized enzymes, such as cross-linked enzyme crystals (CLECs) and cross- linked enzyme aggregates (CLEAs) that offer the advantages of highly concentrated enzyme activity combined with high stability and low production costs owing to the exclusion of an additional (expensive) carrier. Cao, L.; van Langen, L.; Sheldon, R.A.; Immobilised enzymes: carrier-bound of carrier- free?; Curr. Opin. Biotechnol.

In enzymology, a Mg2+-importing ATPase () is an enzyme that catalyzes the chemical reaction :ATP + H2O + Mg2+out \rightleftharpoons ADP + phosphate + Mg2+in The 3 substrates of this enzyme are ATP, H2O, and Mg2+, whereas its 3 products are ADP, phosphate, and Mg2+. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (Mg2+-importing). The mgtA gene which encodes this enzyme is thought to be regulated by a magnesium responsive RNA element.

In enzymology, a glycerol-3-phosphate-transporting ATPase () is an enzyme that catalyzes the chemical reaction :ATP + H2O + glycerol-3-phosphateout \rightleftharpoons ADP + phosphate + glycerol-3-phosphatein The 3 substrates of this enzyme are ATP, H2O, and glycerol-3-phosphate, whereas its 3 products are ADP, phosphate, and glycerol-3-phosphate. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (glycerol-3-phosphate-importing). This enzyme participates in abc transporters - general.

In enzymology, a polar-amino-acid-transporting ATPase () is an enzyme that catalyzes the chemical reaction :ATP + H2O + polar amino acidout ADP + phosphate + polar amino acidin The 3 substrates of this enzyme are ATP, H2O, and polar amino acid, whereas its 3 products are ADP, phosphate, and polar amino acid. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (polar-amino-acid-importing). This enzyme is also called histidine permease.

In enzymology, a fatty-acyl-ethyl-ester synthase () is an enzyme that catalyzes the chemical reaction :a long-chain-fatty-acyl ethyl ester + H2O \rightleftharpoons a long-chain-fatty acid + ethanol Thus, the two substrates of this enzyme are long-chain-fatty-acyl ethyl ester and H2O, whereas its two products are long-chain-fatty acid and ethanol. This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is long-chain-fatty-acyl-ethyl-ester acylhydrolase. This enzyme is also called FAEES.

In enzymology, a glycerol-1,2-cyclic-phosphate 2-phosphodiesterase () is an enzyme that catalyzes the chemical reaction :glycerol 1,2-cyclic phosphate + H2O \rightleftharpoons glycerol 1-phosphate Thus, the two substrates of this enzyme are glycerol 1,2-cyclic phosphate and H2O, whereas its product is glycerol 1-phosphate. This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric diester bonds. The systematic name of this enzyme class is rac-glycerol-1,2-cyclic-phosphate 2-glycerophosphohydrolase. This enzyme is also called rac-glycerol 1:2-cyclic phosphate 2-phosphodiesterase.

In enzymology, a hydroxybutyrate-dimer hydrolase () is an enzyme that catalyzes the chemical reaction :(R)-3-((R)-3-hydroxybutanoyloxy)butanoate + H2O \rightleftharpoons 2 (R)-3-hydroxybutanoate Thus, the two substrates of this enzyme are (R)-3-((R)-3-hydroxybutanoyloxy)butanoate and H2O, whereas its product is (R)-3-hydroxybutanoate. This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is (R)-3-((R)-3-hydroxybutanoyloxy)butanoate hydroxybutanoylhydrolase. This enzyme is also called D-(−)-3-hydroxybutyrate-dimer hydrolase.

In enzymology, a [hydroxymethylglutaryl-CoA reductase (NADPH)]-phosphatase () is an enzyme that catalyzes the chemical reaction :[hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate + HO \rightleftharpoons [hydroxymethylglutaryl- CoA reductase (NADPH)] + phosphate Thus, the two substrates of this enzyme are hydroxymethylglutaryl-CoA reductase (NADPH) phosphate and HO, whereas its two products are hydroxymethylglutaryl-CoA reductase (NADPH) and phosphate. This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name of this enzyme class is [hydroxymethylglutaryl-CoA reductase (NADPH)]-phosphate phosphohydrolase. This enzyme is also called reductase phosphatase.

In enzymology, an inositol-1,4-bisphosphate 1-phosphatase () is an enzyme that catalyzes the chemical reaction :1D-myo-inositol 1,4-bisphosphate + H2O \rightleftharpoons 1D-myo-inositol 4-phosphate + phosphate Thus, the two substrates of this enzyme are 1D-myo-inositol 1,4-bisphosphate and H2O, whereas its two products are 1D-myo-inositol 4-phosphate and phosphate. This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name of this enzyme class is 1D-myo-inositol-1,4-bisphosphate 1-phosphohydrolase. This enzyme is also called inositol-polyphosphate 1-phosphatase.

In enzymology, a glycerophosphodiester phosphodiesterase () is an enzyme that catalyzes the chemical reaction :a glycerophosphodiester + H2O \rightleftharpoons an alcohol + sn-glycerol 3-phosphate Thus, the two substrates of this enzyme are glycerophosphodiester and H2O, whereas its two products are alcohol and sn-glycerol 3-phosphate. This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric diester bonds. The systematic name of this enzyme class is glycerophosphodiester glycerophosphohydrolase. Other names in common use include gene hpd protein, glycerophosphoryl diester phosphodiesterase, and IgD-binding protein D. This enzyme participates in glycerophospholipid metabolism.

In enzymology, a bis(2-ethylhexyl)phthalate esterase () is an enzyme that catalyzes the chemical reaction :bis(2-ethylhexyl)phthalate + H2O \rightleftharpoons 2-ethylhexyl phthalate + 2-ethylhexan-1-ol Thus, the two substrates of this enzyme are bis(2-ethylhexyl)phthalate and H2O, whereas its two products are 2-ethylhexyl phthalate and 2-ethylhexan-1-ol. 300px This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is bis(2-ethylhexyl)phthalate acylhydrolase. This enzyme is also called DEHP esterase.

In enzymology, a [phosphorylase] phosphatase () is an enzyme that catalyzes the chemical reaction :[phosphorylase a] + 4 HO \rightleftharpoons 2 [phosphorylase b] + 4 phosphate Thus, the two substrates of this enzyme are phosphorylase a and HO, whereas its two products are phosphorylase b and phosphate. This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name of this enzyme class is [phosphorylase a] phosphohydrolase. Other names in common use include PR- enzyme, phosphorylase a phosphatase, glycogen phosphorylase phosphatase, protein phosphatase C, and type 1 protein phosphatase.

In enzymology, a 2-deoxyglucose-6-phosphatase () is an enzyme that catalyzes the chemical reaction :2-deoxy-D-glucose 6-phosphate + H2O \rightleftharpoons 2-deoxy-D-glucose + phosphate Thus, the two substrates of this enzyme are 2-deoxy-D-glucose 6-phosphate and H2O, whereas its two products are 2-deoxy-D- glucose and phosphate. This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name of this enzyme class is 2-deoxy-D-glucose-6-phosphate phosphohydrolase. This enzyme is also called 2-deoxyglucose-6-phosphate phosphatase.

In enzymology, an acetylalkylglycerol acetylhydrolase () is an enzyme that catalyzes the chemical reaction :2-acetyl-1-alkyl-sn-glycerol + H2O \rightleftharpoons 1-alkyl-sn-glycerol + acetate Thus, the two substrates of this enzyme are 2-acetyl-1-alkyl-sn-glycerol and H2O, whereas its two products are 1-alkyl-sn-glycerol and acetate. This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is 2-acetyl-1-alkyl-sn-glycerol acetylhydrolase. This enzyme is also called alkylacetylglycerol acetylhydrolase.

In enzymology, an alpha-amino-acid esterase () is an enzyme that catalyzes the chemical reaction :an alpha-amino acid ester + H2O \rightleftharpoons an alpha-amino acid + an alcohol Thus, the two substrates of this enzyme are alpha-amino acid ester and H2O, whereas its two products are alpha-amino acid and alcohol. This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is alpha-amino-acid-ester aminoacylhydrolase. This enzyme is also called alpha-amino acid ester hydrolase.

In enzymology, a chondroitin 4-sulfotransferase () is an enzyme that catalyzes the chemical reaction :3'-phosphoadenosine-5'-phosphosulfate + chondroitin \rightleftharpoons adenosine 3',5'-bisphosphate + chondroitin 4'-sulfate Thus, the two substrates of this enzyme are 3'-phosphoadenylyl sulfate and chondroitin, whereas its two products are adenosine 3',5'-bisphosphate and chondroitin 4'-sulfate. This enzyme belongs to the family of transferases, to be specific, the sulfotransferases, which transfer sulfur-containing groups. The systematic name of this enzyme class is 3'-phosphoadenylyl- sulfate:chondroitin 4'-sulfotransferase. This enzyme is also called chondroitin sulfotransferase.

In enzymology, a trans-feruloyl-CoA synthase () is an enzyme that catalyzes the chemical reaction :ferulic acid + CoASH + ATP \rightleftharpoons trans- feruloyl-CoA + products of ATP breakdown The 3 substrates of this enzyme are ferulic acid, CoASH, and ATP, whereas its two products are trans-feruloyl-CoA and products of ATP breakdown. This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The systematic name of this enzyme class is trans-ferulate:CoASH ligase (ATP- hydrolysing). This enzyme is also called trans-feruloyl-CoA synthetase.

In enzymology, a biotin carboxylase () is an enzyme that catalyzes the chemical reaction :ATP + biotin-carboxyl-carrier protein + CO2 \rightleftharpoons ADP + phosphate + carboxybiotin-carboxyl-carrier protein The 3 substrates of this enzyme are ATP, biotin-carboxyl-carrier protein, and CO2, whereas its 3 products are ADP, phosphate, and carboxybiotin-carboxyl- carrier protein. This enzyme belongs to the family of ligases, specifically those forming generic carbon-nitrogen bonds. The systematic name of this enzyme class is biotin-carboxyl-carrier-protein:carbon-dioxide ligase (ADP- forming). This enzyme is also called biotin carboxylase (component of acetyl CoA carboxylase).

In enzymology, a 2-furoate—CoA ligase () is an enzyme that catalyzes the chemical reaction :ATP + 2-furoate + CoA \rightleftharpoons AMP + diphosphate + 2-furoyl-CoA The 3 substrates of this enzyme are ATP, 2-furoate, and CoA, whereas its 3 products are AMP, diphosphate, and 2-furoyl-CoA. This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The systematic name of this enzyme class is 2-furoate:CoA ligase (AMP-forming). This enzyme is also called 2-furoyl coenzyme A synthetase.

In enzymology, a glutamate-tRNAGln ligase () is an enzyme that catalyzes the chemical reaction :ATP + L-glutamate + tRNAGlx \rightleftharpoons AMP + diphosphate + glutamyl-tRNAGlx The 3 substrates of this enzyme are ATP, L-glutamate, and tRNAGlx, whereas its 3 products are AMP, diphosphate, and glutamyl-tRNAGlx. This enzyme belongs to the family of ligases, to be specific those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. The systematic name of this enzyme class is L-glutamate:tRNAGlx ligase (AMP- forming). This enzyme is also called glutamyl-tRNA synthetase.

In enzymology, a RNA-3'-phosphate cyclase () is an enzyme that catalyzes the chemical reaction :ATP + RNA 3'-terminal-phosphate \rightleftharpoons AMP + diphosphate + RNA terminal-2',3'-cyclic-phosphate Thus, the two substrates of this enzyme are ATP and RNA 3'-terminal-phosphate, whereas its 3 products are AMP, diphosphate, and RNA terminal-2',3'-cyclic-phosphate. This enzyme belongs to the family of ligases, specifically those forming phosphoric-ester bonds. The systematic name of this enzyme class is RNA-3'-phosphate:RNA ligase (cyclizing, AMP-forming). This enzyme is also called RNA cyclase.

In enzymology, a long-chain-fatty-acid-luciferin-component ligase () is an enzyme that catalyzes the chemical reaction :ATP + an acid + protein \rightleftharpoons AMP + diphosphate + an acyl-protein thioester The 3 substrates of this enzyme are ATP, acid, and protein, whereas its 3 products are AMP, diphosphate, and acyl-protein thioester. This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid- thiol ligases. The systematic name of this enzyme class is long-chain-fatty- acid:protein ligase (AMP-forming). This enzyme is also called acyl-protein synthetase.

4-amino-4-deoxychorismate lyase () is an enzyme that participates in folate biosynthesis by catalyzing the production of PABA by the following reaction :4-amino-4-deoxychorismate \rightleftharpoons 4-aminobenzoate + pyruvate This enzyme has one substrate, 4-amino-4-deoxychorismate, and two products, 4-aminobenzoate (PABA) and pyruvate. This enzyme belongs to the family of lyases, specifically the oxo-acid-lyases, which cleave carbon-carbon bonds. This enzyme, encoded by the pabC gene in bacteria and plants, is also known as PabC or ADC lyase. The fungal enzyme has been designated ABZ2.

In enzymology, a hydroxyglutamate decarboxylase () is an enzyme that catalyzes the chemical reaction :3-hydroxy-L-glutamate \rightleftharpoons 4-amino-3-hydroxybutanoate + CO2 Hence, this enzyme has one substrate, 3-hydroxy-L-glutamate, and two products, 4-amino-3-hydroxybutanoate and CO2. This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is 3-hydroxy-L-glutamate 1-carboxy-lyase (4-amino-3-hydroxybutanoate-forming). This enzyme is also called 3-hydroxy-L-glutamate 1-carboxy-lyase.

In enzymology, a tagatose-bisphosphate aldolase () is an enzyme that catalyzes the chemical reaction :D-tagatose 1,6-bisphosphate \rightleftharpoons glycerone phosphate + D-glyceraldehyde 3-phosphate Hence, this enzyme has one substrate, D-tagatose 1,6-bisphosphate, and two products, glycerone phosphate and D-glyceraldehyde 3-phosphate. This enzyme belongs to the family of lyases, specifically the aldehyde-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is D-tagatose 1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase (glycerone-phosphate-forming). This enzyme is also called D-tagatose-1,6-bisphosphate triosephosphate lyase.

In enzymology, a steroid sulfotransferase () is an enzyme that catalyzes the chemical reaction :3'-phosphoadenylyl sulfate + a phenolic steroid \rightleftharpoons adenosine 3',5'-bisphosphate + steroid O-sulfate Thus, the two substrates of this enzyme are 3'-phosphoadenylyl sulfate and phenolic steroid, whereas its two products are adenosine 3',5'-bisphosphate and steroid O-sulfate. This enzyme belongs to the family of transferases, specifically the sulfotransferases, which transfer sulfur-containing groups. The systematic name of this enzyme class is 3'-phosphoadenylyl-sulfate:phenolic-steroid sulfotransferase. This enzyme is also called steroid alcohol sulfotransferase.

The enzyme 4-methoxybenzoate monooxygenase (O-demethylating) transforms 4-methoxybenzoate, an electron acceptor AH2 and O2 into 4-hydroxybenzoate, formaldehyde, the reduction product A and H2O. This enzyme participates in 2,4-dichlorobenzoate degradation in Pseudomonas putida. The enzyme 4-hydroxybenzaldehyde dehydrogenase uses 4-hydroxybenzaldehyde, NAD+ and H2O to produce 4-hydroxybenzoate, NADH and H+. This enzyme participates in toluene and xylene degradation in bacteria such as Pseudomonas mendocina. It is also found in carrots (Daucus carota). The enzyme that 2,4'-dihydroxyacetophenone dioxygenase transforms 2,4'-dihydroxyacetophenone and O2 into 4-hydroxybenzoate and formate.

An adaptive enzyme or inducible enzyme is an enzyme that is expressed only under conditions in which it is clearly of adaptive value, as opposed to a constitutive enzyme which is produced all the time. The Inducible enzyme is used for the breaking-down of things in the cell. It is also a part of the Operon Model, which illustrates a way for genes to turn "on" and "off". The Inducer causes the gene to turn on (controlled by the amount of reactant which turns the gene on).

Transition state analogs (transition state analogues), are chemical compounds with a chemical structure that resembles the transition state of a substrate molecule in an enzyme-catalyzed chemical reaction. Enzymes interact with a substrate by means of strain or distortions, moving the substrate towards the transition state. Transition state analogs can be used as inhibitors in enzyme-catalyzed reactions by blocking the active site of the enzyme. Theory suggests that enzyme inhibitors which resembled the transition state structure would bind more tightly to the enzyme than the actual substrate.

The system was discovered by Saul Roseman in 1964. The bacterial phosphoenolpyruvate:sugar phosphotransferase system (PTS) transports and phosphorylates its sugar substrates in a single energy-coupled step. This transport process is dependent on several cytoplasmic phosphoryl transfer proteins - Enzyme I (I), HPr, Enzyme IIA (IIA), and Enzyme IIB (IIB)) as well as the integral membrane sugar permease (IIC).The PTS Enzyme II complexes are derived from independently evolving 4 PTS Enzyme II complex superfamilies, that include the (1) Glucose (Glc),(2) Mannose (Man), (3) Ascorbate-Galactitol (Asc-Gat) and (4) Dihydroxyacetone (Dha) superfamilies.

In enzymology, an alpha,alpha-phosphotrehalase () is an enzyme that catalyzes the chemical reaction :alpha,alpha-trehalose 6-phosphate + H2O \rightleftharpoons D-glucose + D-glucose 6-phosphate Thus, the two substrates of this enzyme are alpha,alpha'-trehalose 6-phosphate and H2O, whereas its two products are D-glucose and D-glucose 6-phosphate. This enzyme belongs to the family of hydrolases, specifically those glycosidases that hydrolyse O- and S-glycosyl compounds. The systematic name of this enzyme class is alpha,alpha- trehalose-6-phosphate phosphoglucohydrolase. This enzyme is also called phosphotrehalase.

For beta-glucuronidase, see Beta-glucuronidase In enzymology, an alpha- glucuronidase () is an enzyme that catalyzes the chemical reaction :an alpha- D-glucuronoside + H2O \rightleftharpoons an alcohol + D-glucuronate Thus, the two substrates of this enzyme are alpha-D-glucuronoside and H2O, whereas its two products are alcohol and D-glucuronate. This enzyme belongs to the family of hydrolases, to be specific those glycosidases that hydrolyse O- and S-glycosyl compounds. The systematic name of this enzyme class is alpha-D- glucosiduronate glucuronohydrolase. This enzyme is also called alpha- glucosiduronase.

In enzymology, an ureidosuccinase () is an enzyme that catalyzes the chemical reaction :N-carbamoyl-L-aspartate + H2O \rightleftharpoons L-aspartate + CO2 \+ NH3 Thus, the two substrates of this enzyme are N-carbamoyl-L-aspartate and H2O, whereas its 3 products are L-aspartate, CO2, and NH3. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N-carbamoyl-L-aspartate amidohydrolase. This enzyme participates in alanine and aspartate metabolism.

In enzymology, a ricinine nitrilase () is an enzyme that catalyzes the chemical reaction :ricinine + 2 H2O \rightleftharpoons 3-carboxy-4-methoxy-N- methyl-2-pyridone + NH3 Thus, the two substrates of this enzyme are ricinine and H2O, whereas its two products are 3-carboxy-4-methoxy-N-methyl-2-pyridone and NH3. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in nitriles. The systematic name of this enzyme class is ricinine aminohydrolase. This enzyme participates in nitrogen metabolism.

In enzymology, a S-adenosylhomocysteine deaminase () is an enzyme that catalyzes the chemical reaction :S-adenosyl-L-homocysteine + H2O \rightleftharpoons S-inosyl-L-homocysteine + NH3 Thus, the two substrates of this enzyme are S-adenosyl-L-homocysteine and H2O, whereas its two products are S-inosyl-L-homocysteine and NH3. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is S-adenosyl-L-homocysteine aminohydrolase. This enzyme is also called adenosylhomocysteine deaminase.

In enzymology, a (S)-N-acetyl-1-phenylethylamine hydrolase () is an enzyme that catalyzes the chemical reaction :N-acetylphenylethylamine + HO \rightleftharpoons phenethylamine + acetate Thus, the two substrates of this enzyme are N-acetylphenylethylamine and HO, whereas its two products are phenethylamine and acetate. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is (S)-N-acetylphenylethylamine:HO hydrolase. At least one compound, phenylmethanesulfonylfluoride is known to inhibit this enzyme.

In enzymology, a N-isopropylammelide isopropylaminohydrolase () is an enzyme that catalyzes the chemical reaction :N-isopropylammelide + H2O \rightleftharpoons cyanuric acid + isopropylamine Thus, the two substrates of this enzyme are N-isopropylammelide and H2O, whereas its two products are cyanuric acid and isopropylamine. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in compounds that have not been otherwise categorized within EC number 3.5. The systematic name of this enzyme class is N-isopropylammelide isopropylaminohydrolase. This enzyme is also called AtzC.

In enzymology, a N-malonylurea hydrolase () is an enzyme that catalyzes the chemical reaction :3-oxo-3-ureidopropanoate + H2O \rightleftharpoons malonate + urea Thus, the two substrates of this enzyme are 3-oxo-3-ureidopropanoate and H2O, whereas its two products are malonate and urea. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is 3-oxo-3-ureidopropanoate amidohydrolase (urea- and malonate- forming). This enzyme is also called ureidomalonase.

In enzymology, a N-methyl-2-oxoglutaramate hydrolase () is an enzyme that catalyzes the chemical reaction :N-methyl-2-oxoglutaramate + H2O \rightleftharpoons 2-oxoglutarate + methylamine Thus, the two substrates of this enzyme are N-methyl-2-oxoglutaramate and H2O, whereas its two products are 2-oxoglutarate and methylamine. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N-methyl-2-oxoglutaramate methylamidohydrolase. This enzyme is also called 5-hydroxy-N-methylpyroglutamate synthase.

In enzymology, an omega-amidase () is an enzyme that catalyzes the chemical reaction :a monoamide of a dicarboxylic acid + H2O \rightleftharpoons a dicarboxylate + NH3 Thus, the two substrates of this enzyme are monoamide of a dicarboxylic acid and H2O, whereas its two products are dicarboxylate and NH3. This enzyme belongs to the family of hydrolases, those acting on carbon- nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is omega-amidodicarboxylate amidohydrolase. This enzyme is also called alpha-keto acid-omega-amidase.

In enzymology, a N-formylmethionylaminoacyl-tRNA deformylase () is an enzyme that catalyzes the chemical reaction :N-formyl-L-methionylaminoacyl-tRNA + H2O \rightleftharpoons formate + L-methionylaminoacyl-tRNA Thus, the two substrates of this enzyme are N-formyl-L-methionylaminoacyl-tRNA and H2O, whereas its two products are formate and L-methionylaminoacyl-tRNA. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N-formyl-L-methionylaminoacyl-tRNA amidohydrolase. This enzyme participates in glyoxylate and dicarboxylate metabolism.

In enzymology, an allophanate hydrolase () is an enzyme that catalyzes the chemical reaction :allophanate + 3 H2O + H+ \rightleftharpoons 2 HCO3− \+ 2 NH4+ Thus, the two substrates of this enzyme are allophanate (urea-1-carboxylate or N-carbamoylcarbamate) and H2O, whereas its two products are HCO3− and NH4+. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is urea-1-carboxylate amidohydrolase. This enzyme is also called allophanate lyase.

In enzymology, a bromoxynil nitrilase () is an enzyme that catalyzes the chemical reaction :3,5-dibromo-4-hydroxybenzonitrile + 2 H2O \rightleftharpoons 3,5-dibromo-4-hydroxy-benzoate + NH3 Thus, the two substrates of this enzyme are 3,5-dibromo-4-hydroxybenzonitrile and H2O, whereas its two products are 3,5-dibromo-4-hydroxy-benzoate and NH3. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in nitriles. The systematic name of this enzyme class is 3,5-dibromo-4-hydroxybenzonitrile aminohydrolase. This enzyme participates in 1,4-dichlorobenzene degradation.

In enzymology, a cyanoalanine nitrilase () is an enzyme that catalyzes the chemical reaction :3-cyano-L-alanine + 2 H2O \rightleftharpoons L-aspartate + NH3 Thus, the two substrates of this enzyme are 3-cyano-L-alanine and H2O, whereas its two products are L-aspartate and NH3. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in nitriles. The systematic name of this enzyme class is 3-cyano-L-alanine aminohydrolase. This enzyme is also called beta-cyanoalanine nitrilase.

In enzymology, a N-acetyl-beta-alanine deacetylase () is an enzyme that catalyzes the chemical reaction :N-acetyl-beta-alanine + H2O \rightleftharpoons acetate + beta-alanine Thus, the two substrates of this enzyme are N-acetyl-beta-alanine and H2O, whereas its two products are acetate and beta-alanine. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N-acetyl-beta- alanine amidohydrolase. This enzyme participates in beta-alanine metabolism.

In enzymology, a 2-aminomuconate deaminase () is an enzyme that catalyzes the chemical reaction :2-aminomuconate + H2O \rightleftharpoons 4-oxalocrotonate + NH3 Thus, the two substrates of this enzyme are 2-aminomuconate and H2O, whereas its two products are 4-oxalocrotonate and NH3. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in compounds that have not been otherwise categorized within EC number 3.5. The systematic name of this enzyme class is 2-aminomuconate aminohydrolase. This enzyme participates in tryptophan metabolism.

In enzymology, a 4-acetamidobutyrate deacetylase () is an enzyme that catalyzes the chemical reaction :4-acetamidobutanoate + H2O \rightleftharpoons acetate + 4-aminobutanoate Thus, the two substrates of this enzyme are 4-acetamidobutanoate and H2O, whereas its two products are acetate and 4-aminobutanoate. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is 4-acetamidobutanoate amidohydrolase. This enzyme participates in urea cycle and metabolism of amino groups and lysine degradation.

In enzymology, a formimidoylaspartate deiminase () is an enzyme that catalyzes the chemical reaction :N-formimidoyl-L-aspartate + H2O \rightleftharpoons N-formyl-L-aspartate + NH3 Thus, the two substrates of this enzyme are N-formimidoyl-L-aspartate and H2O, whereas its two products are N-formyl-L- aspartate and NH3. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amidines. The systematic name of this enzyme class is N-formimidoyl-L- aspartate iminohydrolase. This enzyme is also called formiminoaspartate deiminase.

In enzymology, a formylaspartate deformylase () is an enzyme that catalyzes the chemical reaction :N-formyl-L-aspartate + H2O \rightleftharpoons formate + L-aspartate Thus, the two substrates of this enzyme are N-formyl-L-aspartate and H2O, whereas its two products are formate and L-aspartate. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N-formyl-L-aspartate amidohydrolase. This enzyme is also called formylaspartic formylase (formylase I, formylase II).

In enzymology, a formylmethionine deformylase () is an enzyme that catalyzes the chemical reaction :N-formyl-L-methionine + H2O \rightleftharpoons formate + L-methionine Thus, the two substrates of this enzyme are N-formyl-L- methionine and H2O, whereas its two products are formate and L-methionine. This enzyme belongs to the family of hydrolases, those acting on carbon- nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N-formyl-L-methionine amidohydrolase. This enzyme participates in methionine metabolism and glyoxylate and dicarboxylate metabolism.

In enzymology, a 6-O-methylnorlaudanosoline 5'-O-methyltransferase () is an enzyme that catalyzes the chemical reaction :S-adenosyl-L-methionine + 6-O-methylnorlaudanosoline \rightleftharpoons S-adenosyl-L-homocysteine + nororientaline Thus, the two substrates of this enzyme are S-adenosyl methionine and 6-O-methylnorlaudanosoline, whereas its two products are S-adenosylhomocysteine and nororientaline. This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L- methionine:6-O-methylnorlaudanosoline 5'-O-methyltransferase. This enzyme participates in alkaloid biosynthesis i.

In enzymology, a cobalt-factor II C20-methyltransferase () is an enzyme that catalyzes the chemical reaction :S-adenosyl-L-methionine + cobalt-factor II \rightleftharpoons S-adenosyl-L-homocysteine + cobalt-factor III The two substrates of this enzyme are S-adenosyl methionine and cobalt-factor II; its two products are S-adenosylhomocysteine and cobalt-factor III. This enzyme belongs to the family of transferases, specifically those transferring one- carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:cobalt-factor-II C20-methyltransferase. This enzyme is also called CbiL.

In enzymology, a 10-hydroxydihydrosanguinarine 10-O-methyltransferase () is an enzyme that catalyzes the chemical reaction :S-adenosyl-L-methionine + 10-hydroxydihydrosanguinarine \rightleftharpoons S-adenosyl-L-homocysteine + dihydrochelirubine Thus, the two substrates of this enzyme are S-adenosyl methionine and 10-hydroxydihydrosanguinarine, whereas its two products are S-adenosylhomocysteine and dihydrochelirubine. This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L- methionine:10-hydroxydihydrosanguinarine 10-O-methyltransferase. This enzyme participates in alkaloid biosynthesis i.

In enzymology, a 12-hydroxydihydrochelirubine 12-O-methyltransferase () is an enzyme that catalyzes the chemical reaction :S-adenosyl-L-methionine + 12-hydroxydihydrochelirubine \rightleftharpoons S-adenosyl-L-homocysteine + dihydromacarpine Thus, the two substrates of this enzyme are S-adenosyl methionine and 12-hydroxydihydrochelirubine, whereas its two products are S-adenosylhomocysteine and dihydromacarpine. This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L- methionine:12-hydroxydihydrochelirubine 12-O-methyltransferase. This enzyme participates in alkaloid biosynthesis i.

In enzymology, a 6-hydroxymellein O-methyltransferase () is an enzyme that catalyzes the chemical reaction :S-adenosyl-L-methionine + 6-hydroxymellein \rightleftharpoons S-adenosyl-L-homocysteine + 6-methoxymellein Thus, the two substrates of this enzyme are S-adenosyl methionine and 6-hydroxymellein, whereas its two products are S-adenosylhomocysteine and 6-methoxymellein. This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:6-hydroxymellein 6-O-methyltransferase. This enzyme is also called 6-hydroxymellein methyltransferase.

In enzymology, a meso-tartrate dehydrogenase () is an enzyme that catalyzes the chemical reaction :meso-tartrate + NAD+ \rightleftharpoons dihydroxyfumarate + NADH + H+ Thus, the two substrates of this enzyme are meso-tartaric acid and NAD+, whereas its 3 products are dihydroxyfumarate, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is meso-tartrate:NAD+ oxidoreductase. This enzyme participates in glyoxylic acid and dicarboxylic acid metabolism.

In enzymology, a L-galactonolactone oxidase () is an enzyme that catalyzes the chemical reaction :L-galactono-1,4-lactone + O2 \rightleftharpoons L-ascorbate + H2O2 Thus, the two substrates of this enzyme are L-galactono-1,4-lactone and O2, whereas its two products are L-ascorbic acid and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with oxygen as acceptor. The systematic name of this enzyme class is L-galactono-1,4-lactone:oxygen 3-oxidoreductase. This enzyme is also called L-galactono-1,4-lactone oxidase.

In enzymology, a pimeloyl-CoA dehydrogenase () is an enzyme that catalyzes the chemical reaction :pimeloyl-CoA + NAD+ \rightleftharpoons 6-carboxyhex-2-enoyl-CoA + NADH + H+ Thus, the two substrates of this enzyme are pimeloyl-CoA and NAD+, whereas its 3 products are 6-carboxyhex-2-enoyl- CoA, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is pimeloyl-CoA:NAD+ oxidoreductase. This enzyme participates in benzoate degradation via coa ligation.

In enzymology, a secologanin synthase (, was wrongly classified as in the past) is an enzyme that catalyzes the chemical reaction :loganin + NADPH + H+ \+ O2 \rightleftharpoons secologanin + NADP+ \+ 2 H2O The 4 substrates of this enzyme are loganin, NADPH, H+, and O2, whereas its 3 products are secologanin, NADP+, and H2O. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with oxygen as acceptor. The systematic name of this enzyme class is loganin:oxygen oxidoreductase (ring-cleaving). This enzyme participates in indole and ipecac alkaloid biosynthesis.

In enzymology, a cis-dihydroethylcatechol dehydrogenase () is an enzyme that catalyzes the chemical reaction :cis-1,2-dihydro-3-ethylcatechol + NAD+ \rightleftharpoons 3-ethylcatechol + NADH + H+ Thus, the two substrates of this enzyme are cis-1,2-dihydro-3-ethylcatechol and NAD+, whereas its 3 products are 3-ethylcatechol, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is cis-1,2-dihydro-3-ethylcatechol:NAD+ oxidoreductase. This enzyme participates in ethylbenzene degradation.

In enzymology, divinyl chlorophyllide a 8-vinyl-reductase () is an enzyme that catalyzes the chemical reaction :3,8-divinylprotochlorophyllide + NADPH + H+ \rightleftharpoons protochlorophyllide + NADP+ The three substrates of this enzyme are 3,8-divinylprotochlorophyllide, NADPH, and H+; its two products are protochlorophyllide and NADP+. This enzyme can also convert alternative substrates, for example 3,8-divinyl chlorophyllide a and in all cases reduces a single specific vinyl group to an ethyl group. This enzyme belongs to the family of oxidoreductases. The systematic name of this enzyme class is chlorophyllide-a :NADP+ oxidoreductase.

In enzymology, a 2,4-dichlorobenzoyl-CoA reductase () is an enzyme that catalyzes the chemical reaction :4-chlorobenzoyl-CoA + NADP+ \+ HCl \rightleftharpoons 2,4-dichlorobenzoyl-CoA + NADPH + H+ The 3 substrates of this enzyme are 4-chlorobenzoyl-CoA, NADP+, and HCl, whereas its 3 products are 2,4-dichlorobenzoyl-CoA, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 4-chlorobenzoyl-CoA:NADP+ oxidoreductase (halogenating). This enzyme participates in 2,4-dichlorobenzoate degradation.

In enzymology, a 2-coumarate reductase or melilotate dehydrogenase () is an enzyme that catalyzes the chemical reaction :3-(2-hydroxyphenyl)propanoate + NAD+ \rightleftharpoons 2-coumarate + NADH + H+ Thus, the two substrates of this enzyme are 3-(2-hydroxyphenyl)propanoate and NAD+, whereas its 3 products are 2-coumarate, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 3-(2-hydroxyphenyl)propanoate:NAD+ oxidoreductase. This enzyme participates in phenylalanine metabolism.

In enzymology, a 1,2-dihydrovomilenine reductase () is an enzyme that catalyzes the chemical reaction :17-O-acetylnorajmaline + NADP \rightleftharpoons 1,2-dihydrovomilenine + NADPH + H Thus, the two substrates of this enzyme are 17-O-acetylnorajmaline and NADP, whereas its 3 products are 1,2-dihydrovomilenine, NADPH, and H. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 17-O-acetylnorajmaline:NADP+ oxidoreductase. This enzyme participates in indole and ipecac alkaloid biosynthesis.

Based on the observations of what happens when there is no substrate, or oxygen, the following steps seem to constitute the hydroxylation reaction. In the absence of oxygen, dopamine or other substrates, the enzyme and ascorbate mixture produces reduced enzyme and dehydroascorbate. Exposing the reduced enzyme to oxygen and dopamine results in oxidation of the enzyme and formation of noradrenaline and water, and this step doesn't require ascorbate. Although details of DBH mechanism are yet to be confirmed, DBH is homologous to another enzyme, peptidylglycine α-hydroxylating monooxygenase (PHM).

In enzymology, a (RS)-norcoclaurine 6-O-methyltransferase () is an enzyme that catalyzes the chemical reaction :S-adenosyl-L-methionine + (RS)-norcoclaurine \rightleftharpoons S-adenosyl-L-homocysteine + (RS)-coclaurine Thus, the two substrates of this enzyme are S-adenosyl methionine and (R,S)-norcoclaurine, whereas its two products are S-adenosylhomocysteine and (R,S)-coclaurine. This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:(RS)-norcoclaurine 6-O-methyltransferase. This enzyme participates in alkaloid biosynthesis i.

In enzymology, a (S)-coclaurine-N-methyltransferase () is an enzyme that catalyzes the chemical reaction :S-adenosyl-L-methionine + (S)-coclaurine \rightleftharpoons S-adenosyl-L-homocysteine + (S)-N-methylcoclaurine Thus, the two substrates of this enzyme are S-adenosyl methionine and (S)-coclaurine, whereas its two products are S-adenosylhomocysteine and (S)-N-methylcoclaurine. This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L- methionine:(S)-coclaurine-N-methyltransferase. This enzyme participates in alkaloid biosynthesis i.

In enzymology, a (S)-scoulerine 9-O-methyltransferase () is an enzyme that catalyzes the chemical reaction :S-adenosyl-L-methionine + (S)-scoulerine \rightleftharpoons S-adenosyl-L-homocysteine + (S)-tetrahydrocolumbamine Thus, the two substrates of this enzyme are S-adenosyl methionine and (S)-scoulerine, whereas its two products are S-adenosylhomocysteine and (S)-tetrahydrocolumbamine. This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:(S)-scoulerine 9-O-methyltransferase. This enzyme participates in alkaloid biosynthesis i.

In enzymology, a tetrahydrocolumbamine 2-O-methyltransferase () is an enzyme that catalyzes the chemical reaction :S-adenosyl-L-methionine + 5,8,13,13a-tetrahydrocolumbamine \rightleftharpoons S-adenosyl-L-homocysteine + tetrahydropalmatine Thus, the two substrates of this enzyme are S-adenosyl methionine and 5,8,13,13a-tetrahydrocolumbamine, whereas its two products are S-adenosylhomocysteine and tetrahydropalmatine. This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L- methionine:5,8,13,13a-tetrahydrocolumbamine 2-O-methyltransferase. This enzyme is also called tetrahydrocolumbamine methyltransferase.

In enzymology, a tetrahydromethanopterin S-methyltransferase () is an enzyme that catalyzes the chemical reaction :5-methyl-5,6,7,8-tetrahydromethanopterin + 2-mercaptoethanesulfonate \rightleftharpoons 5,6,7,8-tetrahydromethanopterin + 2-(methylthio)ethanesulfonate Thus, the two substrates of this enzyme are 5-methyl-5,6,7,8-tetrahydromethanopterin and 2-mercaptoethanesulfonate, whereas its two products are 5,6,7,8-tetrahydromethanopterin and 2-(methylthio)ethanesulfonate. This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is 5-methyl-5,6,7,8-tetrahydromethanopterin:2-mercaptoethanesulfonate 2-methyltransferase. This enzyme is also called tetrahydromethanopterin methyltransferase.

In enzymology, a tocopherol O-methyltransferase () is an enzyme that catalyzes the chemical reaction :S-adenosyl-L-methionine + gamma-tocopherol \rightleftharpoons S-adenosyl-L-homocysteine + alpha-tocopherol Thus, the two substrates of this enzyme are S-adenosyl methionine and gamma-tocopherol, whereas its two products are S-adenosylhomocysteine and alpha-tocopherol. This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:gamma-tocopherol 5-O-methyltransferase. This enzyme is also called gamma-tocopherol methyltransferase.

In enzymology, a phosphoethanolamine N-methyltransferase () is an enzyme that catalyzes the chemical reaction :S-adenosyl-L-methionine + ethanolamine phosphate \rightleftharpoons S-adenosyl-L-homocysteine + N-methylethanolamine phosphate Thus, the two substrates of this enzyme are S-adenosyl methionine and ethanolamine phosphate, whereas its two products are S-adenosylhomocysteine and N-methylethanolamine phosphate. This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:ethanolamine-phosphate N-methyltransferase. This enzyme is also called phosphoethanolamine methyltransferase.

At the maximum reaction rate (Vmax) of the enzyme, all the enzyme active sites are bound to substrate, and the amount of ES complex is the same as the total amount of enzyme. Vmax is only one of several important kinetic parameters. The amount of substrate needed to achieve a given rate of reaction is also important. This is given by the Michaelis–Menten constant (Km), which is the substrate concentration required for an enzyme to reach one-half its maximum reaction rate; generally, each enzyme has a characteristic KM for a given substrate.

3-Deoxy-D-arabinoheptulosonate 7-phosphate (DAHP) synthase () is the first enzyme in a series of metabolic reactions known as the shikimate pathway, which is responsible for the biosynthesis of the amino acids phenylalanine, tyrosine, and tryptophan. Since it is the first enzyme in the shikimate pathway, it controls the amount of carbon entering the pathway. Enzyme inhibition is the primary method of regulating the amount of carbon entering the pathway. Forms of this enzyme differ between organisms, but can be considered DAHP synthase based upon the reaction that is catalyzed by this enzyme.

In enzymology, a 10-hydroxytaxane O-acetyltransferase () is an enzyme that catalyzes the chemical reaction :acetyl-CoA + 10-desacetyltaxuyunnanin C \rightleftharpoons CoA + taxuyunnanin C Thus, the two substrates of this enzyme are acetyl-CoA and 10-desacetyltaxuyunnanin C, whereas its two products are CoA and taxuyunnanin C. This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acetyl-CoA:taxan-10beta-ol O-acetyltransferase. This enzyme is also called acetyl coenzyme A: 10-hydroxytaxane O-acetyltransferase.

In enzymology, an asparagine-oxo-acid transaminase () is an enzyme that catalyzes the chemical reaction :L-asparagine + a 2-oxo acid \rightleftharpoons 2-oxosuccinamate + an amino acid Thus, the two substrates of this enzyme are L-asparagine and 2-oxo acid, whereas its two products are 2-oxosuccinamate and amino acid. This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-asparagine:2-oxo-acid aminotransferase. This enzyme is also called asparagine-keto acid aminotransferase.

In enzymology, an isonocardicin synthase () is an enzyme that catalyzes the chemical reaction :S-adenosyl-L-methionine + nocardicin E \rightleftharpoons 5'-methylthioadenosine + isonocardicin A Thus, the two substrates of this enzyme are S-adenosyl-L-methionine and nocardicin E, whereas its two products are 5'-methylthioadenosine and isonocardicin A. This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is S-adenosyl-L-methionine:nocardicin-E 3-amino-3-carboxypropyltransferase. This enzyme is also called nocardicin aminocarboxypropyltransferase.

In enzymology, an O-phosphoserine sulfhydrylase () is an enzyme that catalyzes the chemical reaction :O-phospho-L-serine + hydrogen sulfide \rightleftharpoons L-cysteine + phosphate Thus, the two substrates of this enzyme are O-phospho-L-serine and hydrogen sulfide, whereas its two products are L-cysteine and phosphate. This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is O-phospho-L- serine:hydrogen-sulfide 2-amino-2-carboxyethyltransferase. This enzyme is also called O-phosphoserine(thiol)-lyase.

In enzymology, a Z-farnesyl diphosphate synthase () is an enzyme that catalyzes the chemical reaction :geranyl diphosphate + isopentenyl diphosphate \rightleftharpoons diphosphate + (2Z,6E)-farnesyl diphosphate Thus, the two substrates of this enzyme are geranyl diphosphate and isopentenyl diphosphate, whereas its two products are diphosphate and (2Z,6E)-farnesyl diphosphate. This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is geranyl-diphosphate:isopentenyl-diphosphate geranylcistransferase. This enzyme is also called (Z)-farnesyl diphosphate synthase.

In enzymology, a 4-hydroxyglutamate transaminase () is an enzyme that catalyzes the chemical reaction :4-hydroxy-L-glutamate + 2-oxoglutarate \rightleftharpoons 4-hydroxy-2-oxoglutarate + L-glutamate Thus, the two substrates of this enzyme are 4-hydroxy-L-glutamate and 2-oxoglutarate, whereas its two products are 4-hydroxy-2-oxoglutarate and L-glutamate. This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is 4-hydroxy-L-glutamate:2-oxoglutarate aminotransferase. This enzyme is also called 4-hydroxyglutamate aminotransferase.

In enzymology, an ornithine N-benzoyltransferase () is an enzyme that catalyzes the chemical reaction :2 benzoyl-CoA + L-ornithine \rightleftharpoons 2 CoA + N2,N5-dibenzoyl-L-ornithine Thus, the two substrates of this enzyme are benzoyl-CoA and L-ornithine, whereas its two products are CoA and N2,N5-dibenzoyl-L-ornithine. This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is benzoyl-CoA:L-ornithine N-benzoyltransferase. This enzyme is also called ornithine N-acyltransferase.

In enzymology, a galactolipid O-acyltransferase () is an enzyme that catalyzes the chemical reaction :2 mono-beta-D-galactosyldiacylglycerol \rightleftharpoons acylmono-beta-D-galactosyldiacylglycerol + mono-beta-D- galactosylacylglycerol Hence, this enzyme has one substrate, mono-beta-D- galactosyldiacylglycerol, and two products, acylmono-beta-D- galactosyldiacylglycerol and mono-beta-D-galactosylacylglycerol. This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is mono-beta-D-galactosyldiacylglycerol:mono-beta-D- galactosyldiacylgly cerol acyltransferase. This enzyme is also called galactolipid:galactolipid acyltransferase.

In enzymology, a phenylalanine N-acetyltransferase () is an enzyme that catalyzes the chemical reaction :acetyl-CoA + L-phenylalanine \rightleftharpoons CoA + N-acetyl-L-phenylalanine Thus, the two substrates of this enzyme are acetyl-CoA and L-phenylalanine, whereas its two products are CoA and N-acetyl-L-phenylalanine. This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acetyl- CoA:L-phenylalanine N-acetyltransferase. This enzyme is also called acetyl- CoA-L-phenylalanine alpha-N-acetyltransferase.

In enzymology, a N-acetylneuraminate 4-O-acetyltransferase () is an enzyme that catalyzes the chemical reaction :acetyl-CoA + N-acetylneuraminate \rightleftharpoons CoA + N-acetyl-4-O-acetylneuraminate Thus, the two substrates of this enzyme are acetyl-CoA and N-acetylneuraminate, whereas its two products are CoA and N-acetyl-4-O-acetylneuraminate. This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acetyl-CoA:N-acetylneuraminate 4-O-acetyltransferase. This enzyme is also called sialate O-acetyltransferase.

In enzymology, a diacylglycerol-sterol O-acyltransferase () is an enzyme that catalyzes the chemical reaction :1,2-diacyl-sn-glycerol + sterol \rightleftharpoons monoacylglycerol + sterol ester Thus, the two substrates of this enzyme are 1,2-diacyl-sn-glycerol and sterol, whereas its two products are monoacylglycerol and sterol ester. This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is 1,2-diacyl- sn-glycerol:sterol O-acyltransferase. This enzyme is also called 1,2-diacyl- sn-glycerol:sterol acyl transferase.

In enzymology, an acridone synthase () is an enzyme that catalyzes the chemical reaction :3 malonyl-CoA + N-methylanthraniloyl-CoA \rightleftharpoons 4 CoA + 1,3-dihydroxy-N-methylacridone + 3 CO2 Thus, the two substrates of this enzyme are malonyl-CoA and N-methylanthraniloyl-CoA, whereas its 3 products are CoA, 1,3-dihydroxy-N-methylacridone, and CO2. This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is malonyl-CoA:N-methylanthraniloyl-CoA malonyltransferase (cyclizing). This enzyme participates in acridone alkaloid biosynthesis.

In enzymology, a 2alpha-hydroxytaxane 2-O-benzoyltransferase () is an enzyme that catalyzes the chemical reaction :benzoyl-CoA + 10-deacetyl-2-debenzoylbaccatin III \rightleftharpoons CoA + 10-deacetylbaccatin III Thus, the two substrates of this enzyme are benzoyl- CoA and 10-deacetyl-2-debenzoylbaccatin III, whereas its two products are CoA and 10-deacetylbaccatin III. This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is benzoyl- CoA:taxan-2alpha-ol O-benzoyltransferase. This enzyme is also called benzoyl- CoA:taxane 2alpha-O-benzoyltransferase.

In enzymology, a D-proline reductase (dithiol) () is an enzyme that catalyzes the chemical reaction :5-aminopentanoate + lipoate \rightleftharpoons D-proline + dihydrolipoate Thus, the two substrates of this enzyme are 5-aminopentanoate and lipoate, whereas its two products are D-proline and dihydrolipoate. This enzyme belongs to the family of oxidoreductases, specifically those acting on X-H and Y-H to form an X-Y bond with a disulfide as acceptor. The systematic name of this enzyme class is 5-aminopentanoate:lipoate oxidoreductase (cyclizing). This enzyme participates in arginine and proline metabolism.

In enzymology, a sulochrin oxidase [(−)-bisdechlorogeodin-forming] () is an enzyme that catalyzes the chemical reaction :2 sulochrin + O2 \rightleftharpoons 2 (−)-bisdechlorogeodin + 2 H2O Thus, the two substrates of this enzyme are sulochrin and O2, whereas its two products are (−)-bisdechlorogeodin and H2O. This enzyme belongs to the family of oxidoreductases, specifically those acting on X-H and Y-H to form an X-Y bond with oxygen as acceptor. The systematic name of this enzyme class is sulochrin:oxygen oxidoreductase (cyclizing, (−)-specific). This enzyme is also called sulochrin oxidase.

In enzymology, a sulochrin oxidase [(+)-bisdechlorogeodin-forming] () is an enzyme that catalyzes the chemical reaction :2 sulochrin + O2 \rightleftharpoons 2 (+)-bisdechlorogeodin + 2 H2O Thus, the two substrates of this enzyme are sulochrin and O2, whereas its two products are (+)-bisdechlorogeodin and H2O. This enzyme belongs to the family of oxidoreductases, specifically those acting on X-H and Y-H to form an X-Y bond with oxygen as acceptor. The systematic name of this enzyme class is sulochrin:oxygen oxidoreductase (cyclizing, (+)-specific). This enzyme is also called sulochrin oxidase.

In enzymology, a hypotaurine dehydrogenase () is an enzyme that catalyzes the chemical reaction :hypotaurine + H2O + NAD+ \rightleftharpoons taurine + NADH + H+ The 3 substrates of this enzyme are hypotaurine, H2O, and NAD+, whereas its 3 products are taurine, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is hypotaurine:NAD+ oxidoreductase. This enzyme participates in taurine and hypotaurine metabolism. It has 2 cofactors: heme, and Molybdenum.

Adenylyl-sulfate reductase (thioredoxin) () is an enzyme that catalyzes the chemical reaction :AMP + sulfite + thioredoxin disulfide \rightleftharpoons 5'-adenylyl sulfate + thioredoxin The 3 substrates of this enzyme are adenosine monophosphate, sulfite, and thioredoxin disulfide, whereas its two products are 5'-adenylyl sulfate and thioredoxin. This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with a disulfide as acceptor. The systematic name of this enzyme class is AMP, sulfite:thioredoxin-disulfide oxidoreductase (adenosine-5'-phosphosulfate-forming). This enzyme is also called thioredoxin- dependent 5'-adenylylsulfate reductase.

Berberine reductase () is an enzyme that catalyzes the chemical reaction :(R)-canadine + 2 NADP+ \rightleftharpoons berberine + 2 NADPH + H+ Thus, the two substrates of this enzyme are (R)-canadine and nicotinamide adenine dinucleotide phosphate ion, whereas its 3 products are berberine, nicotinamide adenine dinucleotide phosphate, and hydrogen ion. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (R)-tetrahydroberberine:NADP+ oxidoreductase. This enzyme is also called (R)-canadine synthase.

In enzymology, a dimethylamine dehydrogenase () is an enzyme that catalyzes the chemical reaction :dimethylamine + H2O + electron-transferring flavoprotein \rightleftharpoons methylamine + formaldehyde + reduced electron- transferring flavoprotein The 3 substrates of this enzyme are dimethylamine, H2O, and electron-transferring flavoprotein, whereas its 3 products are methylamine, formaldehyde, and reduced electron-transferring flavoprotein. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with a flavin as acceptor. The systematic name of this enzyme class is dimethylamine:electron-transferring flavoprotein oxidoreductase. This enzyme participates in methane metabolism.

In enzymology, a 3-aci-nitropropanoate oxidase () is an enzyme that catalyzes the chemical reaction :3-aci-nitropropanoate + O2 \+ H2O \rightleftharpoons 3-oxopropanoate + nitrite + H2O2 The 3 substrates of this enzyme are 3-aci- nitropropanoate, O2, and H2O, whereas its 3 products are 3-oxopropanoate, nitrite, and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on other nitrogenous compounds as donors with oxygen as acceptor. The systematic name of this enzyme class is 3-aci- nitropropanoate:oxygen oxidoreductase. This enzyme is also called propionate-3-nitronate oxidase.

In enzymology, a malonate-semialdehyde dehydrogenase () is an enzyme that catalyzes the chemical reaction :3-oxopropanoate + NAD(P)+ + H2O \rightleftharpoons malonate + NAD(P)H + 2 H+ The 4 substrates of this enzyme are 3-oxopropanoate, NAD+, NADP+, and H2O, whereas its 4 products are malonate, NADH, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 3-oxopropanoate:NAD(P)+ oxidoreductase. This enzyme participates in beta- alanine metabolism.

In enzymology, an oxoglutarate dehydrogenase (NADP+) () is an enzyme that catalyzes the chemical reaction :2-oxoglutarate + CoA + NADP+ \rightleftharpoons succinyl-CoA + CO2 \+ NADPH The 3 substrates of this enzyme are 2-oxoglutarate, CoA, and NADP+, whereas its 3 products are succinyl-CoA, CO2, and NADPH. This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 2-oxoglutarate:NADP+ 2-oxidoreductase (CoA-succinylating). This enzyme is also called oxoglutarate dehydrogenase (NADP+).

In enzymology, a glyoxylate dehydrogenase (acylating) () is an enzyme that catalyzes the chemical reaction :glyoxylate + CoA + NADP+ \rightleftharpoons oxalyl-CoA + NADPH + H+ The 3 substrates of this enzyme are glyoxylate, CoA, and NADP+, whereas its 3 products are oxalyl-CoA, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is glyoxylate:NADP+ oxidoreductase (CoA- oxalylating). This enzyme participates in glyoxylate and dicarboxylate metabolism.

In enzymology, a hexadecanal dehydrogenase (acylating) () is an enzyme that catalyzes the chemical reaction :hexadecanal + CoA + NAD+ \rightleftharpoons hexadecanoyl-CoA + NADH + H+ The 3 substrates of this enzyme are hexadecanal, CoA, and NAD+, whereas its 3 products are hexadecanoyl-CoA, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is hexadecanal:NAD+ oxidoreductase (CoA- acylating). This enzyme is also called fatty acyl-CoA reductase.

In enzymology, a mannitol dehydrogenase (cytochrome) () is an enzyme that catalyzes the chemical reaction :D-mannitol + ferricytochrome c \rightleftharpoons D-fructose + ferrocytochrome c Thus, the two substrates of this enzyme are D-mannitol and ferricytochrome c, whereas its two products are D-fructose and ferrocytochrome c. This enzyme belongs to the family of oxidoreductases, to be specific those acting on the CH-OH group of donor with a cytochrome as acceptor. The systematic name of this enzyme class is D-mannitol:ferricytochrome-c 2-oxidoreductase. This enzyme is also called polyol dehydrogenase.

In enzymology, a hydroxyacid-oxoacid transhydrogenase () is an enzyme that catalyzes the chemical reaction :(S)-3-hydroxybutanoate + 2-oxoglutarate \rightleftharpoons acetoacetate + (R)-2-hydroxyglutarate Thus, the two substrates of this enzyme are (S)-3-hydroxybutanoate and 2-oxoglutarate, whereas its two products are acetoacetate and (R)-2-hydroxyglutarate. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other acceptors. The systematic name of this enzyme class is (S)-3-hydroxybutanoate:2-oxoglutarate oxidoreductase. This enzyme is also called transhydrogenase, hydroxy acid-oxo acid.

In enzymology, a 4-hydroxymuconic-semialdehyde dehydrogenase () is an enzyme that catalyzes the chemical reaction :4-hydroxymuconic semialdehyde + NAD+ \+ H2O \rightleftharpoons maleylacetate + NADH + 2 H+ The 3 substrates of this enzyme are 4-hydroxymuconic semialdehyde, NAD+, and H2O, whereas its 3 products are maleylacetate, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 4-hydroxymuconic-semialdehyde:NAD+ oxidoreductase. This enzyme participates in gamma-hexachlorocyclohexane degradation.

In enzymology, an aryl-aldehyde dehydrogenase () is an enzyme that catalyzes the chemical reaction :an aromatic aldehyde + NAD+ \+ H2O \rightleftharpoons an aromatic acid + NADH + H+ The 3 substrates of this enzyme are aromatic aldehyde, NAD+, and H2O, whereas its 3 products are aromatic acid, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is aryl-aldehyde:NAD+ oxidoreductase. This enzyme participates in tyrosine metabolism and biphenyl degradation.

In enzymology, a butanal dehydrogenase () is an enzyme that catalyzes the chemical reaction :butanal + CoA + NAD(P)+ \rightleftharpoons butanoyl-CoA + NAD(P)H + H+ The 4 substrates of this enzyme are butanal, CoA, NAD+, and NADP+, whereas its 4 products are butanoyl-CoA, NADH, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is butanal:NAD(P)+ oxidoreductase (CoA- acylating). This enzyme participates in butanoate metabolism.

In enzymology, a 4-formylbenzenesulfonate dehydrogenase () is an enzyme that catalyzes the chemical reaction :4-formylbenzenesulfonate + NAD+ \+ H2O \rightleftharpoons 4-sulfobenzoate + NADH + 2 H+ The 3 substrates of this enzyme are 4-formylbenzenesulfonate, NAD+, and H2O, whereas its 3 products are 4-sulfobenzoate, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 4-formylbenzenesulfonate:NAD+ oxidoreductase. This enzyme participates in 2,4-dichlorobenzoate degradation.

In enzymology, a hydroxyphytanate oxidase () is an enzyme that catalyzes the chemical reaction :L-2-hydroxyphytanate + O2 \rightleftharpoons 2-oxophytanate + H2O2 Thus, the two substrates of this enzyme are L-2-hydroxyphytanate and O2, whereas its two products are 2-oxophytanate and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. The systematic name of this enzyme class is L-2-hydroxyphytanate:oxygen 2-oxidoreductase. This enzyme is also called L-2-hydroxyphytanate:oxygen 2-oxidoreductase.

In enzymology, a malate oxidase () is an enzyme that catalyzes the chemical reaction :(S)-malate + O2 \rightleftharpoons oxaloacetate + H2O2 Thus, the two substrates of this enzyme are (S)-malate and O2, whereas its two products are oxaloacetate and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. The systematic name of this enzyme class is (S)-malate:oxygen oxidoreductase. Other names in common use include FAD-dependent malate oxidase, malic oxidase, and malic dehydrogenase II. This enzyme participates in pyruvate metabolism.

In enzymology, a D-sorbitol dehydrogenase (acceptor) () is an enzyme that catalyzes the chemical reaction :D-sorbitol + acceptor \rightleftharpoons L-sorbose + reduced acceptor Thus, the two substrates of this enzyme are D-sorbitol and acceptor, whereas its two products are L-sorbose and reduced acceptor. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other acceptors. The systematic name of this enzyme class is D-sorbitol:acceptor 1-oxidoreductase. This enzyme is also called D-sorbitol:(acceptor) 1-oxidoreductase.

In enzymology, a L-ascorbate—cytochrome-b5 reductase () is an enzyme that catalyzes the chemical reaction :L-ascorbate + ferricytochrome b5 \rightleftharpoons monodehydroascorbate + ferrocytochrome b5 \+ H+ Thus, the two substrates of this enzyme are L-ascorbate and ferricytochrome b5, whereas its 3 products are monodehydroascorbate, ferrocytochrome b5, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on diphenols and related substances as donor with a cytochrome as acceptor. The systematic name of this enzyme class is L-ascorbate:ferricytochrome-b5 oxidoreductase. This enzyme is also called ascorbate-cytochrome b5 reductase.

In enzymology, a phenylacetyl-CoA dehydrogenase () is an enzyme that catalyzes the chemical reaction :phenylacetyl-CoA + H2O + 2 quinone \rightleftharpoons phenylglyoxylyl-CoA + 2 quinol The 3 substrates of this enzyme are phenylacetyl-CoA, H2O, and quinone, whereas its two products are phenylglyoxylyl-CoA and quinol. This enzyme belongs to the family of oxidoreductases, specifically those acting on CH or CH2 groups with a quinone or similar compound as acceptor. The systematic name of this enzyme class is phenylacetyl-CoA:quinone oxidoreductase. This enzyme is also called phenylacetyl-CoA:acceptor oxidoreductase.

In enzymology, an acetylacetone-cleaving enzyme () is an enzyme that catalyzes the chemical reaction :pentane-2,4-dione + O2 \rightleftharpoons acetate + 2-oxopropanal Thus, the two substrates of this enzyme are pentane-2,4-dione and O2, whereas its two products are acetate and 2-oxopropanal. This enzyme belongs to the family of oxidoreductases, specifically those acting on single donors with O2 as oxidant and incorporation of two atoms of oxygen into the substrate (oxygenases). The oxygen incorporated need not be derived from O2. The systematic name of this enzyme class is acetylacetone:oxygen oxidoreductase.

In enzymology, a L-pipecolate dehydrogenase () is an enzyme that catalyzes the chemical reaction :L-pipecolate + acceptor \rightleftharpoons 2,3,4,5-tetrahydropyridine-2-carboxylate + reduced acceptor Thus, the two substrates of this enzyme are L-pipecolate and acceptor, whereas its two products are 2,3,4,5-tetrahydropyridine-2-carboxylate and reduced acceptor. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with other acceptors. The systematic name of this enzyme class is L-pipecolate:acceptor 1,6-oxidoreductase. This enzyme is also called L-pipecolate:(acceptor) 1,6-oxidoreductase.

In enzymology, a polyamine oxidase () is an enzyme that catalyzes the chemical reaction :N1-acetylspermine + O2 \+ H2O \rightleftharpoons N1-acetylspermidine + 3-aminopropanal + H2O2 The 3 substrates of this enzyme are N1-acetylspermine, O2, and H2O, whereas its 3 products are N1-acetylspermidine, 3-aminopropanal, and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with oxygen as acceptor. The systematic name of this enzyme class is N1-acetylspermidine:oxygen oxidoreductase (deaminating). This enzyme is also called 1-N-acetylspermidine:oxygen oxidoreductase (deaminating).

In enzymology, a prenylcysteine oxidase () is an enzyme that catalyzes the chemical reaction :an S-prenyl-L-cysteine + O2 \+ H2O \rightleftharpoons a prenal + L-cysteine + H2O2 The 3 substrates of this enzyme are S-prenyl-L- cysteine, O2, and H2O, whereas its 3 products are prenal, L-cysteine, and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with oxygen as acceptor. The systematic name of this enzyme class is S-prenyl-L-cysteine:oxygen oxidoreductase. This enzyme is also called prenylcysteine lyase.

In enzymology, a L-aspartate oxidase () is an enzyme that catalyzes the chemical reaction :L-aspartate + H2O + O2 \rightleftharpoons oxaloacetate + NH3 \+ H2O2 The 3 substrates of this enzyme are L-aspartate, H2O, and O2, whereas its 3 products are oxaloacetate, NH3, and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with oxygen as acceptor. The systematic name of this enzyme class is L-aspartate:oxygen oxidoreductase (deaminating). This enzyme participates in alanine and aspartate metabolism and nicotinate and nicotinamide metabolism.

In enzymology, a thiol oxidase () is an enzyme that catalyzes the chemical reaction :4 R'C(R)SH + O2 \rightleftharpoons 2 R'C(R)S-S(R)CR' + 2 H2O Thus, the two substrates of this enzyme are R'C(R)SH and O2, whereas its two products are R'C(R)S-S(R)CR' and H2O. This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with oxygen as acceptor. The systematic name of this enzyme class is thiol:oxygen oxidoreductase. This enzyme is also called sulfhydryl oxidase.

In enzymology, a trimethylamine dehydrogenase () is an enzyme that catalyzes the chemical reaction :trimethylamine + H2O + electron-transferring flavoprotein \rightleftharpoons dimethylamine + formaldehyde + reduced electron-transferring flavoprotein The 3 substrates of this enzyme are trimethylamine, H2O, and electron-transferring flavoprotein, whereas its 3 products are dimethylamine, formaldehyde, and reduced electron-transferring flavoprotein. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with a flavin as acceptor. The systematic name of this enzyme class is trimethylamine:electron- transferring flavoprotein oxidoreductase (demethylating). This enzyme participates in methane metabolism.

In enzymology, a 5-carboxymethyl-2-hydroxymuconate Delta-isomerase () is an enzyme that catalyzes the chemical reaction :5-carboxymethyl-2-hydroxymuconate \rightleftharpoons 5-carboxy-2-oxohept-3-enedioate Hence, this enzyme has one substrate, 5-carboxymethyl-2-hydroxymuconate, and one product, 5-carboxy-2-oxohept-3-enedioate. This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases transposing C=C bonds. The systematic name of this enzyme class is 5-carboxymethyl-2-hydroxymuconate Delta2,Delta4-2-oxo,Delta3-isomerase. This enzyme participates in tyrosine metabolism and benzoate degradation via hydroxylation.

In enzymology, an ADP-L-glycero-D-manno-heptose 6-epimerase () is an enzyme that catalyzes the chemical reaction :ADP-D-glycero-D-manno-heptose \rightleftharpoons ADP-L-glycero-D-manno-heptose Hence, this enzyme has one substrate, ADP-D-glycero-D-manno-heptose, and one product, ADP-L-glycero-D- manno-heptose. This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on carbohydrates and derivatives. The systematic name of this enzyme class is ADP-L-glycero-D-manno-heptose 6-epimerase. This enzyme participates in lipopolysaccharide biosynthesis.

In enzymology, a 2-aminohexano-6-lactam racemase () is an enzyme that catalyzes the chemical reaction :L-2-aminohexano-6-lactam \rightleftharpoons D-2-aminohexano-6-lactam Hence, this enzyme has one substrate, L-2-aminohexano-6-lactam, and one product, D-2-aminohexano-6-lactam. This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on amino acids and derivatives. The systematic name of this enzyme class is 2-aminohexano-6-lactam racemase. This enzyme is also called alpha-amino-epsilon-caprolactam racemase.

In enzymology, a carboxy-cis,cis-muconate cyclase () is an enzyme that catalyzes the chemical reaction :3-carboxy-2,5-dihydro-5-oxofuran-2-acetate \rightleftharpoons 3-carboxy-cis,cis-muconate Hence, this enzyme has one substrate, 3-carboxy-2,5-dihydro-5-oxofuran-2-acetate, and one product, 3-carboxy-cis,cis-muconate. This enzyme belongs to the family of isomerases, specifically the class of intramolecular lyases. The systematic name of this enzyme class is 3-carboxy-2,5-dihydro-5-oxofuran-2-acetate lyase (decyclizing). This enzyme is also called 3-carboxymuconate cyclase.

In enzymology, a dichloromuconate cycloisomerase () is an enzyme that catalyzes the chemical reaction :2,4-dichloro-2,5-dihydro-5-oxofuran-2-acetate \rightleftharpoons 2,4-dichloro-cis,cis-muconate Hence, this enzyme has one substrate, 2,4-dichloro-2,5-dihydro-5-oxofuran-2-acetate, and one product, 2,4-dichloro-cis,cis-muconate. This enzyme belongs to the family of isomerases, specifically the class of intramolecular lyases. The systematic name of this enzyme class is 2,4-dichloro-2,5-dihydro-5-oxofuran-2-acetate lyase (decyclizing). This enzyme participates in 1,4-dichlorobenzene degradation.

In enzymology, a muconolactone Delta-isomerase () is an enzyme that catalyzes the chemical reaction :(S)-5-oxo-2,5-dihydrofuran-2-acetate \rightleftharpoons 5-oxo-4,5-dihydrofuran-2-acetate Hence, this enzyme has one substrate, (S)-5-oxo-2,5-dihydrofuran-2-acetate, and one product, 5-oxo-4,5-dihydrofuran-2-acetate. This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases transposing C=C bonds. The systematic name of this enzyme class is 5-oxo-4,5-dihydrofuran-2-acetate Delta3-Delta2-isomerase. This enzyme is also called muconolactone isomerase.

In enzymology, an O-demethylpuromycin O-methyltransferase () is an enzyme that catalyzes the chemical reaction :S-adenosyl-L-methionine + O-demethylpuromycin \rightleftharpoons S-adenosyl-L-homocysteine + puromycin Thus, the two substrates of this enzyme are S-adenosyl methionine and O-demethylpuromycin, whereas its two products are S-adenosylhomocysteine and puromycin. This enzyme belongs to the family of transferases, specifically those transferring one- carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:O-demethylpuromycin O-methyltransferase. This enzyme is also called O-demethylpuromycin methyltransferase.