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"catalyses" Synonyms
results ends in culminates in involves leads to prompts elicits precipitates triggers sparks off provokes causes brings about occasions effects brings to pass contributes to gives rise to creates produces carries out accomplishes achieves attains fulfils(UK) fulfills(US) completes reaches realises(UK) consummates effectuates realizes(US) actualizes catalyzes(US) clinches finalises(UK) finalizes(US) nails perpetrates More
"catalyses" Antonyms
results follows ensues develops arises evolves emerges emanates issues flows occurs takes place comes about proceeds derives happens manifests materializes(US) rises stems

1000 Sentences With "catalyses"

How to use catalyses in a sentence? Find typical usage patterns (collocations)/phrases/context for "catalyses" and check conjugation/comparative form for "catalyses". Mastering all the usages of "catalyses" from sentence examples published by news publications.

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"The eruption of halogens into the stratosphere catalyses ozone-destroying reactions, raising surface levels of biologically damaging UV radiation," the authors wrote in the paper.
The report catalyses the debate about conditions for workers on gig economy platforms, and raises serious questions about the wider societal impacts of tax avoiding, VC-funded tech giants.
After all, a catchy-sounding song sparks an almost automatic kinetic link to it; it catalyses a yearning to dance to along, even when we're not sure what's being said.
In bacteria and plants this protein domain only catalyses the synthesis of SAICAR. However, in mammals it also catalyses phosphoribosylaminoimidazole carboxylase (AIRC) activity.
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.
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.
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.
Molybdenum cofactor guanylyltransferase (, MobA, MoCo guanylyltransferase) is an enzyme with systematic name GTP:molybdenum cofactor guanylyltransferase. This enzyme catalyses the following chemical reaction: : GTP + molybdenum cofactor \rightleftharpoons diphosphate + guanylyl molybdenum cofactor Catalyses the guanylation of the molybdenum cofactor.
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.
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.
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.
Molybdenum cofactor cytidylyltransferase (, MocA, CTP:molybdopterin cytidylyltransferase, MoCo cytidylyltransferase, Mo-MPT cytidyltransferase) is an enzyme with systematic name CTP:molybdenum cofactor cytidylyltransferase. This enzyme catalyses the following chemical reaction: : CTP + molybdenum cofactor \rightleftharpoons diphosphate + cytidylyl molybdenum cofactor Catalyses the cytidylation of the molybdenum cofactor.
Molybdopterin molybdotransferase (, MoeA, Cnx1) is an enzyme with systematic name adenylyl-molybdopterin:molybdate molybdate transferase (AMP-forming). This enzyme catalyses the following chemical reaction : adenylyl-molybdopterin + molybdate \rightleftharpoons molybdenum cofactor + AMP Catalyses the insertion of molybdenum into the ene-dithiol group of molybdopterin.
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.
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.
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.
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.
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 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.
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.
MTO catalyses for the oxidations with hydrogen peroxide. Terminal alkynes yield the corresponding acid or ester, internal alkynes yield diketones, and alkenes give epoxides. MTO also catalyses the conversion of aldehydes and diazoalkanes into an alkene.Hudson, A. (2002) “Methyltrioxorhenium” in Encyclopedia of Reagents for Organic Synthesis.
Cyclic pyranopterin monophosphate synthase (, MOCS1A, MoaA, MoaC, molybdenum cofactor biosynthesis protein 1) is an enzyme with systematic name GTP 8,9-lyase (cyclic pyranopterin monophosphate-forming). This enzyme catalyses the following chemical reaction : GTP \rightleftharpoons cyclic pyranopterin monophosphate + diphosphate This enzyme catalyses an early step in the biosynthesis of molybdopterin.
Phosphonoacetaldehyde reductase (NADH) (, PhpC) is an enzyme with systematic name 2-hydroxyethylphosphonate:NAD+ oxidoreductase. This enzyme catalyses the following chemical reaction : 2-hydroxyethylphosphonate + NAD+ \rightleftharpoons phosphonoacetaldehyde + NADH + H+ The enzyme from Streptomyces viridochromogenes catalyses a step in the biosynthesis of phosphinothricin tripeptide, the reduction of phosphonoacetaldehyde to 2-hydroxyethylphosphonate.
L-galactose 1-dehydrogenase (, L-GalDH, L-galactose dehydrogenase) is an enzyme with the systematic name L-galactose:NAD+ 1-oxidoreductase. This enzyme catalyses the following chemical reaction: : L-galactose + NAD+ \rightleftharpoons L-galactono-1,4-lactone + NADH + H+ The enzyme catalyses a step in the ascorbate biosynthesis in higher plants.
Alpha-D-xyloside xylohydrolase (, alpha-xylosidase) is an enzyme. This enzyme catalyses the following chemical reaction : Hydrolysis of terminal, non- reducing alpha-D-xylose residues with release of alpha-D-xylose. The enzyme catalyses hydrolysis of a terminal, unsubstituted xyloside at the extreme reducing end of a xylogluco-oligosaccharide.
This CCL module catalyses the cleavage of the citryl-CoA intermediate into the products acetyl-CoA and oxaloacetate.
This protein domain provides the precursors necessary for DNA synthesis. It catalyses the biosynthesis of DNA from RNA.
This residue catalyses its own transition, first to dopaquinone and then to topaquinone, in a Cu2+ dependent manner.
Succinate-semialdehyde dehydrogenase (acylating) (, succinyl-coA reductase, coenzyme-A-dependent succinate-semialdehyde dehydrogenase) is an enzyme with systematic name succinate semialdehyde:NADP+ oxidoreductase (CoA-acylating). This enzyme catalyses the following chemical reaction : succinate semialdehyde + CoA + NADP+ \rightleftharpoons succinyl-CoA + NADPH + H+ Catalyses the NADPH-dependent reduction of succinyl-CoA to succinate semialdehyde.
Acrylyl-CoA reductase (NADPH) () is an enzyme with systematic name propanoyl- CoA:NADP+ oxidoreductase. This enzyme catalyses the following chemical reaction : propanoyl-CoA + NADP+ \rightleftharpoons acryloyl-CoA + NADPH + H+ This enzyme catalyses a step in the 3-hydroxypropionate/4-hydroxybutyrate cycle, an autotrophic CO2 fixation pathway found in some Thermoacidophilic archaea.
Flavonoid 4'-O-methyltransferase (, SOMT-2, 4'-hydroxyisoflavone methyltransferase) is an enzyme with systematic name S-adenosyl-L- methionine:flavonoid 4'-O-methyltransferase. This enzyme catalyses the following chemical reaction : S-adenosyl-L-methionine + 4'-hydroxyflavanone \rightleftharpoons S-adenosyl-L-homocysteine + 4'-methoxyflavanone The enzyme catalyses the 4'-methylation of naringenin.
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.
Aldolase () catalyses the breakdown of fructose 1,6-bisphosphate (F-1,6-BP) into glyceraldehyde 3-phosphate and dihydroxyacetone phosphate (DHAP).
Homospermidine synthase (HSS) catalyses the synthesis of the polyamine homospermidine from 2 mol putrescine in an NAD+-dependent reaction.
Ether lipid oxidase (Alkylglycerol monooxygenase, AGMO) catalyses the conversion of 1-alkyl-sn-glycerol to 1-hydroxyalkyl-sn-glycerol.
Carbazole 1,9a-dioxygenase (, CARDO) is an enzyme with systematic name 9H-carbazole,NAD(P)H:oxygen oxidoreductase (2,3-hydroxylating). This enzyme catalyses the following chemical reaction : 9H-carbazole + NAD(P)H + H+ \+ O2 \rightleftharpoons 2'-aminobiphenyl-2,3-diol + NAD(P)+ Carbazole 1,9a-dioxygenase catalyses the first reaction in the pathway of carbazole degradation.
3-hydroxypropionyl-CoA synthase (, 3-hydroxypropionyl-CoA synthetase (AMP- forming), 3-hydroxypropionate-CoA ligase) is an enzyme with systematic name hydroxypropionate:CoA ligase (AMP-forming). This enzyme catalyses the following chemical reaction : 3-hydroxypropionate + ATP + CoA \rightleftharpoons 3-hydroxypropionyl-CoA + AMP + diphosphate This enzyme catalyses a step in the 3-hydroxypropionate/4-hydroxybutyrate cycle.
Triose phosphate isomerase () catalyses the reversible interconvertion of the two triose phosphates isomers dihydroxyacetone phosphate and D-glyceraldehyde 3-phosphate.
16S rRNA (cytosine1402-N4)-methyltransferase (, RsmH, MraW) is an enzyme with systematic name S-adenosyl-L-methionine:16S rRNA (cytosine1402-N4)-methyltransferase. This enzyme catalyses the following chemical reaction : S-adenosyl-L-methionine + cytosine1402 in 16S rRNA \rightleftharpoons S-adenosyl-L-homocysteine + N4-methylcytosine1402 in 16S rRNA RsmH catalyses the N4-methylation of cytosine1402.
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.
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.
3-hydroxypropionate dehydrogenase (NADP+) () is an enzyme with systematic name 3-hydroxypropionate:NADP+ oxidoreductase. This enzyme catalyses the following chemical reaction : 3-hydroxypropionate + NADP+ \rightleftharpoons malonate semialdehyde + NADPH + H+ This enzyme catalyses the reduction of malonate semialdehyde to 3-hydroxypropionate, which is a key step in the 3-hydroxypropionate and the 3-hydroxypropionate/4-hydroxybutyrate cycles, autotrophic CO2 fixation pathways found in some green non-sulfur phototrophic bacteria and archaea, respectively. The enzyme from Chloroflexus aurantiacus is bifunctional, and also catalyses the upstream reaction in the pathway, EC 1.2.1.75. Different from EC 1.1.
23S rRNA (guanosine2251-2'-O)-methyltransferase (, rlmB (gene), yifH (gene)) is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (guanosine2251-2'-O-)-methyltransferase. This enzyme catalyses the following chemical reaction : S-adenosyl-L-methionine + guanosine2251 in 23S rRNA \rightleftharpoons S-adenosyl-L-homocysteine + 2'-O-methylguanosine2251 in 23S rRNA The enzyme catalyses the methylation of guanosine2251.
16S rRNA (cytidine1402-2'-O)-methyltransferase (, RsmI, YraL) is an enzyme with systematic name S-adenosyl-L-methionine:16S rRNA (cytidine1402-2'-O)-methyltransferase. This enzyme catalyses the following chemical reaction : S-adenosyl-L-methionine + cytidine1402 in 16S rRNA \rightleftharpoons S-adenosyl-L-homocysteine + 2'-O-methylcytidine1402 in 16S rRNA RsmI catalyses the 2'-O-methylation of cytidine1402.
Abieta-7,13-dien-18-al dehydrogenase (, abietadienal dehydrogenase (ambiguous)) is an enzyme with systematic name abieta-7,13-dien-18-al:NAD+ oxidoreductase. This enzyme catalyses the following chemical reaction : abieta-7,13-dien-18-al + H2O + NAD+ \rightleftharpoons abieta-7,13-dien-18-oate + NADH + H+ This enzyme catalyses the last step of the pathway of abietic acid biosynthesis in Abies grandis.
Pseudobaptigenin synthase () is an enzyme with systematic name calycosin,NADPH:oxygen oxidoreductase (methylenedioxy-bridge-forming). This enzyme catalyses the following chemical reaction : (1) calycosin + NADPH + H+ \+ O2 \rightleftharpoons pseudobaptigenin + NADP+ \+ 2 H2O : (2) pratensein + NADPH + H+ \+ O2 \rightleftharpoons 5-hydroxypseudobaptigenin + NADP+ + 2 H2O Pseudobaptigenin synthase is a heme-thiolate enzyme (P450) that catalyses a step in the biosynthesis of (-)-maackiain.
2-hydroxyhexa-2,4-dienoate hydratase (, tesE (gene), hsaE (gene)) is an enzyme with systematic name 4-hydroxy-2-oxohexanoate hydro-lyase ((2Z,4Z)-2-hydroxyhexa-2,4-dienoate-forming). This enzyme catalyses the following chemical reaction : 4-hydroxy-2-oxohexanoate \rightleftharpoons (2Z,4Z)-2-hydroxyhexa-2,4-dienoate + H2O This enzyme catalyses a late step in the bacterial steroid degradation pathway.
Gamma-L-glutamyl-butirosin B gamma-glutamyl cyclotransferase (, btrG (gene)) is an enzyme with systematic name gamma-L-glutamyl-butirosin B gamma-glutamyl cyclotransferase (5-oxoproline producing). This enzyme catalyses the following chemical reaction : gamma-L-glutamyl-butirosin B \rightleftharpoons butirosin B + 5-oxoproline The enzyme catalyses the last step in the biosynthesis of the aminoglycoside antibiotic butirosin B.
The fluorinase catalyses the reaction between fluoride ion and the co-factor S-adenosyl-L-methioinine (SAM) to generate 5'-fluoro-5'-deoxyadenosine (FDA) and L-methionine (L-Met).A homologous chlorinase enzyme, which catalyses the same reaction with chloride rather than fluoride ion, has been isolated from Salinospora tropica, from the biosynthetic pathway of salinosporamide A.
11-cis-retinol dehydrogenase (, RDH5 (gene)) is an enzyme with systematic name 11-cis-retinol:NAD+ oxidoreductase. This enzyme catalyses the following chemical reaction : 11-cis-retinol---[retinal-binding-protein] + NAD+ \rightleftharpoons 11-cis-retinal---[retinol-binding-protein] + NADH + H+ This enzyme from retinal pigment epithelium, catalyses the reduction of 11-cis- retinol to 11-cis-retinal.
Dichlorochromopyrrolate synthase (, RebD, dichlorochromopyrrolic acid synthase) is an enzyme with systematic name 2-imino-3-(7-chloroindol-3-yl)propanoate ammonia-lyase (dichlorochromopyrrolate-forming). This enzyme catalyses the following chemical reaction : 4 2-imino-3-(7-chloroindol-3-yl)propanoate + O2 \rightleftharpoons 2 dichlorochromopyrrolate + 2 NH3 \+ 2 H2O This enzyme catalyses a step in the biosynthesis of rebeccamycin.
Demethylrebeccamycin-D-glucose O-methyltransferase (, RebM) is an enzyme with systematic name S-adenosyl-L-methionine:demethylrebeccamycin-D-glucose O-methyltransferase. This enzyme catalyses the following chemical reaction : 4'-demethylrebeccamycin + S-adenosyl-L-methionine \rightleftharpoons rebeccamycin + S-adenosyl-L-homocysteine Demethylrebeccamycin-D-glucose O-methyltransferase catalyses the last step in the biosynthesis of rebeccamycin, an indolocarbazole alkaloid produced by the Actinobacterium Lechevalieria aerocolonigenes.
3,4-Dehydroadipyl-CoA semialdehyde dehydrogenase (NADP+) (, BoxD, 3,4-dehydroadipyl-CoA semialdehyde dehydrogenase) is an enzyme with systematic name 3,4-didehydroadipyl-CoA semialdehyde:NADP+ oxidoreductase. This enzyme catalyses the following chemical reaction : 3,4-didehydroadipyl-CoA semialdehyde + NADP+ \+ H2O \rightleftharpoons 3,4-didehydroadipyl-CoA + NADPH + H+ This enzyme catalyses a step in the aerobic benzoyl-coenzyme A catabolic pathway in Azoarcus evansii and Burkholderia xenovorans.
N1-acetylpolyamine oxidase (, hPAO-1, mPAO, hPAO) is an enzyme with systematic name N1-acetylpolyamine:oxygen oxidoreductase (3-acetamidopropanal-forming). This enzyme catalyses the following chemical reaction : (1) N1-acetylspermidine + O2 \+ H2O \rightleftharpoons putrescine + 3-acetamidopropanal + H2O2 : (2) N1-acetylspermine + O2 \+ H2O \rightleftharpoons spermidine + 3-acetamidopropanal + H2O2 This enzyme also catalyses the reaction: : N1,N12-diacetylspermine + O2 \+ H2O \rightleftharpoons N1-acetylspermidine + 3-acetamamidopropanal + H2O2.
Levopimaradiene synthase (, PtTPS-LAS, LPS, copalyl-diphosphate diphosphate- lyase [abieta-8(14),12-diene-forming]) is an enzyme with systematic name (+)-copalyl-diphosphate diphosphate-lyase (abieta-8(14),12-diene-forming). This enzyme catalyses the following chemical reaction : (+)-copalyl diphosphate \rightleftharpoons abieta-8(14),12-diene + diphosphate In Ginkgo, the enzyme catalyses the initial cyclization step in the biosynthesis of ginkgolides.
2-methylcitrate dehydratase (2-methyl-trans-aconitate forming) () is an enzyme with systematic name (2S,3S)-2-hydroxybutane-1,2,3-tricarboxylate hydro-lyase (2-methyl-trans-aconitate forming). This enzyme catalyses the following chemical reaction : (2S,3S)-2-methylcitrate \rightleftharpoons 2-methyl-trans- aconitate + H2O This enzyme catalyses the dehydration of (2S,3S)-2-methylcitrate, forming the trans isomer of 2-methyl-aconitate.
2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA isomerase (, paaG (gene), 1,2-epoxyphenylacetyl-CoA isomerase) is an enzyme with systematic name 2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA isomerase. This enzyme catalyses the following chemical reaction : 2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA \rightleftharpoons 2-oxepin-2(3H)-ylideneacetyl-CoA The enzyme catalyses the reversible isomerization of 2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA.
Dipeptidase E (, aspartyl dipeptidase, peptidase E, PepE gene product (Salmonella typhimurium)) is an enzyme. This enzyme catalyses the following chemical reaction : Dipeptidase E catalyses the hydrolysis of dipeptides Asp!Xaa. It does not act on peptides with N-terminal Glu, Asn or Gln, nor does it cleave isoaspartyl peptides A free carboxy group is not absolutely required in the substrate.
Yeast ribonuclease () is an enzyme. This enzyme catalyses the following chemical reaction : Exonucleolytic cleavage to nucleoside 3'-phosphates This enzyme is similar RNase U4.
For gram positive bacteria lysins, the N-terminal domain catalyses the hydrolysis of peptidoglycan whereas the C-terminal domain binds to the cell wall substrate.
Demethylmenaquinone methyltransferase (, S-adenosyl-L-methionine-DMK methyltransferase, demethylmenaquinone C-methylase, 2-heptaprenyl-1,4-naphthoquinone methyltransferase, 2-demethylmenaquinone methyltransferase, S-adenosyl-L-methionine:2-demethylmenaquinone methyltransferase) is an enzyme with systematic name S-adenosyl-L- methionine:demethylmenaquinone methyltransferase. This enzyme catalyses the following chemical reaction : demethylmenaquinol + S-adenosyl-L-methionine \rightleftharpoons menaquinol + S-adenosyl-L-homocysteine The enzyme catalyses the last step in menaquinone biosynthesis.
TRNA (cytosine38-C5)-methyltransferase (, hDNMT2 (gene), DNMT2 (gene), TRDMT1 (gene)) is an enzyme with the systematic name S-adenosyl-L-methionine:tRNA (cytosine38-C5)-methyltransferase. This enzyme catalyses the following chemical reaction: : S-adenosyl-L-methionine + cytosine38 in tRNA \rightleftharpoons S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNA The eukaryotic enzyme catalyses methylation of cytosine38 in the anti-codon loop of tRNAAsp(GTC), tRNAVal(AAC) and tRNAGly(GCC).
Enoyl-CoA hydratase 2 (2-enoyl-CoA hydratase 2, AtECH2, ECH2, MaoC, MFE-2, PhaJAc, D-3-hydroxyacyl-CoA hydro-lyase, D-specific 2-trans-enoyl-CoA hydratase) is an enzyme with systematic name (3R)-3-hydroxyacyl-CoA hydro- lyase. This enzyme catalyses the following chemical reaction on D-3-hydroxyacyl-CoA File:Enoyl-CoA hydratase 2 reaction.svg This enzyme catalyses a hydration step in peroxisomal beta oxidation.
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.
In Escherichia coli the activity of a NADP+-dependent form of the enzyme is controlled by the phosphorylation of a serine residue; the phosphorylated form of IDH is completely inactivated. 3-isopropylmalate dehydrogenase (IMDH) catalyses the third step in the biosynthesis of leucine in bacteria and fungi, the oxidative decarboxylation of 3-isopropylmalate into 2-oxo-4-methylvalerate. Tartrate dehydrogenase catalyses the reduction of tartrate to oxaloglycolate.
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.
3-Isopropylmalate dehydratase (E.C.4.2.1.33) is an aconitase homologue, which catalyses the isomerisation of 2-isopropylmalate to 3-isopropylmalate, via dehydration, in the biosynthesis of leucine.
This enzyme catalyses the cyclisation of 5-formylamidoimidazole-4-carboxamide ribonucleotide to IMP, a reaction which is important in de novo purine biosynthesis in archaeal species.
This enzyme catalyses the conversion of L-arabinose to L-ribulose as the first step in the pathway of L-arabinose utilization as a carbon source.
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.
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.
21S rRNA (uridine2791-2'-O)-methyltransferase (, MRM2 (gene), mitochondrial 21S rRNA methyltransferase, mitochondrial rRNA MTase 2) is an enzyme with systematic name S-adenosyl-L-methionine:21S rRNA (uridine2791-2'-O-)-methyltransferase. This enzyme catalyses the following chemical reaction : S-adenosyl-L-methionine + uridine2791 in 21S rRNA \rightleftharpoons S-adenosyl-L-homocysteine + 2'-O-methyluridine2791 in 21S rRNA The enzyme catalyses the methylation of uridine2791 of mitochondrial 21S rRNA.
2-hydroxy-6-oxo-6-(2-aminophenyl)hexa-2,4-dienoate hydrolase (, CarC) is an enzyme with systematic name (2E,4E)-6-(2-aminophenyl)-2-hydroxy-6-oxohexa-2,4-dienoate acylhydrolase. This enzyme catalyses the following chemical reaction : (2E,4E)-6-(2-aminophenyl)-2-hydroxy-6-oxohexa-2,4-dienoate + H2O \rightleftharpoons anthranilate + (2E)-2-hydroxypenta-2,4-dienoate This enzyme catalyses the third step in the aerobic degradation pathway of carbazole.
Biflaviolin synthase (, CYP158A2, CYP 158A2, cytochrome P450 158A2) is an enzyme with systematic name flaviolin,NADPH:oxygen oxidoreductase. This enzyme catalyses the following chemical reaction : (1) 2 flaviolin + NADPH + H+ \+ O2 \rightleftharpoons 3,3'-biflaviolin + NADP+ \+ 2 H2O : (2) 2 flaviolin + NADPH + H+ \+ O2 \rightleftharpoons 3,8'-biflaviolin + NADP+ \+ 2 H2O This cytochrome P450 enzyme, from the soil-dwelling bacterium Streptomyces coelicolor A3(2), catalyses a phenol oxidation C-C coupling reaction.
D-xylose reductase (, XylR, XyrA, msXR, dsXR, monospecific xylose reductase, dual specific xylose reductase, NAD(P)H-dependent xylose reductase, xylose reductase) is an enzyme with systematic name xylitol:NAD(P)+ oxidoreductase. This enzyme catalyses the following chemical reaction : xylitol + NAD(P)+ \rightleftharpoons D-xylose + NAD(P)H + H+ Xylose reductase catalyses the initial reaction in the xylose utilization pathway, the NAD(P)H dependent reduction of xylose to xylitol.
Sepiapterin reductase (L-threo-7,8-dihydrobiopterin forming) () is an enzyme with systematic name L-threo-7,8-dihydrobiopterin:NADP+ oxidoreductase. This enzyme catalyses the following chemical reaction : (1) L-threo-7,8-dihydrobiopterin + NADP+ \rightleftharpoons sepiapterin + NADPH + H+ : (2) L-threo-tetrahydrobiopterin + 2 NADP+ \rightleftharpoons 6-pyruvoyl-5,6,7,8-tetrahydropterin + 2 NADPH + 2 H+ This bacterial (Chlorobium tepidum) enzyme catalyses the final step in the de novo synthesis of tetrahydrobiopterin from GTP.
All-trans-decaprenyl-diphosphate synthase (, decaprenyl-diphosphate synthase, decaprenyl pyrophosphate synthetase, polyprenylpyrophosphate synthetase, terpenoidallyltransferase, terpenyl pyrophosphate synthetase, trans- prenyltransferase) is an enzyme with systematic name (2E,6E)-farnesyl- diphosphate:isopentenyl-diphosphate farnesyltranstransferase (adding 7 isopentenyl units). This enzyme catalyses the following chemical reaction : (2E,6E)-farnesyl diphosphate + 7 isopentenyl diphosphate \rightleftharpoons 7 diphosphate + all-trans-decaprenyl diphosphate This enzyme catalyses the condensation reactions resulting in the formation of all-trans-decaprenyl diphosphate.
Methylrhenium trioxide serves as a heterogeneous catalyst for a variety of transformations. Supported on Al2O3/SiO2, it catalyzes olefin metathesis at 25 °C. In solution, MTO catalyses for the oxidations with hydrogen peroxide. Terminal alkynes yield the corresponding acid or ester, internal alkynes yield diketones, and alkenes give epoxides. MTO also catalyses the conversion of aldehydes and diazoalkanes into an alkene,Hudson, A. “Methyltrioxorhenium” Encyclopedia of Reagents for Organic Synthesis.
4-dimethylallyltryptophan N-methyltransferase (, fgaMT (gene), easF (gene)) is an enzyme with systematic name S-adenosyl-L- methionine:4-(3-methylbut-2-enyl)-L-tryptophan N-methyltransferase. This enzyme catalyses the following chemical reaction : S-adenosyl-L-methionine + 4-dimethylallyl-L-tryptophan \rightleftharpoons S-adenosyl-L-homocysteine + 4-dimethylallyl-L-abrine The enzyme catalyses a step in the pathway leading to biosynthesis of ergot alkaloids in certain fungi.
It catalyses AMPylation of Rho GTPases in eukaryotic cells and therefore induces the collapse of the actin cytoskeleton. Doc (death on curing) protein is also part of a toxin-antitoxin module Phd-Doc from prophage P1. Doc toxin uses inverted substrate and catalyses phosphorylation instead of transferring NMP moiety. Doc phosphorylates elongation factor EF-Tu and locks it in an unfavorable open conformation to bind tRNAs and therefore blocks protein translation.
Homocitrate is enzymatically dehydrated by homoaconitase (HAc) (E.C 4.2.1.36) to yield cis-homoaconitate. HAc then catalyses a second reaction in which cis- homoaconitate undergoes rehydration to produce homoisocitrate.
GluDH isozymes are generally involved with either ammonia assimilation or glutamate catabolism. Two separate enzymes are present in yeasts: the NADP- dependent enzyme, which catalyses the amination of alpha-ketoglutarate to L-glutamate; and the NAD-dependent enzyme, which catalyses the reverse reaction \- this form links the L-amino acids with the Krebs cycle, which provides a major pathway for metabolic interconversion of alpha-amino acids and alpha-keto acids. Leucine dehydrogenase (LeuDH) is a NAD-dependent enzyme that catalyses the reversible deamination of leucine and several other aliphatic amino acids to their keto analogues. Each subunit of this octameric enzyme from Bacillus sphaericus contains 364 amino acids and folds into two domains, separated by a deep cleft.
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.
Fluoroacetyl-CoA thioesterase () is an enzyme with systematic name fluoroacetyl-CoA hydrolase. This enzyme catalyses the following chemical reaction : fluoroacetyl-CoA + H2O \rightleftharpoons fluoroacetate + CoA Fluoroacetate is extremely toxic.
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.
In humans and in animals that cannot synthesize vitamin C, the enzyme -gulonolactone oxidase (GULO), that catalyses the last step in the biosynthesis, is highly mutated and non-functional.
This enzyme catalyses the following chemical reaction: : Hydrolysis of proteins and small molecule substrates at -Asn-Xaa- bonds Both plant and animal legumains are most active in acidic environments.
27S pre-rRNA (guanosine2922-2'-O)-methyltransferase (, Spb1p (gene), YCL054W (gene)) is an enzyme with systematic name S-adenosyl-L-methionine:27S pre-rRNA (guanosine2922-2'-O-)-methyltransferase. This enzyme catalyses the following chemical reaction : S-adenosyl-L-methionine + guanosine2922 in 27S pre-rRNA \rightleftharpoons S-adenosyl-L-homocysteine + 2'-O-methylguanosine2922 in 27S pre-rRNA Spb1p is a site-specific 2'-O-ribose RNA methyltransferase that catalyses the formation of 2'-O-methylguanosine2922.
TRNA (cytidine32/guanosine34-2'-O)-methyltransferase (, Trm7p) is an enzyme with systematic name S-adenosyl-L-methionine:tRNA (cytidine32/guanosine34-2'-O)-methyltransferase. This enzyme catalyses the following chemical reaction : S-adenosyl-L-methionine + cytidine32/guanosine34 in tRNA \rightleftharpoons S-adenosyl-L-homocysteine + 2'-O-methylcytidine32/2'-O-methylguanosine34 in tRNA The enzyme from Saccharomyces cerevisiae catalyses the formation of 2'-O-methylnucleotides at positions 32 and 34 of the yeast tRNAPhe and tRNATrp.
The glycosyl hydrolase 68 family (CAZY GH_68) includes several bacterial levansucrase enzymes, and invertase from Zymomonas. Levansucrase (), also known as beta-D-fructofuranosyl transferase, catalyses the conversion of sucrose and (2,6-beta-D-fructosyl)(N) to glucose and (2,6-beta-D- fructosyl)(N+1), where other sugars can also act as fructosyl acceptors. Invertase, or extracellular sucrase (), catalyses the hydrolysis of terminal non-reducing beta-D-fructofuranoside residues in beta-D-fructofuranosides.
Long-chain acyl-(acyl-carrier-protein) reductase (, long-chain acyl-[acp] reductase, fatty acyl-[acyl-carrier-protein] reductase, acyl-[acp] reductase) is an enzyme with systematic name long-chain-aldehyde:NAD(P)+ oxidoreductase (acyl-(acyl-carrier protein)-forming). This enzyme catalyses the following chemical reaction : a long-chain aldehyde + acyl-carrier protein + NAD(P)+ \rightleftharpoons a long-chain acyl-[acyl-carrier protein] + NAD(P)H + H+ This enzyme catalyses the reaction in the opposite direction.
Aspartate---tRNAAsn ligase (, nondiscriminating aspartyl-tRNA synthetase) is an enzyme with systematic name L-aspartate:tRNAAsx ligase (AMP-forming). This enzyme catalyses the following chemical reaction : ATP + L-aspartate + tRNAAsx \rightleftharpoons AMP + diphosphate + aspartyl-tRNAAsx The 3 substrates of this enzyme are ATP, L-asparagine, and tRNAAsx, whereas its 3 products are AMP, diphosphate, and asparaginyl-tRNAAsx. When this enzyme acts on tRNAAsp, it catalyses the same reaction as EC 6.1.1.12, aspartate---tRNA ligase.
Physiologia Plantarum 100, 806-816 For this reason, the xanthophyll cycle is sometimes called the violaxanthin cycle. Violaxanthin de- epoxidase is an enzyme that reduces one epoxide group from violaxanthin into a double bond to create antheraxanthin. It also functions to create zeaxanthin, where it catalyses the reduction of two epoxide groups from violaxanthin. Zeaxanthin epoxidase catalyses the attachment of one epoxide group to zeaxanthin to generate antheraxanthin, and two epoxide groups to generate violaxanthin.
D-inositol-3-phosphate glycosyltransferase (, mycothiol glycosyltransferases, MshA) is an enzyme with systematic name UDP-N-acetyl-D-glucosamine:1D-myo- inositol 3-phosphate alpha-D-glycosyltransferase. This enzyme catalyses the following chemical reaction : UDP-N-acetyl-D-glucosamine + 1D-myo-inositol 3-phosphate \rightleftharpoons 1-O-(2-acetamido-2-deoxy-alpha-D- glucopyranosyl)-1D-myo-inositol 3-phosphate + UDP This enzyme catalyses the first dedicated reaction in the biosynthesis of mycothiol.
Thiazole tautomerase (, tenI (gene)) is an enzyme with systematic name 2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate isomerase. This enzyme catalyses the following chemical reaction : 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate \rightleftharpoons 2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate The enzyme catalyses the irreversible aromatization of the thiazole moiety of 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate.
All-trans-octaprenyl-diphosphate synthase (, octaprenyl-diphosphate synthase, octaprenyl pyrophosphate synthetase, polyprenylpyrophosphate synthetase, terpenoidallyltransferase, terpenyl pyrophosphate synthetase, trans- heptaprenyltranstransferase, trans-prenyltransferase) is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate:isopentenyl-diphosphate farnesyltranstransferase (adding 5 isopentenyl units). This enzyme catalyses the following chemical reaction : (2E,6E)-farnesyl diphosphate + 5 isopentenyl diphosphate \rightleftharpoons 5 diphosphate + all-trans-octaprenyl diphosphate This enzyme catalyses the condensation reactions resulting in the formation of all-trans-octaprenyl diphosphate.
2-polyprenyl-6-hydroxyphenol methylase (, ubiG (gene), ubiG methyltransferase, 2-octaprenyl-6-hydroxyphenol methylase) is an enzyme with systematic name S-adenosyl-L-methionine:3-(all-trans-polyprenyl)benzene-1,2-diol 2-O-methyltransferase. This enzyme catalyses the following chemical reaction : S-adenosyl-L-methionine + 3-(all-trans-polyprenyl)benzene-1,2-diol \rightleftharpoons S-adenosyl-L-homocysteine + 2-methoxy-6-(all-trans- polyprenyl)phenol UbiG catalyses both methylation steps in ubiquinone biosynthesis in Escherichia coli.
TRNA (carboxymethyluridine34-5-O)-methyltransferase (, ALKBH8, ABH8, Trm9, tRNA methyltransferase 9) is an enzyme with systematic name S-adenosyl-L- methionine:tRNA (carboxymethyluridine34-5-O)-methyltransferase. This enzyme catalyses the following chemical reaction : S-adenosyl-L-methionine + carboxymethyluridine34 in tRNA \rightleftharpoons S-adenosyl-L-homocysteine + 5-(2-methoxy-2-oxoethyl)uridine34 in tRNA The enzyme catalyses the posttranslational modification of uridine residues at the wobble position 34 of the anticodon loop of tRNA.
TRNA (adenine57-N1/adenine58-N1)-methyltransferase (, TrmI, PabTrmI, AqTrmI, MtTrmI) is an enzyme with systematic name S-adenosyl-L-methionine:tRNA (adenine57/adenine58-N1)-methyltransferase. This enzyme catalyses the following chemical reaction: :2 S-adenosyl-L-methionine + adenine57/adenine58 in tRNA \rightleftharpoons 2 S-adenosyl-L-homocysteine + N1-methyladenine57/N1-methyladenine58 in tRNA The enzyme catalyses the formation of N1-methyladenine at two adjacent positions (57 and 58) in the T-loop of certain tRNAs .
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.
This entry also includes folylpolyglutamate synthase that transfers glutamate to folylpolyglutamate and cyanophycin synthetase that catalyses the biosynthesis of the cyanobacterial reserve material multi-L-arginyl-poly-L-aspartate (cyanophycin).
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).
Myosin ATPase () is an enzyme with systematic name ATP phosphohydrolase (actin-translocating). This enzyme catalyses the following chemical reaction : ATP + H2O \rightleftharpoons ADP + phosphate ATP hydrolysis provides energy for actomyosin contraction.
This enzyme catalyses the following chemical reaction : 3β-hydroxyandrost-5-en-17-one 3-sulfate + H2O \rightleftharpoons 3β-hydroxyandrost-5-en-17-one + sulfate Also acts on some related steryl sulfates.
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.
Thermitase (, thermophilic Streptomyces serine proteinase, Thermoactinomyces vulgaris serine proteinase) is an enzyme. This enzyme catalyses the following chemical reaction : Hydrolysis of proteins, including collagen This peptidase is isolated from Thermoactinomyces vulgaris.
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.
Cobalt-precorrin-5B (C1)-methyltransferase (), cobalt-precorrin-6A synthase, CbiD (gene)) is an enzyme with systematic name S-adenosyl-L-methionine:cobalt- precorrin-5B (C1)-methyltransferase. This enzyme catalyses the following chemical reaction : cobalt-precorrin-5B + S-adenosyl-L-methionine \rightleftharpoons cobalt-precorrin-6A + S-adenosyl-L-homocysteine This enzyme catalyses the C-1 methylation of cobalt-precorrin-5B in the anaerobic pathway of adenosylcobalamin biosynthesis in bacteria such as Salmonella typhimurium, Bacillus megaterium, and Propionibacterium freudenreichii subsp. shermanii.
6-hydroxy-3-succinoylpyridine 3-monooxygenase (, 6-hydroxy-3-succinoylpyridine hydroxylase, hspA (gene), hspB (gene)) is an enzyme with systematic name 4-(6-hydroxypyridin-3-yl)-4-oxobutanoate,NADH:oxygen oxidoreductase (3-hydroxylating, succinate semialdehyde releasing). This enzyme catalyses the following chemical reaction : 4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ \+ O2 \rightleftharpoons 2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ \+ H2O 6-hydroxy-3-succinoylpyridine 3-monooxygenase catalyses a reaction in the nicotine degradation pathway of Pseudomonas species.
Malate dehydrogenase (NAD(P)+) (, MdH II, NAD(P)+-dependent malate dehyrogenase) is an enzyme with systematic name (S)-malate:NAD(P)+ oxidoreductase. This enzyme catalyses the following chemical reaction : (S)-malate + NAD(P)+ \rightleftharpoons oxaloacetate + NAD(P)H + H+ This enzyme, which was characterized from the methanogenic archaeon Methanobacterium thermoautotrophicum, catalyses only the reduction of oxaloacetate, and can use NAD+ and NADP+ with similar specific activity. It is different from EC 1.1.1.37 (malate dehydrogenase (NAD+)), EC 1.1.
Dissimilatory sulfite reductase () is an enzyme that participates in sulfur metabolism in dissimilatory sulfate reduction. The enzyme is essential in prokaryotic sulfur-based energy metabolism, including sulfate/sulfite reducing organisms, sulfur-oxidizing bacteria, and organosulfonate reducers. In sulfur reducers it catalyses the reduction of sulfite to sulfide (reaction 1), while in sulfur oxidizers it catalyses the opposite reaction (reaction 2). The reaction involves the small protein DsrC, which is present in all the organisms that contain dissimilatory sulfite reductase.
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.
Geranial dehydrogenase (, GaDH, geoB (gene)) is an enzyme with systematic name geranial:NAD+ oxidoreductase. This enzyme catalyses the following chemical reaction : geranial + H2O + NAD+ \rightleftharpoons geranate + NADH + H+ Does not act on neral.
The HIS3 gene, found in the Saccharomyces cerevisiae yeast, encodes a protein called Imidazoleglycerol-phosphate dehydratase which catalyses the sixth step in histidine biosynthesis. It is analogous to hisB in Escherichia coli.
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.
Phenylalanine hydroxylase (PAH) catalyses the conversion of L-phenylalanine (PHE) to L-tyrosine (TYR). Therefore, a deficiency in tetrahydrobiopterin can cause severe neurological issues related to a toxic buildup of L-phenylalanine.
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.
It is a homodimeric protein. In fungi, dehydroquinase forms the core of the pentafunctional AROM complex, which catalyses five consecutive steps in the shikimate pathway. A histidine is involved in the catalytic mechanism.
This protein domain is found in eukaryotes, bacteria and archaea. It is vital for living organisms since it catalyses a step in the purine biosynthesis pathway which aids energy metabolism and DNA synthesis.
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.
Chaperonin ATPase (, chaperonin) is an enzyme with systematic name ATP phosphohydrolase (polypeptide-unfolding). This enzyme catalyses the following chemical reaction : ATP + H2O \rightleftharpoons ADP + phosphate These enzymes are a subclass of molecular chaperones.
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.
Aspartyl aminopeptidase () is an enzyme. This enzyme catalyses the following chemical reaction : Release of an N-terminal aspartate or glutamate from a peptide, with a preference for aspartate Aminoacyl-arylamides are poor substrates.
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).
23S rRNA (uridine2552-2'-O)-methyltransferase (, Um(2552) 23S ribosomal RNA methyltransferase, heat shock protein RrmJ, RrmJ, FTSJ, Um2552 methyltransferase) is an enzyme with systematic name S-adenosyl-L- methionine:23S rRNA (uridine2552-2'-O-)-methyltransferase. This enzyme catalyses the following chemical reaction : S-adenosyl-L-methionine + uridine2552 in 23S rRNA \rightleftharpoons S-adenosyl-L-homocysteine + 2'-O-methyluridine2552 in 23S rRNA The enzyme catalyses the 2'-O-methylation of the universally conserved U2552 in the A loop of 23S rRNA.
UDP-2,3-diacylglucosamine diphosphatase (, UDP-2,3-diacylglucosamine hydrolase, UDP-2,3-diacylglucosamine pyrophosphatase, ybbF (gene), lpxH (gene)) is an enzyme with systematic name UDP-2,3-bis((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine 2,3-bis((3R)-3-hydroxymyristoyl)-beta-D-glucosaminyl 1-phosphate phosphohydrolase. This enzyme catalyses the following chemical reaction : UDP-2,3-bis[(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine + H2O \rightleftharpoons 2,3-bis[(3R)-3-hydroxymyristoyl]-beta-D-glucosaminyl 1-phosphate + UMP The enzyme catalyses a step in the biosynthesis of lipid A.
2-hydroxy-6-oxonona-2,4-dienedioate hydrolase (, mhpC (gene)) is an enzyme with systematic name (2Z,4E)-2-hydroxy-6-oxona-2,4-dienedioate succinylhydrolase. This enzyme catalyses the following chemical reaction: # (2Z,4E)-2-hydroxy-6-oxonona-2,4-diene-1,9-dioate + H2O \rightleftharpoons (2Z)-2-hydroxypenta-2,4-dienoate + succinate # (2Z,4E,7E)-2-hydroxy-6-oxonona-2,4,7-triene-1,9-dioate + H2O \rightleftharpoons (2Z)-2-hydroxypenta-2,4-dienoate + fumarate This enzyme catalyses a step in a pathway of phenylpropanoid compounds degradation.
Exo-(1->4)-alpha-D-glucan lyase (, alpha-(1->4)-glucan 1,5-anhydro-D-fructose eliminase, alpha-1,4-glucan exo-lyase, alpha-1,4-glucan lyase, GLase) is an enzyme with systematic name (1->4)-alpha-D-glucan exo-4-lyase (1,5-anhydro-D- fructose-forming). This enzyme catalyses the following chemical reaction : linear alpha-glucan \rightleftharpoons (n-1) 1,5-anhydro-D-fructose + D-glucose The enzyme catalyses the sequential degradation of (1->4)-alpha-D- glucans from the non-reducing end.
CDP-archaeol synthase (, CDP-2,3-di-O-geranylgeranyl-sn-glycerol synthase, CTP:2,3-GG-GP ether cytidylyltransferase, CTP:2,3-di-O-geranylgeranyl-sn- glycero-1-phosphate cytidyltransferase) is an enzyme with systematic name CTP:2,3-bis-O-(geranylgeranyl)-sn-glycero-1-phosphate cytidylyltransferase. This enzyme catalyses the following chemical reaction : CTP + 2,3-bis-O-(geranylgeranyl)-sn-glycero-1-phosphate \rightleftharpoons diphosphate + CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol This enzyme catalyses one of the steps in the biosynthesis of polar lipids in Archaea.
Monoterpene epsilon-lactone hydrolase (, MLH) is an enzyme with systematic name isoprop(en)ylmethyloxepan-2-one lactonohydrolase. This enzyme catalyses the following chemical reaction : (1) isoprop(en)ylmethyloxepan-2-one + H2O \rightleftharpoons 6-hydroxyisoprop(en)ylmethylhexanoate (general reaction) : (2) 4-isopropenyl-7-methyloxepan-2-one + H2O \rightleftharpoons 6-hydroxy-3-isopropenylheptanoate : (3) 7-isopropyl-4-methyloxepan-2-one + H2O \rightleftharpoons 6-hydroxy-3,7-dimethyloctanoate The enzyme catalyses the ring opening of epsilon-lactones in Gram-positive bacterium Rhodococcus erythropolis DCL14.
The nicotinamide ring of the NAD+ cofactor binds deep in this cleft, which is thought to close during the hydride transfer step of the catalytic cycle. Phenylalanine dehydrogenase (PheDH) is an NAD-dependent enzyme that catalyses the reversible deamidation of L-phenylalanine into phenyl-pyruvate. Valine dehydrogenase (ValDH) is an NADP- dependent enzyme that catalyses the reversible deamidation of L-valine into 3-methyl-2-oxobutanoate. These enzymes contain two domains, an N-terminal dimerisation domain, and a C-terminal domain.
In molecular biology, group II pyridoxal-dependent decarboxylases are family of enzymes including aromatic-L-amino-acid decarboxylase (L-dopa decarboxylase or tryptophan decarboxylase) , which catalyses the decarboxylation of tryptophan to tryptamine, tyrosine decarboxylase , which converts tyrosine into tyramine and histidine decarboxylase , which catalyses the decarboxylation of histidine to histamine. Pyridoxal-5'-phosphate-dependent amino acid decarboxylases can be divided into four groups based on amino acid sequence. Group II includes glutamate, histidine, tyrosine, and aromatic-L- amino-acid decarboxylases.
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.
Maleamate amidohydrolase (, NicF) is an enzyme with systematic name maleamate amidohydrolase. This enzyme catalyses the following chemical reaction : maleamate + H2O \rightleftharpoons maleate + NH3 The reaction is involved in the aerobic catabolism of nicotinic acid.
8-oxoguanine deaminase (, 8-OGD) is an enzyme with systematic name 8-oxoguanine aminohydrolase. This enzyme catalyses the following chemical reaction : 8-oxoguanine + H2O \rightleftharpoons urate + NH3 Zn2+ is bound in the active site.
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.
This enzyme catalyses the first step in ubiquinone biosynthesis, the removal of pyruvate from chorismate, to yield 4-hydroxybenzoate in Escherichia coli and other Gram-negative bacteria. Its activity does not require metal cofactors.
Gallate dioxygenase (, GalA) is an enzyme with systematic name gallate:oxygen oxidoreductase. This enzyme catalyses the following chemical reaction : gallate + O2 \rightleftharpoons (1E)-4-oxobut-1-ene-1,2,4-tricarboxylate Gallate dioxygenase contains non-heme Fe2+.
Nitrilotriacetate monooxygenase () is an enzyme with systematic name nitrilotriacetate,FMNH2:oxygen oxidoreductase (glyoxylate-forming). This enzyme catalyses the following chemical reaction : nitrilotriacetate + FMNH2 \+ H+ \+ O2 \rightleftharpoons iminodiacetate + glyoxylate + FMN + H2O Nitrilotriacetate monooxygenase requires Mg2+.
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.
Methane monooxygenase (particulate) () is an enzyme with systematic name methane,quinol:oxygen oxidoreductase. This enzyme catalyses the following chemical reaction : methane + quinol + O2 \rightleftharpoons methanol + quinone + H2O Methane monooxygenase contains copper. It is membrane-bound.
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.
Glutathione synthetase (GSS) (EC 6.3.2.3) is the second enzyme in the glutathione (GSH) biosynthesis pathway. It catalyses the condensation of gamma-glutamylcysteine and glycine, to form glutathione. Glutathione synthetase is also a potent antioxidant.
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).
Putidaredoxin—NAD+ reductase (, putidaredoxin reductase, camA (gene)) is an enzyme with systematic name putidaredoxin:NAD+ oxidoreductase. This enzyme catalyses the following chemical reaction : reduced putidaredoxin + NAD+ \rightleftharpoons oxidized putidaredoxin + NADH + H+ Putidaredoxin—NAD+ reductase requires FAD.
Cannabidiolic acid synthase (, CBDA synthase) is an enzyme with systematic name cannabigerolate:oxygen oxidoreductase (cyclizing, cannabidiolate- forming). It is an oxidoreductase found in Cannabis sativa that catalyses the formation of cannabidiolate, a carboxylated precursor of cannabidiol.
Taxoid 7beta-hydroxylase () is an enzyme with systematic name taxusin,NADPH:oxygen 7-oxidoreductase. This enzyme catalyses the following chemical reaction : taxusin + O2 \+ NADPH + H+ \rightleftharpoons 7beta- hydroxytaxusin + NADP+ \+ H2O Taxoid 7beta-hydroxylase requires cytochrome P450.
Sporulenol synthase (, sqhC (gene)) is an enzyme with systematic name tetraprenyl-beta-curcumene—sporulenol cyclase. This enzyme catalyses the following chemical reaction : sporulenol \rightleftharpoons tetraprenyl-beta- curcumene + H2O The reaction occurs in the reverse direction.
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.
Cobalt-precorrin-7 (C15)-methyltransferase (decarboxylating) (, CbiT) is an enzyme with systematic name S-adenosyl-L-methionine:precorrin-7 C15-methyltransferase (C12-decarboxylating). This enzyme catalyses the following chemical reaction : cobalt-precorrin-7 + S-adenosyl-L-methionine \rightleftharpoons cobalt-precorrin-8x + S-adenosyl-L-homocysteine + CO2 This enzyme catalyses both methylation at C-15 and decarboxylation of the C-12 acetate side chain of cobalt-precorrin-7 in the anaerobic pathway of adenosylcobalamin biosynthesis in bacteria such as Salmonella typhimurium, Bacillus megaterium, and Propionibacterium freudenreichii subsp. shermanii.
Crotonyl-CoA reductase (, butyryl-CoA dehydrogenase, butyryl dehydrogenase, unsaturated acyl-CoA reductase, ethylene reductase, enoyl-coenzyme A reductase, unsaturated acyl coenzyme A reductase, butyryl coenzyme A dehydrogenase, short-chain acyl CoA dehydrogenase, short-chain acyl-coenzyme A dehydrogenase, 3-hydroxyacyl CoA reductase, butanoyl-CoA:(acceptor) 2,3-oxidoreductase, CCR) is an enzyme with systematic name butanoyl-CoA:NADP+ 2,3-oxidoreductase. This enzyme catalyses the following chemical reaction : butanoyl-CoA + NADP+ \rightleftharpoons (E)-but-2-enoyl-CoA + NADPH + H+ This enzyme catalyses the reaction in the reverse direction.
L-galactonolactone dehydrogenase (, galactonolactone dehydrogenase, L-galactono-gamma-lactone dehydrogenase, L-galactono-gamma- lactone:ferricytochrome-c oxidoreductase, GLDHase, GLDase) is an enzyme with systematic name L-galactono-1,4-lactone:ferricytochrome-c oxidoreductase. This enzyme catalyses the following chemical reaction : (1) L-galactono-1,4-lactone + 2 ferricytochrome c \rightleftharpoons L-ascorbate + 2 ferrocytochrome c + 2 H+ : (2) L-ascorbate + 2 ferricytochrome c \rightleftharpoons L-dehydroascorbate + 2 ferrocytochrome c + 2 H+ (spontaneous) This enzyme catalyses the final step in the biosynthesis of L-ascorbic acid in plants and other photosynthetic eukaryotes.
2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5'-monophosphate deformylase (, ArfB) is an enzyme with systematic name 2-amino-5-formylamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one amidohydrolase. This enzyme catalyses the following chemical reaction : 2-Amino-5-formylamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one + H2O \rightleftharpoons 2,5-diamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one + formate The enzyme catalyses the second step in archaeal riboflavin and 7,8-didemethyl-8-hydroxy-5-deazariboflavin biosynthesis.
Riboflavin reductase (NAD(P)H) (, NAD(P)H-FMN reductase, Fre) is an enzyme with systematic name riboflavin:NAD(P)+ oxidoreductase. This enzyme catalyses the following chemical reaction : reduced riboflavin + NAD(P)+ \rightleftharpoons riboflavin + NAD(P)H + H+ This enzyme catalyses the reduction of soluble flavins. The structure of the protein suggests that the enzymatic mechanism of flavin reductase is of a bisubstrate-biproduct nature3. Due to its structural features, the enzyme is not able to bind both NAD(P)H and flavin at the same time.
2-oxoglutarate/L-arginine monooxygenase/decarboxylase (succinate-forming) (, ethylene-forming enzyme, EFE) is an enzyme with systematic name L-arginine,2-oxoglutarate:oxygen oxidoreductase (succinate-forming). This enzyme catalyses the following chemical reaction : 2-oxoglutarate + L-arginine + O2 \rightleftharpoons succinate + CO2 \+ guanidine + (S)-1-pyrroline-5-carboxylate + H2O (overall reaction) :(1a) 2-oxoglutarate + L-arginine + O2 \rightleftharpoons succinate + CO2 \+ L-hydroxyarginine :(1b) L-hydroxyarginine \rightleftharpoons guanidine + (S)-1-pyrroline-5-carboxylate + H2O 2-oxoglutarate/L-arginine monooxygenase/decarboxylase catalyses two cycles of the ethylene-forming reaction.
Acrylyl-CoA reductase (NADH) () is an enzyme with systematic name propanoyl- CoA:NAD+ oxidoreductase. This enzyme catalyses the following chemical reaction : propanoyl-CoA + NAD+ \rightleftharpoons acryloyl-CoA + NADH + H+ The reaction is catalysed in the opposite direction.
Nitrite dismutase (, Prolixin S, Nitrophorin 7) is an enzyme with systematic name nitrite:nitrite oxidoreductase. This enzyme catalyses the following chemical reaction : 3 nitrite + 2 H+ \rightleftharpoons 2 nitric oxide + nitrate + H2O Nitrite dismutase contains ferriheme b.
1.27) has occasionally been incorrectly termed an "undecaprenol kinase". However, that name should be reserved for a distinct enzyme (EC 2.7.1.66), which catalyses the addition of a phosphate group from ATP to undecaprenol (C55-isoprenyl alcohol).
Coccolysin (, Streptococcus thermophilus intracellular proteinase, EM 19000) is an enzyme. This enzyme catalyses the following chemical reaction : Preferential cleavage: -Leu, -Phe, -Tyr, -Ala This endopeptidase is present in S. thermophilus and S. diacetilactis and S. faecalis.
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.
Barrierpepsin (, barrier proteinase, Bar proteinase) is an enzyme. This enzyme catalyses the following chemical reaction : Selective cleavage of -Leu6-Lys- bond in the pheromone alpha-mating factor This endopeptidase is present in baker's yeast (Saccharomyces cerevisiae).
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+.
TRNA pseudouridine65 synthase (, TruC, YqcB) is an enzyme with systematic name tRNA-uridine65 uracil mutase. This enzyme catalyses the following chemical reaction : tRNA uridine65 \rightleftharpoons tRNA pseudouridine65 TruC specifically modifies uridines at positions 65 in tRNA.
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.
Desmosterol is a molecule similar to cholesterol. Desmosterol is the immediate precursor of cholesterol in the Bloch pathway of cholesterol biosynthesis. 24-dehydrocholesterol reductase catalyses the reduction of desmosterol to cholesterol. It is accumulated in desmosterolosis.
Autodisplay was invented with goals such as whole cell catalyses, especially with substrates which cannot cross the membranes of bacteria, the expression of peptides/proteins without an attached purification and the expression of immobilized peptides/proteins.
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+.
S-palmitoylation is generally done by proteins with the DHHC domain. Exceptions exist in non-enzymatic reactions. Acyl-protein thioesterase (APT) catalyses the reverse reaction.Lanyon-Hogg, T., Faronato, M., Serwa, R. A., & Tate, E. W. (2017).
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.
Involved in the reductive remethylation of cob(II)alamin using S-adenosylhomocysteine as a methyl donor. Catalyses the reaction: [methionine synthase]- cob(II)alamin + NADPH + H+ + S-adenosylmethionine → [methionine synthase]-methylcob(I)alamin + S-adenosylhomocysteine + NADP+.
Thermomycolin (, thermomycolase) is an enzyme. This enzyme catalyses the following chemical reaction : Rather nonspecific hydrolysis of proteins. Preferential cleavage: Ala-, Tyr-, Phe- in small molecule substrates This peptidase is isolated from the thermophilic fungus Malbranchea pulchella.
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.
J. Biol. Chem. 1970, 245, 4178–4186. Like Nε-trimethyllysine hydroxylase, γ-butyrobetaine hydroxylase is a 2-oxoglutarate and iron(II)-dependent oxygenase. γ-Butyrobetaine hydroxylase catalyses the stereospecific hydroxylation of γ-butyrobetaine to L-carnitine.
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.
Saccharolysin (, proteinase yscD, yeast cysteine proteinase D, Saccharomyces cerevisiae proteinase yscD) is an enzyme. This enzyme catalyses the following chemical reaction : Cleavage of Pro-Phe and Ala-Ala bonds This cytoplasmic metalloendopeptidase is present in Saccharomyces cerevisiae.
FMN reductase (NADPH) (, FRP, flavin reductase P, SsuE) is an enzyme with systematic name FMNH2:NADP+ oxidoreductase. This enzyme catalyses the following chemical reaction: : FMNH2 + NADP+ \rightleftharpoons FMN + NADPH + H+ The enzymes from bioluminescent bacteria contain FMN.
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.
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.
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.
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.
4-(gamma-L-glutamylamino)butanoyl-(BtrI acyl-carrier protein) monooxygenase (, btrO (gene)) is an enzyme with systematic name 4-(gamma-L- glutamylamino)butanoyl-(BtrI acyl-carrier protein),FMN:oxygen oxidoreductase (2-hydroxylating). This enzyme catalyses the following chemical reaction : 4-(gamma-L-glutamylamino)butanoyl-[BtrI acyl-carrier protein] + FMNH2 + O2 \rightleftharpoons 4-(gamma-L-glutamylamino)-(2S)-2-hydroxybutanoyl-[BtrI acyl-carrier protein] + FMN + H2O 4-(gamma-L-glutamylamino)butanoyl-(BtrI acyl-carrier protein) monooxygenase catalyses a step in the biosynthesis of the side chain of the aminoglycoside antibiotics of the butirosin family.
Methanogen homoaconitase (, methanogen HACN) is an enzyme with systematic name (R)-2-hydroxybutane-1,2,4-tricarboxylate hydro-lyase ((1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate-forming). This enzyme catalyses the following chemical reaction : (R)-2-hydroxybutane-1,2,4-tricarboxylate \rightleftharpoons (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate (overall reaction) : (1a) (R)-2-hydroxybutane-1,2,4-tricarboxylate \rightleftharpoons (Z)-but-1-ene-1,2,4-tricarboxylate + H2O : (1b) (Z)-but-1-ene-1,2,4-tricarboxylate + H2O \rightleftharpoons (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate This enzyme catalyses several reactions in the pathway of coenzyme-B biosynthesis in methanogenic archaea.
Trans-resveratrol di-O-methyltransferase (, ROMT, resveratrol O-methyltransferase, pterostilbene synthase) is an enzyme with systematic name S-adenosyl-L-methionine:trans-resveratrol 3,5-O-dimethyltransferase. This enzyme catalyses the following chemical reaction : 2 S-adenosyl-L-methionine + trans-resveratrol \rightleftharpoons 2 S-adenosyl-L-homocysteine + pterostilbene (overall reaction) : (1a) S-adenosyl-L-methionine + trans- resveratrol \rightleftharpoons S-adenosyl-L-homocysteine + 3-methoxy-4',5-dihydroxy-trans-stilbene : (1b) S-adenosyl-L-methionine + 3-methoxy-4',5-dihydroxy-trans-stilbene \rightleftharpoons S-adenosyl-L- homocysteine + pterostilbene The enzyme catalyses the biosynthesis of pterostilbene from resveratrol.
Phosphoenolpyruvate carboxykinase (diphosphate) (, phosphopyruvate carboxylase, phosphoenolpyruvate carboxylase, PEP carboxyphosphotransferase, PEP carboxykinase, phosphopyruvate carboxykinase (pyrophosphate), PEP carboxylase, phosphoenolpyruvic carboxykinase, phosphoenolpyruvic carboxylase, phosphoenolpyruvate carboxykinase, phosphoenolpyruvate carboxytransphosphorylase, phosphoenolpyruvate carboxykinase, phosphoenolpyruvic carboxykinase, PEPCTrP, phosphoenolpyruvic carboxykinase (pyrophosphate), phosphoenolpyruvic carboxylase (pyrophosphate), phosphoenolpyruvate carboxyphosphotransferase, phosphoenolpyruvic carboxytransphosphorylase, phosphoenolpyruvate carboxylase (pyrophosphate), phosphopyruvate carboxylase (pyrophosphate), diphosphate:oxaloacetate carboxy- lyase (transphosphorylating)) is an enzyme with systematic name diphosphate:oxaloacetate carboxy-lyase (transphosphorylating; phosphoenolpyruvate-forming). This enzyme catalyses the following chemical reaction : diphosphate + oxaloacetate \rightleftharpoons phosphate + phosphoenolpyruvate + CO2 This enzyme also catalyses the reaction: :phosphoenolpyruvate + GTP + CO2 \rightleftharpoons pyruvate + GDP. It is transcriptionally upregulated in the liver by glucagon.
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.
Glutathione amide reductase (, GAR) is an enzyme with systematic name glutathione amide:NAD+ oxidoreductase. This enzyme catalyses the following chemical reaction : 2 glutathione amide + NAD+ \rightleftharpoons glutathione amide disulfide + NADH + H+ Glutathione amide reductase is a dimeric flavoprotein (FAD).
5'-deoxyadenosine deaminase catalyses the salvage pathway of 5'-deoxyadenosine to 5'-deoxyinosine following the reaction pathway of C10H13N5O3 + H+ + H2O <=>> C10H12N4O4 + NH4+. In this reaction 5'-deoxyadenosine is converted to 5'-deoxyinosine with ammonia as a byproduct.
Soyasaponin III rhamnosyltransferase (, UGT91H4, GmSGT3 (gene)) is an enzyme with systematic name UDP-rhamnose:soyasaponin III rhamnosyltransferase. This enzyme catalyses the following chemical reaction : UDP-rhamnose + soyasaponin III \rightleftharpoons UDP + soyasaponin I Part of the biosynthetic pathway for soyasaponins.
Hepsin () is an enzyme. This enzyme catalyses the following chemical reaction : Cleavage after basic amino-acid residues, with Arg strongly preferred to Lys This type-II membrane-associated serine peptidase plays a role in cell growth and development.
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+.
Perakine reductase () is an enzyme with systematic name raucaffrinoline:NADP+ oxidoreductase. This enzyme catalyses the following chemical reaction : raucaffrinoline + NADP+ \rightleftharpoons perakine + NADPH + H+ The biosynthesis of raucaffrinoline from perakine is a side route of the ajmaline biosynthesis pathway.
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.
The dimerization reaction 2SF2 FSSF3 is reversible. It also disproportionates: SF2 \+ FSSF3 → FSSF + SF4. A side reaction also produces the intermediate F3SSSF3. hydrogen fluoride catalyses disproportionation to sulfur and sulfur tetrafluoride by forming a reactive intermediate HSF molecule.
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.
Hydrazine oxidoreductase (, HAO (ambiguous)) is an enzyme with systematic name hydrazine:acceptor oxidoreductase. This enzyme catalyses the following chemical reaction : hydrazine + acceptor \rightleftharpoons N2 \+ reduced acceptor Hydrazine oxidoreductase is involved in the pathway of anaerobic ammonium oxidation in anammox bacteria.
N-formylmaleamate deformylase (, NicD) is an enzyme with systematic name N-formylmaleamic acid amidohydrolase. This enzyme catalyses the following chemical reaction : N-formylmaleamic acid + H2O \rightleftharpoons maleamate + formate The reaction is involved in the aerobic catabolism of nicotinic 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.
2-hydroxyethylphosphonate dioxygenase (, HEPD, phpD (gene)) is an enzyme with systematic name 2-hydroxyethylphosphonate:O2 1,2-oxidoreductase (hydroxymethylphosphonate forming). This enzyme catalyses the following chemical reaction : 2-hydroxyethylphosphonate + O2 \rightleftharpoons hydroxymethylphosphonate + formate 2-hydroxyethylphosphonate dioxygenase contains non-heme-Fe(II).
Methylphosphonate synthase (, mpnS (gene)) is an enzyme with systematic name 2-hydroxyethylphosphonate:O2 1,2-oxidoreductase (methylphosphonate forming). This enzyme catalyses the following chemical reaction : 2-hydroxyethylphosphonate + O2 \rightleftharpoons methylphosphonate + HCO3− Methylphosphonate synthase is isolated from the marine archaeon Nitrosopumilus maritimus.
Geranylhydroquinone 3''-hydroxylase (, GHQ 3''-hydroxylase) is an enzyme with systematic name geranylhydroquinone,NADPH:oxygen oxidoreductase (3''-hydroxylating). This enzyme catalyses the following chemical reaction : geranylhydroquinone + NADPH + H+ \+ O2 \rightleftharpoons 3''-hydroxygeranylhydroquinone + NADP+ \+ H2O Geranylhydroquinone 3''-hydroxylase contains cytochrome P450.
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).
Lupeol synthase (, LUPI, BPW, RcLUS) is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualene mutase (cyclizing, lupeol-forming). This enzyme catalyses the following chemical reaction : (3S)-2,3-epoxy-2,3-dihydrosqualene \rightleftharpoons lupeol Also forms some beta-amyrin.
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.
Chitosanase () is an enzyme with systematic name chitosan N-acetylglucosaminohydrolase. This enzyme catalyses the following chemical reaction : Endohydrolysis of beta-(1->4)-linkages between D-glucosamine residues in a partly acetylated chitosan A whole spectrum of chitosanases are known.
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.
Iduronidase (, L-iduronidase, alpha-L-iduronidase, laronidase), sold as Aldurazyme, is an enzyme with the systematic name glycosaminoglycan alpha-L- iduronohydrolase. This enzyme catalyses the hydrolysis of unsulfated alpha-L- iduronosidic linkages in dermatan sulfate.Aldurazyme (Laronidase). BioMarin Pharmaceuticals Inc.
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.
Polyprenol reductase (, SRD5A3 (gene), DFG10 (gene)) is an enzyme with systematic name ditrans,polycis-dolichol:NADP+ 2,3-oxidoreductase. This enzyme catalyses the following chemical reaction : ditrans, polycis-dolichol + NADP+ \rightleftharpoons ditrans, polycis-polyprenol + NADPH + H+ The reaction occurs in the reverse direction.
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.
D-aspartate oxidase (DASOX) is an enzyme, structurally related to DAO, which catalyses the same reaction but is active only toward dicarboxylic D-amino acids. In DAO, a conserved histidine has been shown to be important for the enzyme's catalytic activity.
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.
Peptidyl-Lys metalloendopeptidase (, Armillaria mellea neutral proteinase, peptidyllysine metalloproteinase) is an enzyme. This enzyme catalyses the following chemical reaction : Preferential cleavage in proteins: -Xaa-Lys- (in which Xaa may be Pro) This encyme is isolated from the honey fungus Armillaria mellea.
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.
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.
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.
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.
In molecular biology, members of the ArgJ protein family are bifunctional protein that catalyses the first () and fifth steps () in arginine biosynthesis. The structure has been determined for glutamate N-acetyltransferase 2 (ornithine acetyltransferase), an ArgJ-like protein from Streptomyces clavuligerus.
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).
N-alkylglycine oxidase (, N-carboxymethylalkylamine:oxygen oxidoreductase (decarboxymethylating)) is an enzyme with systematic name N-alkylglycine:oxygen oxidoreductase (alkylamine forming). This enzyme catalyses the following chemical reaction : N-alkylglycine + H2O + O2 \rightleftharpoons alkylamine + glyoxalate + H2O2 Isolated from the mold Cladosporium sp. G-10.
Thebaine 6-O-demethylase (, T6ODM) is an enzyme with systematic name thebaine,2-oxoglutarate:oxygen oxidoreductase (6-O-demethylating). This enzyme catalyses the following chemical reaction : thebaine + 2-oxoglutarate + O2 \rightleftharpoons neopinone + formaldehyde + succinate + CO2 Thebaine 6-O-demethylase contains Fe2+.
Carotene epsilon-monooxygenase (, CYP97C1, LUT1) is an enzyme with systematic name alpha-carotene:oxygen oxidoreductase (3-hydroxylating). This enzyme catalyses the following chemical reaction : alpha-carotene + O2 \+ AH2 \rightleftharpoons alpha-cryptoxanthin + A + H2O Carotene epsilon- monooxygenase is a heme-thiolate protein (P450).
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.
Alpha-pinene monooxygenase () is an enzyme with systematic name (-)-alpha- pinene,NADH:oxygen oxidoreductase. This enzyme catalyses the following chemical reaction : (-)-alpha-pinene + NADH + H+ \+ O2 \rightleftharpoons alpha-pinene oxide + NAD+ \+ H2O Alpha-pinene monooxygenase takes part in catabolism of alpha-pinene.
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.
Tetrahymanol synthase (, squalenea€”tetrahymanol 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.
23S rRNA pseudouridine2605 synthase (, RluB, YciL) is an enzyme with systematic name 23S rRNA-uridine2605 uracil mutase. This enzyme catalyses the following chemical reaction : 23S rRNA uridine2605 \rightleftharpoons 23S rRNA pseudouridine2605 Pseudouridine synthase RluB converts uridine2605 of 23S rRNA to pseudouridine.
Hygromycin B 4-O-kinase (, hygromycin-B kinase) is an enzyme with systematic name ATP:hygromycin-B 4-O-phosphotransferase. This enzyme catalyses the following chemical reaction : ATP + hygromycin B \rightleftharpoons ADP + 4-O-phosphohygromycin B Phosphorylates the antibiotic hygromycin B.
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+.
DNA-3-methyladenine glycosylase II () is an enzyme that catalyses the following chemical reaction: : Hydrolysis of alkylated DNA, releasing 3-methyladenine, 3-methylguanine, 7-methylguanine, and 7-methyladenine Involved in the removal of alkylated bases from DNA in Escherichia coli.
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.
File:Hypothesized substraight binding location.png The structure of the Candida glabrata GDE has been reported. The structure revealed that distinct domains in GDE encode the glucanotransferase and glucosidase activities. Their catalyses are similar to that of alpha-amylase and glucoamylase, respectively.
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.
Oviductin (, oviductal protease) is an enzyme. It catalyses the following chemical reaction: : Preferential cleavage at Gly-Ser-Arg373- of glycoprotein gp43 in Xenopus laevis coelemic egg envelope to yield gp41 This enzyme is also found in the Japanese toad (Bufo japonicus).
Pancreatic elastase II (, pancreatic elastase 2) is an enzyme. This enzyme catalyses the following chemical reaction : Preferential cleavage: Leu-, Met- and Phe-. Hydrolyses elastin This peptidase from trypsin family is formed by activation of proelastase II from mammalian pancreas by trypsin.
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.
Tricin synthase (, ROMT-17, ROMT-15, HvOMT1, ZmOMT1) is an enzyme with systematic name S-adenosyl-L-methionine:tricetin 3',5'-O-dimethyltransferase. This enzyme catalyses the following chemical reaction : 2 S-adenosyl-L- methionine + tricetin \rightleftharpoons 2 S-adenosyl-L-homocysteine + 3',5'-O-dimethyltricetin (overall reaction) :(1a) S-adenosyl-L-methionine + tricetin \rightleftharpoons S-adenosyl-L-homocysteine + 3'-O-methyltricetin :(1b) S-adenosyl-L-methionine + 3'-O-methyltricetin \rightleftharpoons S-adenosyl-L-homocysteine + 3',5'-O-dimethyltricetin The enzymes from Oryza sativa (ROMT-15 and ROMT-17) catalyses the stepwise methylation of tricetin to its 3'-mono- and 3',5'-dimethyl ethers.
3-(cis-5,6-dihydroxycyclohexa-1,3-dien-1-yl)propanoate dehydrogenase (, hcaB (gene), cis-dihydrodiol dehydrogenase, 2,3-dihydroxy-2,3-dihydro- phenylpropionate dehydrogenase) is an enzyme with systematic name 3-(cis-5,6-dihydroxycyclohexa-1,3-dien-1-yl)propanoate:NAD+ oxidoreductase. This enzyme catalyses the following chemical reaction : (1) 3-(cis-5,6-dihydroxycyclohexa-1,3-dien-1-yl)propanoate + NAD+ \rightleftharpoons 3-(2,3-dihydroxyphenyl)propanoate + NADH + H+ : (2) (2E)-3-(cis-5,6-dihydroxycyclohexa-1,3-dien-1-yl)prop-2-enoate + NAD+ \rightleftharpoons (2E)-3-(2,3-dihydroxyphenyl)prop-2-enoate + NADH + H+ This enzyme catalyses a step in indegradation of phenylpropanoid compounds.
Aldos-2-ulose dehydratase (, pyranosone dehydratase, AUDH, 1,5-anhydro-D- fructose dehydratase (microthecin-forming)) is an enzyme with systematic name 1,5-anhydro-D-fructose hydro-lyase (microthecin-forming). This enzyme catalyses the following chemical reaction : 1,5-anhydro-D-fructose \rightleftharpoons 2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one + H2O (overall reaction) : (1a) 1,5-anhydro-D-fructose \rightleftharpoons 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose + H2O : (1b) 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose \rightleftharpoons 2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one This enzyme catalyses two of the steps in the anhydrofructose pathway.
C 1.5.1.10) catalyses a condensation reaction with glutamate and NAD(P)H, as a proton donor, and the imine is reduced to produce the penultimate product, saccharopine. The final step of the pathway in fungi involves the saccharopine dehydrogenase (SDH) (E.C 1.5.
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.
Atroxase () is an enzyme. This enzyme catalyses the following chemical reaction : Cleavage of His5-Leu, Ser9-His, His10-Leu, Ala14-Leu and Tyr16-Leu of insulin B chain This endopeptidase is present in the venom of the western diamondback rattlesnake (Crotalus atrox).
Sulfometuron methyl is an organic compound used as a herbicide. It is classed as a sulfonylurea. It functions via the inhibitition of acetolactate synthase enzyme, which catalyses the first step in biosynthesis of the branched-chain amino acids valine, leucine and isoleucine.
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.
Jararhagin (, HF2-proteinase, JF1) is an enzyme. This enzyme catalyses the following chemical reaction : Hydrolysis of -His10-Leu-, -Ala14-Leu-, -Tyr16-Leu-and -Phe24-Phe- bonds in insulin B chain This endopeptidase is present in the venom of the jararaca snake (Bothrops jararaca).
Terminal alkynes yield the corresponding acid or ester, internal alkynes yield diketones, and alkenes give epoxides. MTO also catalyses the conversion of aldehydes and diazoalkanes into an alkene.Hudson, A. "Methyltrioxorhenium" Encyclopedia of Reagents for Organic Synthesis. John Wiley & Sons: New York, 2002.
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.
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.
Non-chaperonin molecular chaperone ATPase (, molecular chaperone Hsc70 ATPase) is an enzyme with systematic name ATP phosphohydrolase (polypeptide- polymerizing). This enzyme catalyses the following chemical reaction : ATP + H2O \rightleftharpoons ADP + phosphate These enzymes perform many functions that are similar to those of chaperonins.
Codeine 3-O-demethylase (, codeine O-demethylase, CODM) is an enzyme with systematic name codeine,2-oxoglutarate:oxygen oxidoreductase (3-O-demethylating). This enzyme catalyses the following chemical reaction : codeine + 2-oxoglutarate + O2 \rightleftharpoons morphine + formaldehyde + succinate + CO2 Codeine 3-O-demethylase contains Fe2+.
Dinoflagellate luciferase (, Gonyaulax luciferase) is a specific luciferase, an enzyme with systematic name dinoflagellate-luciferin:oxygen 132-oxidoreductase. This enzyme catalyses the following chemical reaction : dinoflagellate luciferin + O2 \rightleftharpoons oxidized dinoflagellate luciferin + H2O + hnu Dinoflagellate luciferase is a single protein with three luciferase domains.
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.
Mycoredoxin (, Mrx1, MrxI) is an enzyme with systematic name arseno- mycothiol:mycoredoxin oxidoreductase. This enzyme catalyses the following chemical reaction : arseno-mycothiol + mycoredoxin \rightleftharpoons arsenite + mycothiol-mycoredoxin disulfide Reduction of arsenate is part of a defense mechanism of the cell against toxic arsenate.
Geranylgeraniol 18-hydroxylase (, GGOH-18-hydroxylase) is an enzyme with systematic name geranylgeraniol,NADPH:oxygen oxidoreductase (18-hydroxylating). This enzyme catalyses the following chemical reaction : geranylgeraniol + NADPH + H+ \+ O2 \rightleftharpoons 18-hydroxygeranylgeraniol + NADP+ \+ H2O Geranylgeraniol 18-hydroxylase is a heme-thiolate protein (P-450).
7-Methylxanthine demethylase () is an enzyme with systematic name 7-methylxanthine:oxygen oxidoreductase (demethylating). This enzyme catalyses the following chemical reaction : 7-methylxanthine + O2 + NAD(P)H + H+ \rightleftharpoons xanthine + NAD(P)+ + H2O + formaldehyde 7-Methylxanthine demethylase is a non-heme iron oxygenase.
Alpha-humulene 10-hydroxylase (, CYP71BA1) is an enzyme with systematic name alpha-humulene,NADPH:oxygen 10-oxidoreductase. This enzyme catalyses the following chemical reaction : alpha-humulene + O2 \+ NADPH + H+ \rightleftharpoons 10-hydroxy-alpha-humulene + NADP+ \+ H2O Alpha-humulene 10-hydroxylase requires cytochrome P-450.
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.
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.
Beta-cubebene synthase (, cop4, Mg25) is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate diphosphate-lyase (cyclizing, beta-cubebene- forming). This enzyme catalyses the following chemical reaction : (2E,6E)-farnesyl diphosphate \rightleftharpoons beta-cubebene + diphosphate Isolated from the fungus Coprinus cinereus.
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.
Camelliol C synthase (, CAMS1, LUP3 (gene)) is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualene mutase (cyclizing, camelliol-C-forming). This enzyme catalyses the following chemical reaction : (3S)-2,3-epoxy-2,3-dihydrosqualene \rightleftharpoons camelliol C The product is mainly camelliol.
UDP-arabinopyranose mutase (, Os03g40270 protein, UAM1, UAM3, RGP1, RGP3, OsUAM1, OsUAM2, Os07g41360 protein) is an enzyme with systematic name UDP- arabinopyranose pyranomutase. This enzyme catalyses the following chemical reaction : UDP-beta-L-arabinofuranose \rightleftharpoons UDP-beta-L- arabinopyranose The reaction is reversible.
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.
Benjamin Cummings, December 7, 2007. (also: 3-phosphoglyceric acid, PGA, 3PGA). # The enzyme phosphoglycerate kinase catalyses the phosphorylation of 3-PGA by ATP (which was produced in the light-dependent stage). 1,3-Bisphosphoglycerate (1,3BPGA, glycerate-1,3-bisphosphate) and ADP are the products.
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).
G-protein-coupled receptor kinase 7 (, GRK7, cone opsin kinase, iodopsin kinase) is a serine/threonine-specific protein kinase involved in phototransduction. This enzyme catalyses the phosphorylation of cone (color) photopsins in retinal cones during high acuity color vision primarily in the fovea.
Neomycin C transaminase (, neoN (gene)) is an enzyme with systematic name 2-oxoglutarate:neomycin C aminotransferase. This enzyme catalyses the following chemical reaction : neomycin C + 2-oxoglutarate \rightleftharpoons 6-deamino-6-oxoneomycin C + L-glutamate The reaction occurs in vivo in the opposite direction.
Fumigaclavine A dimethylallyltransferase (, FgaPT1) is an enzyme with systematic name dimethylallyl-diphosphate:fumigaclavine A dimethylallyltransferase. This enzyme catalyses the following chemical reaction : fumigaclavine A + dimethylallyl diphosphate \rightleftharpoons fumigaclavine C + diphosphate Fumigaclavine C is an ergot alkaloid produced by some fungi of the Trichocomaceae family.
Geranyl-pyrophosphate—olivetolic acid geranyltransferase (, GOT) is an enzyme with systematic name geranyl-diphosphate:olivetolate geranyltransferase. This enzyme catalyses the following chemical reaction : geranyl diphosphate + 2,4-dihydroxy-6-pentylbenzoate \rightleftharpoons diphosphate + cannabigerolate Part of the cannabinoids biosynthetic pathway of the plant Cannabis sativa.
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.
Firefly luciferase is the light-emitting enzyme responsible for the bioluminescence of fireflies and click beetles. The enzyme catalyses the oxidation of firefly luciferin, requiring oxygen and ATP. Because of the requirement of ATP, firefly luciferases have been used extensively in biotechnology.
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.
Chemical mutagenesis involves the use of chemical agents to introduce mutations into genetic sequences. Examples of chemical mutagens follow. Sodium bisulfate is effective at mutating G/C rich genomic sequences. This is because sodium bisulfate catalyses deamination of unmethylated cytosine to uracil.
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.
Troxipide inhibits H. pylori-derived urease, a multimeric nickel- containing enzyme that catalyses the hydrolysis of urea to yield ammonia and carbonic acid, which damage host tissues and trigger inflammatory response, including recruitment of leukocytes and triggering of the oxidative burst in neutrophils.
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.
4-hydroxycoumarin synthase (, BIS2, BIS3) is an enzyme with systematic name malonyl-CoA:2-hydroxybenzoyl-CoA malonyltransferase. This enzyme catalyses the following chemical reaction : malonyl-CoA + 2-hydroxybenzoyl-CoA \rightleftharpoons 2 CoA + 4-hydroxycoumarin + CO2 This polyketide synthase can also accept benzoyl-CoA as substrate.
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.
Mucrolysin (, Trimeresurus metalloendopeptidase A, mucrotoxin A) is an enzyme. This enzyme catalyses the following chemical reaction : Cleavage of Ser9-His, His10-Leu, Ala14-Leu, Leu15-Tyr and Tyr16-Leu bonds in insulin B chain This endopeptidase from the venom of Taiwan habu snake (Protobothrops mucrosquamatus).
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).
Fragilysin (, Bacteroides fragilis (entero)toxin) is an enzyme. This enzyme catalyses the following chemical reaction : Broad proteolytic specificity, bonds hydrolysed including -Gly-Leu-, -Met-Leu-, -Phe-Leu-, -Cys-Leu-, Leu-Gly It is thought to be a cause of diarrhoea in animals and humans.
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.
Mammals biosynthesize the amino acid cysteine via homocysteine. Cystathionine β-synthase catalyses the condensation of homocysteine and serine to give cystathionine. This reaction uses pyridoxine (vitamin B6) as a cofactor. Cystathionine γ-lyase then converts this double amino acid to cysteine, ammonia, and α-ketobutyrate.
Linoleate 10R-lipoxygenase (, 10R-DOX, (10R)-dioxygenase, 10R-dioxygenase) is an enzyme with systematic name linoleate:oxygen (10R)-oxidoreductase. This enzyme catalyses the following chemical reaction : linoleate + O2 \rightleftharpoons (8E,10R,12Z)-10-hydroperoxy-8,12-octadecadienoate Linoleate 10R-lipoxygenase is involved in biosynthesis of oxylipins.
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.
Torulene dioxygenase (, CAO-2, CarT) is an enzyme with systematic name torulene:oxygen oxidoreductase. This enzyme catalyses the following chemical reaction : torulene + O2 \rightleftharpoons 4'-apo-beta, psi-caroten-4'-al + 3-methylbut-2-enal It is assumed that 3-methylbut-2-enal is formed.
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.
Preflagellin peptidase (, FlaK) is an enzyme that catalyses the following chemical reaction: : Cleaves the signal peptide of 3 to 12 amino acids from the N-terminal of preflagellin, usually at Arg-Gly- or Lys-Gly-, to release flagellin. This aspartic peptidase is present in Archaea.
Bothropasin (, Bothrops jararaca venom metalloproteinase) is an enzyme. This enzyme catalyses the following chemical reaction : Cleavage of His5-Leu, His10-Leu, Ala14-Leu, Tyr16-Leu and Phe24-Phe in insulin B chain This endopeptidase is present in the venom of jararaca snake (Bothrops jararaca).
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).
Methanesulfonate monooxygenase (, mesylate monooxygenase, mesylate,reduced- FMN:oxygen oxidoreductase, MsmABCD, methanesulfonic acid monooxygenase, MSA monooxygenase, MSAMO) is an enzyme with systematic name methanesulfonate,NADH:oxygen oxidoreductase. This enzyme catalyses the following chemical reaction : methanesulfonate + NADH + H+ \+ O2 \rightleftharpoons formaldehyde + NAD+ \+ sulfite + H2O Methanesulfonate monooxygenase is a flavoprotein.
Quinolinate synthase (, NadA, QS, quinolinate synthetase) is an enzyme with systematic name glycerone phosphate:iminosuccinate alkyltransferase (cyclizing). This enzyme catalyses the following chemical reaction : glycerone phosphate + iminosuccinate \rightleftharpoons pyridine-2,3-dicarboxylate + 2 H2O + phosphate This iron-sulfur protein that requires a [4Fe-4S] cluster for activity.
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.
Phyllocladan-16alpha-ol synthase (, PaDC1) is an enzyme with systematic name (+)-copalyl-diphosphate diphosphate-lyase (phyllocladan-16alpha-ol-forming). This enzyme catalyses the following chemical reaction : (+)-copalyl diphosphate + H2O \rightleftharpoons phyllocladan-16alpha-ol + diphosphate The adjacent gene PaDC2 codes EC 5.5.1.12, copalyl diphosphate synthase.
Glycogen synthase (UDP-glucose-glycogen glucosyltransferase) is a key enzyme in glycogenesis, the conversion of glucose into glycogen. It is a glycosyltransferase () that catalyses the reaction of UDP-glucose and (1,4-α-D-glucosyl)n to yield UDP and (1,4-α-D-glucosyl)n+1.
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.
Tryptophan synthase or tryptophan synthetase is an enzyme that catalyses the final two steps in the biosynthesis of tryptophan. It is commonly found in Eubacteria, Archaebacteria, Protista, Fungi, and Plantae. However, it is absent from Animalia. It is typically found as an α2β2 tetramer.
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.
Rhamnogalacturonan acetylesterase (, RGAE) is an enzyme with systematic name rhamnogalacturonan 2/3-O-acetyl-alpha-D-galacturonate O-acetylhydrolase. This enzyme catalyses the following chemical reaction : Hydrolytic cleavage of 2-O-acetyl- or 3-O-acetyl groups of alpha-D-galacturonic acid in rhamnogalacturonan I.
Arsenate-mycothiol transferase (, ArsC1, ArsC2, mycothiol:arsenate transferase) is an enzyme with systematic name mycothiol:arsenate S-arsenotransferase. This enzyme catalyses the following chemical reaction center mycothiol + arsenate \rightleftharpoons arseno-mycothiol + H2O Reduction of arsenate is part of a defence mechanism of the cell against toxic arsenate.
Poly(ADP-ribose) glycohydrolase () is an enzyme. This enzyme catalyses the following chemical reaction : hydrolyses poly(ADP-ribose) at glycosidic (1-2') linkage of ribose-ribose bond to produce free ADP-ribose Specific to (1-2') linkage of ribose-ribose bond of poly(ADP-ribose).
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.
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+.
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.
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.
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.
Gunzberg's test is a chemical test used for detecting the presence of hydrochloric acid. Gunzberg's reagent is made by dissolving two grams of phloroglucinol and one gram of vanillin in 100 millilitres of 95% ethanol. Hydrochloric acid catalyses Gunzberg's reagent to form a red complex.
Testosterone 17beta-dehydrogenase (NADP+) (, 17-ketoreductase, NADP-dependent testosterone-17beta-oxidoreductase, testosterone 17beta-dehydrogenase (NADP)) is an enzyme with systematic name 17beta-hydroxysteroid:NADP+ 17-oxidoreductase. This enzyme catalyses the following chemical reaction : testosterone + NADP+ \rightleftharpoons androstenedione + NADPH + H+ Also oxidizes 3-hydroxyhexobarbital to 3-oxohexobarbital.
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.
UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase (, UDP-3-O-acyl- glucosamine N-acyltransferase, UDP-3-O-(R-3-hydroxymyristoyl)-glucosamine N-acyltransferase, acyltransferase LpxD, acyl-ACP:UDP-3-O-(3-hydroxyacyl)-GlcN N-acyltransferase, firA (gene), lpxD (gene)) is an enzyme with systematic name (3R)-3-hydroxymyristoyl-(acyl-carrier protein):UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine N-acetyltransferase. This enzyme catalyses the following chemical reaction : (3R)-3-hydroxymyristoyl-[acyl-carrier protein] + UDP-3-O-[(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine \rightleftharpoons UDP-2,3-bis[O-(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine + holo-[acyl- carrier protein] The enzyme catalyses a step of lipid A biosynthesis.
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 molecular biology, 3,4-dihydroxy-2-butanone 4-phosphate synthase (DHBP synthase) (RibB) is an enzyme which catalyses the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate, the latter serving as the biosynthetic precursor for the xylene ring of riboflavin. In Photobacterium leiognathi, the riboflavin synthesis genes ribB (DHBP synthase), ribE (riboflavin synthase), ribH (lumazine synthase) and ribA (GTP cyclohydrolase II) all reside in the lux operon. RibB is sometimes found as a bifunctional enzyme with GTP cyclohydrolase II that catalyses the first committed step in the biosynthesis of riboflavin. No sequences with significant homology to DHBP synthase are found in the metazoa.
Structurally speaking, YopE has 4 alpha helices arranged in a left handed Four-helical up- and-down bundle. This bundle acts as the GAP domain, because arginine from an alpha helix is inserted into a GTP-ase which catalyses GTP hydrolysis through stabilisation of the transition state.
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.
Biotin-dependent malonate decarboxylase (, malonate decarboxylase (with biotin), malonate decarboxylase) is an enzyme with systematic name malonate carboxy-lyase (biotin-dependent). This enzyme catalyses the following chemical reaction : malonate + H+ \rightleftharpoons acetate + CO2 Two types of malonate decarboxylase are currently known, both of which form multienzyme complexes.
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.
Farnesylcysteine lyase (, FC lyase, FCLY) is an enzyme with systematic name S-(2E,6E)-farnesyl-L-cysteine oxidase. This enzyme catalyses the following chemical reaction : S-(2E,6E)-farnesyl-L-cysteine + O2 \+ H2O \rightleftharpoons (2E,6E)-farnesal + L-cysteine + H2O2 Farnesylcysteine lyase is a flavoprotein (FAD).
Meprin B (, meprin-b) is an enzyme. This enzyme catalyses the following chemical reaction : Hydrolysis of proteins, including azocasein, and peptides. Hydrolysis of -His5-Leu-, -Leu6-Cys-, -Ala14-Leu- and -Cys19-Gly- bonds in insulin B chain This membrane-bound metalloendopeptidase is present in mouse intestines.
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).
Methylphenyltetrahydropyridine N-monooxygenase () is an enzyme with systematic name 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine:oxygen N-oxidoreductase. This enzyme catalyses the following chemical reaction : 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine + O2 \rightleftharpoons 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine N-oxide + methanol Methylphenyltetrahydropyridine N-monooxygenase is a flavoprotein.
Pheophorbide A oxygenase (, pheide a monooxygenase, pheide a oxygenase, PAO) is an enzyme with systematic name pheophorbide-a,NADPH:oxygen oxidoreductase (biladiene-forming). This enzyme catalyses the following chemical reaction : Pheophorbide A + NADPH + H+ \+ O2 \rightleftharpoons red chlorophyll catabolite + NADP+ Pheophorbide A oxygenase participates in chlorophyll degradation.
Zeaxanthin glucosyltransferase (, crtX (gene)) is an enzyme with systematic name UDP-glucose:zeaxanthin beta-D-glucosyltransferase. This enzyme catalyses the following chemical reaction : 2 UDP-glucose + zeaxanthin \rightleftharpoons 2 UDP + zeaxanthin bis(beta-D-glucoside) The reaction proceeds in two steps with the monoglucoside as an intermediate.
Linoleate 9S-lipoxygenase (, 9-lipoxygenase, 9S-lipoxygenase, linoleate 9-lipoxygenase, LOX1 (gene), 9S-LOX) is an enzyme with systematic name linoleate:oxygen 9S-oxidoreductase. This enzyme catalyses the following chemical reaction : linoleate + O2 \rightleftharpoons (9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate Linoleate 9S-lipoxygenase contains nonheme iron.
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+.
Cyclohexanone monooxygenase (, cyclohexanone 1,2-monooxygenase, cyclohexanone oxygenase, cyclohexanone:NADPH:oxygen oxidoreductase (6-hydroxylating, 1,2-lactonizing)) is an enzyme with systematic name cyclohexanone,NADPH:oxygen oxidoreductase (lactone-forming). This enzyme catalyses the following chemical reaction : cyclohexanone + NADPH + H+ \+ O2 \rightleftharpoons hexano-6-lactone + NADP+ \+ H2O Cyclohexanone monooxygenase is a flavoprotein (FAD).
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.
Adrenodoxin-NADP+ reductase (, adrenodoxin reductase, nicotinamide adenine dinucleotide phosphate-adrenodoxin reductase, ADR, NADPH:adrenal ferredoxin oxidoreductase) is an enzyme with systematic name adrendoxin:NADP+ oxidoreductase. This enzyme catalyses the following chemical reaction : 2 reduced adrenodoxin + NADP+ \rightleftharpoons 2 oxidized adrenodoxin + NADPH + H+ Adrenodoxin-NADP+ reductase is a flavoprotein (FAD).
Abieta-7,13-diene hydroxylase () is an enzyme with systematic name abieta-7,13-diene,NADPH:oxygen oxidoreductase (18-hydroxylating). This enzyme catalyses the following chemical reaction : abieta-7,13-diene + NADPH + H+ \+ O2 \rightleftharpoons abieta-7,13-dien-18-ol + NADP+ \+ H2O Abietadiene hydroxylase is a heme-thiolate protein (P-450).
Neopentalenolactone D synthase (, ptlE (gene)) is an enzyme with systematic name 1-deoxy-11-oxopentalenate,NADH:oxygen oxidoreductase (neopentalenolactone-D forming). This enzyme catalyses the following chemical reaction : 1-deoxy-11-oxopentalenate + NADPH + H+ \+ O2 \rightleftharpoons neopentalenolactone D + NADP+ \+ H2O Neopentalenolactone D synthase is a FAD- dependent oxygenase.
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.
Erythromycin 12 hydroxylase (, EryK) is an enzyme with systematic name erythromycin-D,NADPH:oxygen oxidoreductase (12-hydroxylating) . This enzyme catalyses the following chemical reaction : erythromycin D + NADPH + H+ \+ O2 \rightleftharpoons erythromycin C + NADP+ \+ H2O Erythromycin 12 hydroxylase is responsible for the C-12 hydroxylation of the macrolactone ring.
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.
Cathepsin V (, Cathepsin L2, cathepsin U) is an enzyme that catalyses the following chemical reaction: The recombinant enzyme hydrolyses proteins (serum albumin, collagen) and synthetic substrates (Z-Phe-Arg-NHMec > Z-Leu-Arg-NHMec > Z-Val-Arg-NHMec) Cathepsin V is a human lysosomal cysteine endopeptidase.
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.
Olivetolic acid cyclase (, OAC) is an enzyme with systematic name 3,5,7-trioxododecanoyl-CoA CoA-lyase (2,4-dihydroxy-6-pentylbenzoate-forming). This enzyme catalyses the following chemical reaction : 3,5,7-trioxododecanoyl-CoA → CoA + 2,4-dihydroxy-6-pentylbenzoate This enzymes participates in the cannabinoids biosynthesis in the plant Cannabis sativa.
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.
Pantoate kinase (, PoK, TK2141 protein) is an enzyme with systematic name ATP:(R)-pantoate 4-phosphotransferase. This enzyme catalyses the following chemical reaction : ATP + (R)-pantoate \rightleftharpoons ADP + (R)-4-phosphopantoate The conversion of (R)-pantoate to (R)-4'-phosphopantothenate is done during biosynthesis of 4'-phosphopantetheine,.
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.
Neamine transaminase (, glutamate---6'-dehydroparomamine aminotransferase, btrB (gene), neoN (gene), kacL (gene)) is an enzyme with systematic name neamine:2-oxoglutarate aminotransferase. This enzyme catalyses the following chemical reaction : neamine + 2-oxoglutarate \rightleftharpoons 6'-dehydroparomamine + L-glutamate The reaction occurs in vivo in the opposite direction.
D-amino-acid dehydrogenase (EC 1.4.99.1) is a bacterial enzyme that catalyses the oxidation of D-amino acids into their corresponding oxoacids. It contains both flavin and nonheme iron as cofactors. The enzyme has a very broad specificity and can act on most D-amino acids.
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.
Protein phosphatase methylesterase-1 (, PME-1, PPME1) is an enzyme with systematic name (phosphatase 2A protein)-leucine ester acylhydrolase. This enzyme catalyses the following chemical reaction : [phosphatase 2A protein]-leucine methyl ester + H2O \rightleftharpoons [phosphatase 2A protein]-leucine + methanol A key regulator of protein phosphatase 2A.
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.
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).
Exodeoxyribonuclease (phage SP3-induced) (, phage SP3 DNase, DNA 5'-dinucleotidohydrolase, deoxyribonucleate 5'-dinucleotidase, deoxyribonucleic 5'-dinucleotidohydrolase, bacteriophage SP3 deoxyribonuclease) is an enzyme. This enzyme catalyses the following chemical reaction : Exonucleolytic cleavage in the 5'- to 3'-direction to yield nucleoside 5'-phosphates Preference for single-stranded DNA.
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.
In bacteria HDH is a single chain polypeptide; in fungi it is the C-terminal domain of a multifunctional enzyme which catalyses three different steps of histidine biosynthesis; and in plants it is expressed as a nuclear encoded protein precursor which is exported to the chloroplast.
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.
Endopeptidase So (, E. coli cytoplasmic proteinase, proteinase So, Escherichia coli serine proteinase So) is an enzyme. This enzyme catalyses the following chemical reaction : Hydrolysis of proteins, but not Bz-Tyr-OEt, Ac-Phe-beta- naphthylester, or Bz-Arg-OEt This is an Escherichia coli cytoplasmic endopeptidase.
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.
Beta-aspartyl-peptidase (, beta-aspartyl dipeptidase, beta-aspartyl peptidase, beta-aspartyldipeptidase) is an enzyme. This enzyme catalyses the following chemical reaction : Cleavage of a beta-linked Asp residue from the N-terminus of a polypeptide Other isopeptide bonds, e.g. gamma-glutamyl and beta-alanyl, are not hydrolysed.
Biotin-independent malonate decarboxylase (, malonate decarboxylase (without biotin), malonate decarboxylase, MDC) is an enzyme with systematic name malonate carboxy-lyase (biotin-independent). This enzyme catalyses the following chemical reaction : malonate + H+ \rightleftharpoons acetate + CO2 Two types of malonate decarboxylase are currently known, both of which form multienzyme complexes.
Ed., 2004, 43, p. 1017-1021Ziegler, D. S.; Karaghiosoff, K.; Knochel, P., « Generation of Aryl and Heteroaryl Magnesium Reagents in Toluene by Br/Mg or Cl/Mg Exchange », Angew. Chem. Int. Ed., 2018, 57, p. 6701-6704 catalyses the halogen-metal exchange in the preparation of organomagnesians and organozinciques.
Omega-hydroxypalmitate O-feruloyl transferase (, hydroxycinnamoyl-CoA omega- hydroxypalmitic acid O-hydroxycinnamoyltransferase, HHT) is an enzyme with systematic name feruloyl-CoA:16-hydroxypalmitate feruloyltransferase. This enzyme catalyses the following chemical reaction : feruloyl-CoA + 16-hydroxypalmitate \rightleftharpoons CoA + 16-feruloyloxypalmitate p-Coumaroyl-CoA and sinapoyl-CoA also act as substrates.
Nardilysin (, N-arginine dibasic convertase, NRD-convertase) is an enzyme. This enzyme catalyses the following chemical reaction : Hydrolysis of polypeptides, preferably at -Xaa-Arg-Lys-, and less commonly at -Arg-Arg-Xaa-, in which Xaa is not Arg or Lys This enzyme is present rat brain and testis.
Bothrolysin (, Bothrops metalloendopeptidase J, J protease) is an enzyme. This enzyme catalyses the following chemical reaction : Cleavage of Gln4-His, Ser9-His and Ala14-Leu of insulin B chain and Pro-Phe of angiotensin I This endopeptidase is present in the venom of the jararaca snake (Bothrops jararaca).
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.
Snapalysin (, small neutral protease, SnpA gene product (Streptomyces lividans)) is an enzyme. This enzyme catalyses the following chemical reaction : Hydrolyses proteins with a preference for Tyr or Phe in the P1' position. Has no action on amino-acid p-nitroanilides This enzyme belongs to the peptidase family M7.
8-oxo-dGTP diphosphatase (, MutT, 7,8-dihydro-8-oxoguanine triphosphatase, 8-oxo-dGTPase, 7,8-dihydro-8-oxo-dGTP pyrophosphohydrolase) is an enzyme with systematic name 8-oxo-dGTP diphosphohydrolase. This enzyme catalyses the following chemical reaction: : 8-oxo-dGTP + H2O \rightleftharpoons 8-oxo-dGMP + diphosphate This enzyme requires Mg2+.
Crotonyl-CoA carboxylase/reductase (, CCR, crotonyl-CoA reductase (carboxylating)) is an enzyme with systematic name (2S)-ethylmalonyl-CoA:NADP+ oxidoreductase (decarboxylating). This enzyme catalyses the following chemical reaction : (2S)-ethylmalonyl-CoA + NADP+ \rightleftharpoons (E)-but-2-enoyl- CoA + CO2 \+ NADPH + H+ The reaction is catalysed in the reverse direction.
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.
Glutaryl-CoA dehydrogenase (non-decarboxylating) (, GDHDes, nondecarboxylating glutaryl-coenzyme A dehydrogenase, nondecarboxylating glutaconyl-coenzyme A-forming GDH) is an enzyme with systematic name glutaryl-CoA:acceptor 2,3-oxidoreductase (non-decarboxylating). This enzyme catalyses the following chemical reaction : glutaryl-CoA + acceptor \rightleftharpoons (E)-glutaconyl- CoA + reduced acceptor The enzyme contains FAD.
Glycine oxidase () is an enzyme with systematic name glycine:oxygen oxidoreductase (deaminating). This enzyme catalyses the following chemical reaction : glycine + H2O + O2 \rightleftharpoons glyoxylate + NH3 \+ H2O2 (overall reaction) :(1a) glycine + O2 \rightleftharpoons 2-iminoacetate + H2O2 :(1b) 2-iminoacetate + H2O \rightleftharpoons glyoxylate + NH3 This flavoenzyme containing non-covalently bound FAD.
FAD reductase (NAD(P)H) (, GTNG_3158 (gene)) is an enzyme with systematic name FADH2:NAD(P)+ oxidoreductase. This enzyme catalyses the following chemical reaction : FADH2 \+ NAD(P)+ \rightleftharpoons FAD + NAD(P)H + H+ This enzyme is isolated from the bacterium Geobacillus thermodenitrificans. It takes part in degradation tryptophan.
L-saccharopine oxidase (, FAP2) is an enzyme with systematic name L-saccharopine:oxygen oxidoreductase (L-glutamate forming). This enzyme catalyses the following chemical reaction : N6-(L-1,3-dicarboxypropyl)-L-lysine + H2O + O2 \rightleftharpoons (S)-2-amino-6-oxohexanoate + L-glutamate + H2O2 The enzyme is involved in pipecolic acid biosynthesis.
2-oxoglutarate dioxygenase (ethylene-forming) (, ethylene-forming enzyme, EFE) is an enzyme with systematic name 2-oxoglutarate:oxygen oxidoreductase (decarboxylating, ethylene-forming). This enzyme catalyses the following chemical reaction : 2-oxoglutarate + O2 \rightleftharpoons ethylene + 3 CO2 \+ H2O 2-oxoglutarate dioxygenase produces ethylene in bacteria of the Pseudomonas syringae group.
Glucosylglycerate synthase (, Ggs (gene)) is an enzyme with systematic name ADP-glucose:D-glycerate 2-alpha-D-glucosyltransferase. This enzyme catalyses the following chemical reaction : ADP-glucose + D-glycerate \rightleftharpoons 2-O-(alpha-D-glucopyranosyl)-D-glycerate + ADP Persephonella marina possesses two enzymatic systems for the synthesis of glucosylglycerate.
1,2-dihydroxynaphthalene dioxygenase (, 1,2-DHN dioxygenase, DHNDO, 1,2-dihydroxynaphthalene oxygenase, 1,2-dihydroxynaphthalene:oxygen oxidoreductase) is an enzyme with systematic name naphthalene-1,2-diol:oxygen oxidoreductase. This enzyme catalyses the following chemical reaction : naphthalene-1,2-diol + O2 \rightleftharpoons 2-hydroxy-2H-chromene-2-carboxylate This enzyme is involved in naphthalene degradation.
Ribonucleoside-triphosphate reductase (, ribonucleotide reductase, 2'-deoxyribonucleoside-triphosphate:oxidized-thioredoxin 2'-oxidoreductase) is an enzyme with systematic name 2'-deoxyribonucleoside- triphosphate:thioredoxin-disulfide 2'-oxidoreductase. This enzyme catalyses the following chemical reaction : 2'-deoxyribonucleoside triphosphate + thioredoxin disulfide + H2O \rightleftharpoons ribonucleoside triphosphate + thioredoxin Ribonucleoside-triphosphate reductase requires a cobamide coenzyme and ATP.
Germacrene A hydroxylase () is an enzyme with systematic name (+)-germacrene-A,NADPH:oxygen oxidoreductase (12-hydroxylating). This enzyme catalyses the following chemical reaction : (+)-germacrene A + NADPH + H+ \+ O2 \rightleftharpoons germacra-1(10),4,11(13)-trien-12-ol + NADP+ \+ H2O Germacrene A hydroxylase is a heme-thiolate protein (P-450).
6-Hydroxynicotinate 3-monooxygenase (, NicC, 6HNA monooxygenase, HNA-3-monooxygenase) is an enzyme with systematic name 6-hydroxynicotinate,NADH:oxygen oxidoreductase (3-hydroxylating, decarboxylating). This enzyme catalyses the following chemical reaction : 6-hydroxynicotinate + NADH + H+ \+ O2 \rightleftharpoons 2,5-dihydroxypyridine + NAD+ \+ H2O + CO2 6-Hydroxynicotinate 3-monooxygenase a flavoprotein (FAD).
Diapolycopene oxygenase (, crtP) is an enzyme with systematic name 4,4'-diapolycopene,AH2:oxygen oxidoreductase (4,4'-hydroxylating). This enzyme catalyses the following chemical reaction : 4,4'-diapolycopene + 4 AH2 \+ 4 O2 \rightleftharpoons 4,4'-diapolycopenedial + 4 A + 6 H2O Diapolycopene oxygenase is involved in the biosynthesis of C30 carotenoids such as staphyloxanthin.
4-nitrophenol 4-monooxygenase (, pnpA (gene), pdcA (gene)) is an enzyme with systematic name 4-nitrophenol,NAD(P)H:oxygen 4-oxidoreductase (4-hydroxylating, nitrite-forming). This enzyme catalyses the following chemical reaction : 4-nitrophenol + NADPH + H+ \+ O2 \rightleftharpoons 1,4-benzoquinone + nitrite + NADP+ \+ H2O 4-nitrophenol 4-monooxygenase contains FAD.
Pentalenolactone D synthase (, penE (gene), pntE (gene)) is an enzyme with systematic name 1-deoxy-11-oxopentalenate,NADH:oxygen oxidoreductase (pentalenolactone-D forming). This enzyme catalyses the following chemical reaction : 1-deoxy-11-oxopentalenate + NADPH + H+ \+ O2 \rightleftharpoons pentalenolactone D + NADP+ \+ H2O Pentalenolactone D synthase is a FAD- dependent oxygenase.
Tryptophan 7-halogenase (, PrnA, RebH) is an enzyme with systematic name L-tryptophan:FADH2 oxidoreductase (7-halogenating). This enzyme catalyses the following chemical reaction: : tryptophan + FADH2 \+ Cl− \+ O2 \+ H+ \rightleftharpoons 7-chloro-L-tryptophan + FAD + 2 H2O The enzyme can use bromide ions (Br−) in place of chloride (Cl−).
Pyrrole-2-carboxylate monooxygenase (, pyrrole-2-carboxylate oxygenase) is an enzyme with systematic name pyrrole-2-carboxylate,NADH:oxygen oxidoreductase (5-hydroxylating). This enzyme catalyses the following chemical reaction : pyrrole-2-carboxylate + NADH + H+ \+ O2 \rightleftharpoons 5-hydroxypyrrole-2-carboxylate + NAD+ \+ H2O Pyrrole-2-carboxylate monooxygenase is a flavoprotein (FAD).
Dimethyl-sulfide monooxygenase (, dimethylsulfide monooxygenase) is an enzyme with systematic name dimethyl sulfide,NADH:oxygen oxidoreductase. This enzyme catalyses the following chemical reaction : dimethyl sulfide + O2 \+ NADH + H+ \rightleftharpoons methanethiol + formaldehyde + NAD+ \+ H2O Dimethyl-sulfide monooxygenase has lower activity with diethyl sulfide and other short-chain alkyl methyl sulfides.
Copal-8-ol diphosphate hydratase (, CcCLS) is an enzyme with systematic name geranylgeranyl-diphosphate hydro-lyase ((13E)-8alpha-hydroxylabda-13-en-15-yl diphosphate forming). This enzyme catalyses the following chemical reaction : (13E)-8alpha-hydroxylabda-13-en-15-yl diphosphate \rightleftharpoons geranylgeranyl diphosphate + H2O This enzyme requires Mg2+.
Arabidiol synthase (, PEN1 (gene), (S)-squalene-2,3-epoxide hydro-lyase (arabidiol forming)) is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualene hydro-lyase (arabidiol forming). This enzyme catalyses the following chemical reaction : arabidiol \rightleftharpoons (3S)-2,3-epoxy-2,3-dihydrosqualene + H2O The reaction occurs in the reverse direction.
Beta-chamigrene synthase () is an enzyme with systematic name (2E,6E)-farnesyl diphosphate lyase (cyclizing, (+)-beta-chamigrene-forming). This enzyme catalyses the following chemical reaction : (2E,6E)-farnesyl diphosphate \rightleftharpoons (+)-beta-chamigrene + diphosphate The recombinant enzyme from the plant Arabidopsis thaliana produces (+)-alpha-barbatene, (+)-thujopsene and (+)-beta-chamigrene.
Gamma-curcumene synthase (, PatTpsA (gene)) is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate diphosphate-lyase (cyclizing, gamma-curcumene- forming). This enzyme catalyses the following chemical reaction : (2E,6E)-farnesyl diphosphate \rightleftharpoons gamma-curcumene + diphosphate This enzyme is one of five sesquiterpenoid synthases in Pogostemon cablin (patchouli).
1,8-cineole synthase (, 1,8-cineole cyclase, geranyl pyrophoshate:1,8-cineole cyclase, 1,8-cineole synthetase) is an enzyme with systematic name geranyl- diphosphate diphosphate-lyase (cyclizing, 1,8-cineole-forming). This enzyme catalyses the following chemical reaction : geranyl diphosphate + H2O \rightleftharpoons 1,8-cineole + diphosphate This enzyme requires Mn2+ or Zn2+.
Threo-3-hydroxy-D-aspartate ammonia-lyase (, D-threo-3-hydroxyaspartate dehydratase) is an enzyme with systematic name threo-3-hydroxy-D-aspartate ammonia-lyase (oxaloacetate-forming). This enzyme catalyses the following chemical reaction : threo-3-hydroxy-D-aspartate \rightleftharpoons oxaloacetate + NH3 This enzyme is a pyridoxal-phosphate protein.
Methanol dehydrogenase (cytochrome c) (, methanol dehydrogenase, MDH) is an enzyme with systematic name methanol:cytochrome c oxidoreductase. This enzyme catalyses the following chemical reaction : a primary alcohol + 2 ferricytochrome cL \rightleftharpoons an aldehyde + 2 ferrocytochrome cL + 2 H+ A periplasmic quinoprotein alcohol dehydrogenase is only present in methylotrophic bacteria.
Paromamine 6'-oxidase (, btrQ (gene), neoG (gene), kanI (gene), tacB (gene)) is an enzyme with systematic name paromamine:oxygen 6'-oxidoreductase. This enzyme catalyses the following chemical reaction : paromamine + O2 \rightleftharpoons 6'-dehydroparomamine + H2O2 This enzymes participates in biosynthesis of several aminocyclitol antibiotics, including kanamycin, butirosin, neomycin and ribostamycin.
Delta-amyrin synthase (, SlTTS2 (gene)) is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualene mutase (cyclizing, delta-amyrin-forming). This enzyme catalyses the following chemical reaction : (3S)-2,3-epoxy-2,3-dihydrosqualene \rightleftharpoons delta-amyrin The enzyme from tomato (Solanum lycopersicum) gives delta-amyrin, alpha-amyrin, beta- amyrin.
CDP-abequose synthase (, rfbJ (gene)) is an enzyme with systematic name CDP- alpha-D-abequose:NADP+ 4-oxidoreductase. This enzyme catalyses the following chemical reaction : CDP-alpha-D-abequose + NADP+ \rightleftharpoons CDP-4-dehydro-3,6-dideoxy-alpha-D-glucose + NADPH + H+ This enzyme is from Yersinia pseudotuberculosis and Salmonella enterica.
CDP-paratose synthase (, rfbS (gene)) is an enzyme with systematic name CDP- alpha-D-paratose:NADP+ 4-oxidoreductase. This enzyme catalyses the following chemical reaction : CDP-alpha-D-paratose + NADP+ \rightleftharpoons CDP-4-dehydro-3,6-dideoxy-alpha-D-glucose + NADPH + H+ This enzyme participates in synthesis of paratose and tyvelose.
Syn-copalyl-diphosphate synthase (, OsCyc1, OsCPSsyn, syn-CPP synthase, syn- copalyl diphosphate synthase) is an enzyme with systematic name 9alpha- copalyl-diphosphate lyase (decyclizing). This enzyme catalyses the following chemical reaction : geranylgeranyl diphosphate \rightleftharpoons 9alpha- copalyl diphosphate This enzyme requires a divalent metal ion, preferably Mg2+, for activity.
Hydantoin racemase (, 5'-monosubstituted-hydantoin racemase, HyuA, HyuE) is an enzyme with systematic name D-5-monosubstituted-hydantoin racemase. This enzyme catalyses the following chemical reaction : D-5-monosubstituted hydantoin \rightleftharpoons L-5-monosubstituted hydantoin This enzyme is a part of the reaction cascade known as the "hydantoinase process".
Prolycopene isomerase (, CRTISO, carotene cis-trans isomerase, ZEBRA2 (gene), carotene isomerase, carotenoid isomerase) is an enzyme with systematic name 7,9,7',9'-tetracis-lycopene cis-trans-isomerase. This enzyme catalyses the following chemical reaction : 7,9,7',9'-tetracis-lycopene \rightleftharpoons all-trans-lycopene This enzyme is involved in carotenoid biosynthesis.
Benzil reductase ((R)-benzoin forming) () is an enzyme with systematic name (R)-benzoin:NADP+ oxidoreductase. This enzyme catalyses the following chemical reaction : (R)-benzoin + NADP+ \rightleftharpoons benzil + NADPH + H+ The bacterial enzyme (Xanthomonas oryzae) enantioselectively reduces one of the two carbonyl groups of benzil to form optically active (R)-benzoin.
4-oxalomesaconate tautomerase (, GalD) is an enzyme with systematic name 4-oxalomesaconate keto---enol-isomerase. This enzyme catalyses the following chemical reaction : (1E)-4-oxobut-1-ene-1,2,4-tricarboxylate \rightleftharpoons (1E,3E)-4-hydroxybuta-1,3-diene-1,2,4-tricarboxylate This enzyme has been characterized from the bacterium Pseudomonas putida.
Adenosyl-chloride synthase (, chlorinase, 5'-chloro-5'-deoxyadenosine synthase) is an enzyme with systematic name S-adenosyl-L-methionine:chloride adenosyltransferase. This enzyme catalyses the following chemical reaction : S-adenosyl-L-methionine + chloride \rightleftharpoons 5-deoxy-5-chloroadenosine + L-methionine This enzyme is isolated from the marine bacterium Salinispora tropica.
2-Phospho-L-lactate guanylyltransferase (, CofC, MJ0887) is an enzyme with systematic name GTP:2-phospho-L-lactate guanylyltransferase. This enzyme catalyses the following chemical reaction : (2S)-2-phospholactate + GTP \rightleftharpoons (2S)-lactyl-2-diphospho-5'-guanosine + diphosphate This enzyme is involved in the biosynthesis of coenzyme F420.
The Staphylococcus aureus sortase is a transpeptidase that attaches surface proteins to the cell wall; it cleaves between the Gly and Thr of the LPXTG motif and catalyses the formation of an amide bond between the carboxyl-group of threonine and the amino-group of the cell-wall peptidoglycan.
Mandelate racemase () is a bacterial enzyme which catalyzes the interconversion of the enantiomers of mandelate via an enol intermediate. This enzyme catalyses the following chemical reaction : (S)-mandelate \rightleftharpoons (R)-mandelate It is a member of the enolase superfamily of enzymes, along with muconate lactonizing enzyme and enolase.
Adenosylhomocysteinase (, S-adenosylhomocysteine synthase, S-adenosylhomocysteine hydrolase, adenosylhomocysteine hydrolase, S-adenosylhomocysteinase, SAHase, AdoHcyase) is an enzyme that converts S-adenosylhomocysteine to homocysteine and adenosine. This enzyme catalyses the following chemical reaction : S-adenosyl-L-homocysteine + H2O L-homocysteine + adenosine The enzyme contains one tightly bound NAD+ per subunit.
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.
Beta-Ala-His dipeptidase (, serum carnosinase) is an enzyme. This enzyme catalyses the following chemical reaction : Preferential hydrolysis of the beta-Ala!His dipeptide (carnosine), and also anserine, Xaa!His dipeptides and other dipeptides including homocarnosine This enzyme is present in the serum of humans and higher primates.
PepB aminopeptidase (, Salmonella enterica serovar Typhimurium peptidase B) is an enzyme which catalyses the following chemical reaction: : Release of an N-terminal amino acid, Xaa, from a peptide or arylamide. Xaa is preferably Glu or Asp, but may be other amino acids, including Leu, Met, His, Cys and Gln.
1,4-dihydroxy-2-naphthoyl-CoA hydrolase () is an enzyme with systematic name 1,4-dihydroxy-2-naphthoyl-CoA hydrolase. This enzyme catalyses the following chemical reaction : 1,4-dihydroxy-2-naphthoyl-CoA + H2O \rightleftharpoons 1,4-dihydroxy-2-naphthoate + CoA This enzyme participates in the biosynthesis of menaquinones, , and several plant pigments.
Exoribonuclease H () is an enzyme. This enzyme catalyses the following chemical reaction : 3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid This is a secondary reaction to the RNA 5'-end directed cleavage 13-19 nucleotides from the RNA end performed by EC 3.1.26.13 (retroviral ribonuclease H).
CC-preferring endodeoxyribonuclease (, Streptomyces glaucescens exocytoplasmic dodeoxyribonuclease) is an enzyme. This enzyme catalyses the following chemical reaction : endonucleolytic cleavage to give 5'-phosphooligonucleotide end-products, with a preference for cleavage within the sequence CC This enzyme has preference for CC sites in double-stranded circular and linear DNA.
Ribonuclease (poly-(U)-specific) (, ribonuclease (uracil-specific), uracil- specific endoribonuclease, uracil-specific RNase) is an enzyme. This enzyme catalyses the following chemical reaction : Endonucleolytic cleavage of poly(U) to fragments terminated by 3'-hydroxy and 5'-phosphate groups This enzyme forms oligonucleotides with chain lengths of 6 to 12.
2,3-bisphosphoglycerate 3-phosphatase (, MIPP1, 2,3-BPG 3-phosphatase) is an enzyme with systematic name 2,3-bisphospho-D-glycerate 3-phosphohydrolase. This enzyme catalyses the following chemical reaction : 2,3-bisphospho-D- glycerate + H2O \rightleftharpoons 2-phospho-D-glycerate + phosphate This reaction is a shortcut in the Luebering-Rapoport pathway.
Calpain-3 (, p94, calpain p94, CAPN3, muscle calpain, calpain 3, calcium- activated neutral proteinase 3, muscle-specific calcium-activated neutral protease 3, CANP 3, calpain L3) is an enzyme. This enzyme catalyses the following chemical reaction : Broad endopeptidase activity This Ca2+ dependent enzyme is found in skeletal muscles.
Streptogrisin B (, Streptomyces griseus protease B, pronase B, serine proteinase B, Streptomyces griseus proteinase B, Streptomyces griseus proteinase 1, Streptomyces griseus serine proteinase B) is an enzyme. This enzyme catalyses the following chemical reaction : Hydrolysis of proteins with trypsin-like specificity This enzyme is isolated from Streptomyces griseus.
Streptogrisin A (, Streptomyces griseus protease A, protease A, proteinase A, Streptomyces griseus proteinase A, Streptomyces griseus serine proteinase 3, Streptomyces griseus serine proteinase A) is an enzyme. This enzyme catalyses the following chemical reaction : Hydrolysis of proteins with specificity similar to chymotrypsin This enzyme is isolated from Streptomyces griseus.
Equine arterivirus serine peptidase () is an enzyme. This enzyme catalyses the following chemical reaction : Cleavage of (Glu/Gln)-(Gly/Ser/Ala) in arterivirus replicase translation products ORF1a and ORF1ab In the equine arterivirus (EAV), the replicase gene is translated into open reading frame 1a (ORF1a) and ORF1ab [polyprotein]s.
SpoIVB peptidase (, sporulation factor IV B protease) is an enzyme. This enzyme catalyses the following chemical reaction : Self-cleaves Val52-Asn53, Ala62-Phe63 and Val74-Thr75 at the N-terminus of SpoIVB This enzyme participates in gene expression during the later stages of spore formation in Bacillus subtilis.
Scutelarin (, taipan activator, Oxyuranus scutellatus prothrombin-activating proteinase) is an enzyme. This enzyme catalyses the following chemical reaction : Selective cleavage of Arg-Thr and Arg-Ile in prothrombin to form thrombin and two inactive fragments This enzyme is isolated from the venom of the Taipan snake (Oxyuranus scutellatus).
Helper-component proteinase (, HC-Pro) is an enzyme. This enzyme catalyses the following chemical reaction : Hydrolyses a Gly-Gly bond at its own C-terminus, commonly in the sequence -Tyr-Xaa-Val-Gly-Gly, in the processing of the potyviral polyprotein This enzyme is present in many potyviruses.
The energy required for domain closure comes from the interaction of the enzyme with the substrate. Type II enzymes possess an extra N-terminal beta-sheet domain, and some type II enzymes are allosterically inhibited by NADH. 2-methylcitrate synthase catalyses the conversion of oxaloacetate and propanoyl-CoA into (2R,3S)-2-hydroxybutane-1,2,3-tricarboxylate and coenzyme A. This enzyme is induced during bacterial growth on propionate, while type II hexameric citrate synthase is constitutive. ATP citrate lyase catalyses the Mg.ATP-dependent, CoA-dependent cleavage of citrate into oxaloacetate and acetyl-CoA, a key step in the reductive tricarboxylic acid pathway of CO2 assimilation used by a variety of autotrophic bacteria and archaea to fix carbon dioxide.
Ketosteroid monooxygenase (, steroid-ketone monooxygenase, progesterone, NADPH2:oxygen oxidoreductase (20-hydroxylating, ester-producing), 17alpha- hydroxyprogesterone, NADPH2:oxygen oxidoreductase (20-hydroxylating, side- chain cleaving), androstenedione, NADPH2:oxygen oxidoreductase (17-hydroxylating, lactonizing)) is an enzyme with systematic name ketosteroid,NADPH:oxygen oxidoreductase (20-hydroxylating, ester- producing/20-hydroxylating, side-chain cleaving/17-hydroxylating, lactonizing). This enzyme catalyses the following chemical reaction : ketosteroid + NADPH + H+ \+ O2 \rightleftharpoons steroid ester/lactone + NADP+ \+ H2O (general reaction) :(1) progesterone + NADPH + H+ \+ O2 \rightleftharpoons testosterone acetate + NADP+ \+ H2O :(2) androstenedione + NADPH + H+ \+ O2 \rightleftharpoons testololactone + NADP+ \+ H2O :(3) 17alpha-hydroxyprogesterone + NADPH + H+ \+ O2 \rightleftharpoons androstenedione + acetate + NADP+ \+ H2O Ketosteroid monooxygenase is a single FAD-containing enzyme that catalyses three types of monooxygenase reaction.
8-hydroxygeraniol dehydrogenase (, 8-hydroxygeraniol oxidoreductase, CYP76B10, G10H, CrG10H, SmG10H, acyclic monoterpene primary alcohol:NADP+ oxidoreductase) is an enzyme with systematic name (6E)-8-hydroxygeraniol:NADP+ oxidoreductase. This enzyme catalyses the following chemical reaction : (6E)-8-hydroxygeraniol + 2 NADP+ \rightleftharpoons (6E)-8-oxogeranial + 2 NADPH + 2 H+ (overall reaction) : (1a) (6E)-8-hydroxygeraniol + NADP+ \rightleftharpoons (6E)-8-hydroxygeranial + NADPH + H+ : (1b) (6E)-8-hydroxygeraniol + NADP+ \rightleftharpoons (6E)-8-oxogeraniol + NADPH + H+ : (1c) (6E)-8-hydroxygeranial + NADP+ \rightleftharpoons (6E)-8-oxogeranial + NADPH + H+ : (1d) (6E)-8-oxogeraniol + NADP+ \rightleftharpoons (6E)-8-oxogeranial + NADPH + H+ This enzyme contains Zn2+. It catalyses the oxidation of (6E)-8-hydroxygeraniol to (6E)-8-oxogeranial via either (6E)-8-hydroxygeranial or (6E)-8-oxogeraniol.
UDP-N-acetylglucosamine—undecaprenyl-phosphate N-acetylglucosaminephosphotransferase (, UDP-N-acetylglucosamine:undecaprenyl- phosphate GlcNAc-1-phosphate transferase, WecA, WecA transferase, UDP- GIcNAc:undecaprenyl phosphate N-acetylglucosaminyl 1-P transferase, GlcNAc-P- P-Und synthase, GPT, TagO, UDP-GlcNAc:undecaprenyl-phosphate GlcNAc-1-phosphate transferase, UDP-N-acetyl-D-glucosamine:ditrans,octacis- undecaprenyl phosphate N-acetylglucosaminephosphotransferase) is an enzyme with systematic name UDP-N-acetyl-alpha-D-glucosamine:ditrans,octacis- undecaprenyl phosphate N-acetyl-alpha-D-glucosaminephosphotransferase. This enzyme catalyses the following chemical reaction : UDP-N-acetyl-alpha-D- glucosamine + ditrans, octacis-undecaprenyl phosphate \rightleftharpoons UMP + N-acetyl-alpha-D-glucosaminyldiphospho-ditrans, octacis-undecaprenol This enzyme catalyses the synthesis of ditrans, octacis-undecaprenyl-N-acetyl- alpha-D-glucosaminyl diphosphate.
Both the apo (PDB id: 3N6W); and the holo (PDB id: 3O2G); structures of gamma-butyrobetaine dioxygenase have been solved, demonstrating an induced fit mechanism may contribute to the catalytic activity of gamma-butyrobetaine dioxygenase. Gamma-butyrobetaine dioxygenase is promiscuous in substrate selectivity and it processes a number of modified substrates, including the natural catalytic products L-carnitine and D-carnitine, forming 3-dehydrocarnitine and trimethylaminoacetone. Gamma- butyrobetaine dioxygenase also catalyses the oxidation of mildronate to form multiple products including malonic acid semialdehyde, dimethylamine, formaldehyde and (1-methylimidazolidin-4-yl)acetic acid, which is proposed to be formed via a Stevens rearrangement mechanism. Gamma-butyrobetaine dioxygenase is unique among other human 2OG oxygenases that it catalyses both hydroxylation (e.g.
Polymerisation of coniferyl alcohol to lignin. The reaction has two alternative routes catalysed by two different oxidative enzymes, peroxidases or oxidases. An oxidative enzyme is an enzyme that catalyses an oxidation reaction. Two most common types of oxidative enzymes are peroxidases, which use hydrogen peroxide, and oxidases, which use molecular oxygen.
TRNA-dihydrouridine47 synthase (NAD(P)+) (, Dus3p, tRNA-dihydrouridine synthase 3) is an enzyme with systematic name tRNA-5,6-dihydrouracil47:NAD(P)+ oxidoreductase. This enzyme catalyses the following chemical reaction : 5,6-dihydrouracil47 in tRNA + NAD(P)+ \rightleftharpoons uracil47 in tRNA + NAD(P)H + H+ This enzyme specifically modifies uracil47 in tRNA.
TRNA-dihydrouridine20 synthase (NAD(P)+) (, Dus2p, tRNA-dihydrouridine synthase 2) is an enzyme with systematic name tRNA-5,6-dihydrouracil20:NAD(P)+ oxidoreductase. This enzyme catalyses the following chemical reaction : 5,6-dihydrouracil20 in tRNA + NAD(P)+ \rightleftharpoons uracil20 in tRNA + NAD(P)H + H+ This enzyme specifically modifies uracil20 in tRNA.
L-glutamyl-(BtrI acyl-carrier protein) decarboxylase (, btrK (gene)) is an enzyme with systematic name L-glutamyl-(BtrI acyl-carrier protein) carboxy- lyase. This enzyme catalyses the following chemical reaction : L-glutamyl-[BtrI acyl-carrier protein] \rightleftharpoons 4-amino butanoyl-[BtrI acyl-carrier protein] + CO2 This enzyme binds pyridoxal 5'-phosphate.
Nitric oxide reductase (NAD(P), nitrous oxide-forming) (, fungal nitric oxide reductase, cytochrome P450nor, NOR (ambiguous)) is an enzyme with systematic name nitrous oxide:NAD(P) oxidoreductase. This enzyme catalyses the following chemical reaction : N2O + NAD(P)+ \+ H2O \rightleftharpoons 2 NO + NAD(P)H + H+ This enzyme is heme-thiolate protein (P450).
Trimerelysin I (, Trimeresurus metalloendopeptidase I, hemorrhagic proteinase HR1A, hemorrhagic metalloproteinase HR1A, metalloproteinase HR1A) is an enzyme. This enzyme catalyses the following chemical reaction : Cleavage of only two bonds His10-Leu and Ala14-Leu in the insulin B chain This endopeptidase is present in the venom of the habu snake (Trimeresurus flavoviridis).
Upon the addition of a small amount of manganese dioxide, the hydrogen peroxide reacts rapidly. This effect is readily seen by the effervescence of oxygen. The manganese dioxide is not consumed in the reaction, and thus may be recovered unchanged, and re-used indefinitely. Accordingly, manganese dioxide catalyses this reaction.
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.
Carvone reductase () is an enzyme with systematic name (+)-dihydrocarvone:acceptor 1,6-oxidoreductase. This enzyme catalyses the following chemical reaction : (1) (+)-dihydrocarvone + acceptor \rightleftharpoons (-)-carvone + reduced acceptor : (2) (-)-isodihydrocarvone + acceptor \rightleftharpoons (+)-carvone + reduced acceptor This enzyme participates in the carveol and dihydrocarveol degradation pathway of the Gram-positive bacterium Rhodococcus erythropolis DCL14.
Polyamine oxidase (propane-1,3-diamine-forming) (, MPAO, maize PAO) is an enzyme with systematic name spermidine:oxygen oxidoreductase (propane-1,3-diamine-forming). This enzyme catalyses the following chemical reaction : spermidine + O2 \+ H2O \rightleftharpoons propane-1,3-diamine + 4-aminobutanal + H2O2 The products of the reaction cannot be converted directly to other polyamines.
Type III site-specific deoxyribonuclease (, type III restriction enzyme, restriction-modification system) is an enzyme. This enzyme catalyses the following chemical reaction : Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates This group of enzymes has an absolute requirement for ATP, but does not hydrolyse it.
Exoribonuclease II (, ribonuclease II, ribonuclease Q, BN ribonuclease, Escherichia coli exo-RNase II, RNase II, exoribonuclease (misleading), 5'-exoribonuclease) 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 preference for single-stranded RNA.
Nitronate monooxygenase (, NMO) is an enzyme with systematic name nitronate:oxygen 2-oxidoreductase (nitrite-forming). This enzyme catalyses the following chemical reaction : ethylnitronate + O2 \rightleftharpoons acetaldehyde + nitrite + other products The enzymes from the fungus Neurospora crassa and the yeast Williopsis saturnus var. mrakii contain non-covalently bound FMN as the cofactor.
Alpha,alpha-trehalose synthase (, trehalose synthase, trehalose synthetase, UDP-glucose:glucose 1-glucosyltransferase, TreT, PhGT) is an enzyme with systematic name ADP-glucose:D-glucose 1-alpha-D-glucosyltransferase. This enzyme catalyses the following chemical reaction : ADP-glucose + D-glucose \rightleftharpoons alpha,alpha-trehalose + ADP This enzyme requires Mg2+ for maximal activity.
Versatile peroxidase (, VP, hybrid peroxidase, polyvalent peroxidase) is an enzyme with systematic name reactive-black-5:hydrogen-peroxide oxidoreductase. This enzyme catalyses the following chemical reaction : (1) Reactive Black 5 + H2O2 \rightleftharpoons oxidized Reactive Black 5 + 2 H2O : (2) donor + H2O2 \rightleftharpoons oxidized donor + 2 H2O Versatile peroxidase is a hemoprotein.
Fatty-acid peroxygenase (, fatty acid hydroxylase (ambiguous), P450 peroxygenase, CYP152A1, P450BS, P450SPalpha) is an enzyme with systematic name fatty acid:hydroperoxide oxidoreductase (RH-hydroxylating). This enzyme catalyses the following chemical reaction : fatty acid + H2O2 \rightleftharpoons 3- or 2-hydroxy fatty acid + H2O Fatty-acid peroxygenase is a cytosolic heme-thiolate protein.
Polyporopepsin (, Polyporus aspartic proteinase, Irpex lacteus aspartic proteinase, Irpex lacteus carboxyl proteinase B) is an enzyme. This enzyme catalyses the following chemical reaction : Milk clotting activity, broad specificity, but fails to cleave Leu15-Tyr or Tyr16-Leu of insulin B chain This enzyme is isolated from the basidiomycete Polyporus tulipiferae.
Nicotinate dehydrogenase (cytochrome) (, nicotinic acid hydroxylase, nicotinate hydroxylase) is an enzyme with systematic name nicotinate:cytochrome 6-oxidoreductase (hydroxylating). This enzyme catalyses the following chemical reaction 400px nicotinate + a ferricytochrome + H2O \rightleftharpoons 6-hydroxynicotinate + a ferrocytochrome + 2 H+ This smelly two-component enzyme from Pseudomonas belongs to the family of xanthine dehydrogenases.
Arsenate reductase (cytochrome c) (, arsenite oxidase) is an enzyme with systematic name arsenite:cytochrome c oxidoreductase. This enzyme catalyses the following chemical reaction : arsenite + H2O + 2 oxidized cytochrome c \rightleftharpoons arsenate + 2 reduced cytochrome c + 2 H+ Arsenate reductase is a molybdoprotein isolated from alpha-proteobacteria that contains iron- sulfur clusters.
7-dimethylallyltryptophan synthase (, 7-DMATS) is an enzyme with systematic name dimethylallyl-diphosphate:L-tryptophan 7-dimethylallyltransferase. This enzyme catalyses the following chemical reaction : dimethylallyl diphosphate + L-tryptophan \rightleftharpoons diphosphate + 7-(3-methylbut-2-enyl)-L-tryptophan This enzyme is more flexible towards the aromatic substrate than EC 2.5.1.34 (4-dimethylallyltryptophan synthase).
4-nitrocatechol 4-monooxygenase () is an enzyme with systematic name 4-nitrocatechol,NAD(P)H:oxygen 4-oxidoreductase (4-hydroxylating, nitrite- forming). This enzyme catalyses the following chemical reaction : 4-nitrocatechol + NAD(P)H + H+ \+ O2 \rightleftharpoons 2-hydroxy-1,4-benzoquinone + nitrite + NAD(P)+ + H2O 4-nitrocatechol 4-monooxygenase contains FAD.
Macrophage elastase (, metalloelastase, human macrophage metalloelastase (HME), MMP-12) is an enzyme. This enzyme catalyses the following chemical reaction : Hydrolysis of soluble and insoluble elastin. Specific cleavages are also produced at -Ala14-Leu- and -Tyr16-Leu- in the B chain of insulin This enzyme belongs to the peptidase family M10.
1,8-Cineole 2-exo-monooxygenase (, CYP3A4) is an enzyme with systematic name 1,8-cineole,NADPH:oxygen oxidoreductase (2-exo-hydroxylating). This enzyme catalyses the following chemical reaction : 1,8-cineole + NADPH + H+ \+ O2 \rightleftharpoons 2-exo-hydroxy-1,8-cineole + NADP+ \+ H2O 1,8-Cineole 2-exo- monooxygenase is a heme-thiolate protein (P-450).
Lupan-3beta,20-diol synthase (, LUP1 (gene)) is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualene hydro-lyase (lupan-3beta,20-diol forming). This enzyme catalyses the following chemical reaction : lupan-3beta,20-diol \rightleftharpoons (3S)-2,3-epoxy-2,3-dihydrosqualene + H2O The reaction occurs in the reverse direction.
N-succinylornithine carbamoyltransferase (, succinylornithine transcarbamylase, N-succinyl-L-ornithine transcarbamylase, SOTCase) is an enzyme with systematic name carbamoyl phosphate:N2-succinyl-L-ornithine carbamoyltransferase. This enzyme catalyses the following chemical reaction : carbamoyl phosphate + N2-succinyl-L-ornithine \rightleftharpoons phosphate + N-succinyl-L-citrulline This enzyme is specific for N-succinyl-L-ornithine.
5-epi-alpha-selinene synthase (, 8a-epi-alpha-selinene synthase, NP1) is an enzyme with systematic name (2Z,6E)-farnesyl-diphosphate diphosphate-lyase (cyclizing, 5-epi-alpha-selinene-forming). This enzyme catalyses the following chemical reaction : (2E,6E)-farnesyl diphosphate \rightleftharpoons 5-epi- alpha-selinene + diphosphate This enzyme requires Mg2+.
2-deoxy-scyllo-inosose synthase (, btrC (gene), neoC (gene), kanC (gene)) is an enzyme with systematic name D-glucose-6-phosphate phosphate-lyase (2-deoxy- scyllo-inosose-forming). This enzyme catalyses the following chemical reaction : D-glucose 6-phosphate \rightleftharpoons 2-deoxy-L-scyllo-inosose + phosphate This enzyme requires Co2+.
Alpha-isocomene synthase (, MrTPS2) is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate diphosphate-lyase (cyclizing, (-)-alpha- isocomene-forming). This enzyme catalyses the following chemical reaction : (2E,6E)-farnesyl diphosphate \rightleftharpoons (-)-alpha-isocomene + diphosphate This enzyme is isolated from the roots of the plant Matricaria chamomilla var. recutita (chamomile).
Valerena-4,7(11)-diene synthase (, VoTPS2) is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate diphosphate-lyase (cyclizing, valerena-4,7(11)-diene-forming). This enzyme catalyses the following chemical reaction : (2E,6E)-farnesyl diphosphate \rightleftharpoons valerena-4,7(11)-diene + diphosphate This enzyme is isolated from the plant Valeriana officinalis (valerian).
7-epi-sesquithujene synthase (, TPS4-B73) is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate diphosphate-lyase (7-epi-sesquithujene-forming). This enzyme catalyses the following chemical reaction : (2E,6E)-farnesyl diphosphate \rightleftharpoons 7-epi-sesquithujene + diphosphate The enzyme from Zea mays, variety B73, gives mainly 7-epi-sesquithujene.
Ent-isokaurene synthase (, OsKSL5i, OsKSL6) is an enzyme with systematic name ent-copalyl-diphosphate diphosphate-lyase (cyclizing, ent-isokaurene-forming). This enzyme catalyses the following chemical reaction : ent-copalyl diphosphate \rightleftharpoons ent-isokaurene + diphosphate Two enzymes of the rice sub-species Oryza sativa ssp. indica, OsKSL5 and OsKSL6, produce ent- isokaurene.
Gamma-terpinene synthase (, OvTPS2, ClcTS) is an enzyme with systematic name geranyl-diphosphate diphosphate-lyase (cyclizing, gamma-terpinene-forming). This enzyme catalyses the following chemical reaction : geranyl diphosphate \rightleftharpoons gamma-terpinene + diphosphate This enzyme is isolated from Thymus vulgaris (thyme), Citrus limon (lemon), Citrus unshiu (satsuma) and Origanum vulgare (oregano).
6-hydroxyneomycin C oxidase (, neoG (gene)) is an enzyme with systematic name 6-deamino-6-hydroxyneomycin C:oxygen 6-oxidoreductase. This enzyme catalyses the following chemical reaction : 6-deamino-6-hydroxyneomycin C + O2 \rightleftharpoons 6-deamino-6-oxoneomycin C + H2O2 This enzyme participates in biosynthesis of aminoglycoside antibiotics of the neomycin family.
Alpha-amyrin synthase (, 2,3-oxidosqualene alpha-amyrin cyclase, mixed amyrin synthase) is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualene mutase (cyclizing, alpha-amyrin-forming). This enzyme catalyses the following chemical reaction : (3S)-2,3-epoxy-2,3-dihydrosqualene \rightleftharpoons alpha-amyrin This multifunctional enzyme produces both alpha- and beta-amyrin.
Tirucalladienol synthase (, PEN3) is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualene mutase (cyclizing, tirucalla-7,24-dien-3beta-ol-forming). This enzyme catalyses the following chemical reaction : (3S)-2,3-epoxy-2,3-dihydrosqualene \rightleftharpoons tirucalla-7,24-dien-3beta-ol The product from Arabidopsis thaliana is tirucalla-7,24-dien-3beta-ol.
2-deoxy-scyllo-inosamine dehydrogenase (, (gene name), kanK (gene name)) is an enzyme with systematic name 2-deoxy-scyllo-inosamine:NAD(P)+ 1-oxidoreductase. This enzyme catalyses the following chemical reaction : 2-deoxy-scyllo- inosamine + NAD(P)+ \rightleftharpoons 3-amino-2,3-dideoxy-scyllo-inosose + NAD(P)H + H+ This enzyme requires zinc.
TRNA pseudouridine13 synthase (, TruD, YgbO, tRNA PSI13 synthase, RNA:PSI- synthase Pus7p, Pus7p, RNA:pseudouridine-synthase Pus7p, Pus7 protein) is an enzyme with systematic name tRNA-uridine13 uracil mutase. This enzyme catalyses the following chemical reaction : tRNA uridine13 \rightleftharpoons tRNA pseudouridine13 Pseudouridine synthase TruD from Escherichia coli specifically acts on uridine13 in tRNA.
Presqualene diphosphate synthase (, SSL-1 (gene)) is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate:(2E,6E)-farnesyl-diphosphate farnesyltransferase (presqualene diphosphate forming). This enzyme catalyses the following chemical reaction : 2 (2E,6E)-farnesyl diphosphate \rightleftharpoons presqualene diphosphate + diphosphate This enzyme is isolated from the green alga Botryococcus braunii BOT22.
He later catalyses Junko's reawakening, per her pre-experiment orders. He is killed in a fit of despair by Ryoko after she regains her memories and his body is mutilated post-mortem. ; :The . He assists Ryoko in investigating the murders of the Hope's Peak Academy School Board members in Danganronpa/Zero.
2'-Deamino-2'-hydroxyneamine transaminase (, kacL (gene)) is an enzyme with systematic name 2'-deamino-2'-hydroxyneamine:2-oxoglutarate aminotransferase. This enzyme catalyses the following chemical reaction : 2'-deamino-2'-hydroxyneamine + 2-oxoglutarate \rightleftharpoons 2'-deamino-2'-hydroxy-6'-dehydroparomamine + L-glutamate The reaction occurs in vivo in the opposite direction.
TRNA1Val (adenine37-N6)-methyltransferase (, YfiC) is an enzyme with systematic name S-adenosyl-L-methionine:tRNA1Val (adenine37-N6)-methyltransferase. This enzyme catalyses the following chemical reaction : S-adenosyl-L-methionine + adenine37 in tRNA1Val \rightleftharpoons S-adenosyl-L-homocysteine + N6-methyladenine37 in tRNA1Val The enzyme specifically methylates adenine37 in tRNA1Val (anticodon cmo5UAC).
Mycinamicin III 3-O-methyltransferase (, MycF) is an enzyme with systematic name S-adenosyl-L-methionine:mycinamicin III 3-O-methyltransferase. This enzyme catalyses the following chemical reaction : S-adenosyl-L-methionine + mycinamicin III \rightleftharpoons S-adenosyl-L-homocysteine + mycinamicin IV The enzyme is involved in the biosynthesis of mycinamicin macrolide antibiotics.
Aliphatic (R)-hydroxynitrile lyase (, (R)-HNL, (R)-oxynitrilase, (R)-hydroxynitrile lyase, LuHNL) is an enzyme with systematic name (2R)-2-hydroxy-2-methylbutanenitrile butan-2-one-lyase (cyanide forming). This enzyme catalyses the following chemical reaction : (2R)-2-hydroxy-2-methylbutanenitrile \rightleftharpoons cyanide + butan-2-one The enzyme contains Zn2+.
Mycinamicin VI 2-O-methyltransferase (, MycE) is an enzyme with systematic name S-adenosyl-L-methionine:mycinamicin VI 2-O-methyltransferase. This enzyme catalyses the following chemical reaction: : S-adenosyl-L-methionine + mycinamicin VI \rightleftharpoons S-adenosyl-L-homocysteine + mycinamicin III The enzyme is involved in the biosynthesis of mycinamicin macrolide antibiotics.
Methylamine-corrinoid protein Co-methyltransferase (, mtmB (gene), monomethylamine methyltransferase) is an enzyme with systematic name monomethylamine:5-hydroxybenzimidazolylcobamide Co-methyltransferase. This enzyme catalyses the following chemical reaction : methylamine + [Co(I) methylamine-specific corrinoid protein] \rightleftharpoons [methyl-Co(III) methylamine-specific corrinoid protein] + ammonia This enzyme is involved in methanogenesis from methylamine.
Dimethylamine-corrinoid protein Co-methyltransferase (, mtbB (gene), dimethylamine methyltransferase) is an enzyme with systematic name dimethylamine:5-hydroxybenzimidazolylcobamide Co-methyltransferase. This enzyme catalyses the following chemical reaction : dimethylamine + [Co(I) dimethylamine-specific corrinoid protein] \rightleftharpoons [methyl-Co(III) dimethylamine-specific corrinoid protein] + methylamine This enzyme is involved in methanogenesis from dimethylamine.
Trimethylamine-corrinoid protein Co-methyltransferase (, mttB (gene), trimethylamine methyltransferase) is an enzyme with systematic name trimethylamine:5-hydroxybenzimidazolylcobamide Co-methyltransferase. This enzyme catalyses the following chemical reaction : trimethylamine + [Co(I) trimethylamine-specific corrinoid protein] \rightleftharpoons [methyl-Co(III) trimethylamine-specific corrinoid protein] + dimethylamine This enzyme is involved in methanogenesis from trimethylamine.
Tetramethylammonium-corrinoid protein Co-methyltransferase (, mtqB (gene), tetramethylammonium methyltransferase) is an enzyme with systematic name tetramethylammonium:5-hydroxybenzimidazolylcobamide Co-methyltransferase. This enzyme catalyses the following chemical reaction : tetramethylammonium + [Co(I) tetramethylammonium-specific corrinoid protein] \rightleftharpoons [methyl-Co(III) tetramethylammonium-specific corrinoid protein] + trimethylamine This enzyme is involved in methanogenesis from tetramethylammonium.
Undecaprenyl-phosphate glucose phosphotransferase (, GumD, undecaprenylphosphate glucosylphosphate transferase) is an enzyme with systematic name UDP-glucose:ditrans,octacis-undecaprenyl-phosphate glucose phosphotransferase. This enzyme catalyses the following chemical reaction : UDP-glucose + ditrans, octacis-undecaprenyl phosphate \rightleftharpoons UMP + alpha-D-glucopyranosyl-diphospho-ditrans, octacis-undecaprenol The enzyme is involved in biosynthesis of xanthan.
This example illustrates a 6-enolendo aldolization. In the , proline catalyses an asymmetric aldol reaction. The zwitterionic character and the H-bonding of proline in the transition state determine the reaction outcome. An enamine is formed during the reaction and only one proline molecule is involved in forming the transition state.
Peptidyl-dipeptidase B (, dipeptidyl carboxyhydrolase, atriopeptin convertase, atrial di-(tri)peptidyl carboxyhydrolase, peptidyldipeptidase B, atrial dipeptidyl carboxyhydrolase, atrial peptide convertase) is an enzyme. It catalyses the following chemical reaction : Release of a C-terminal dipeptide or exceptionally a tripeptide This membrane-bound, zinc metallopeptidase is located in mammalian atrial myocytes.
Serratia marcescens nuclease (, endonuclease (Serratia marcescens), barley nuclease, plant nuclease I, nucleate endonuclease) is an enzyme. This enzyme catalyses the following chemical reaction : Endonucleolytic cleavage to 5'-phosphomononucleotide and 5'-phosphooligonucleotide end-products Hydrolyses double- or single-stranded substrate. It is a representative of the DNA/RNA non-specific endonuclease family.
Beta-D-fucosidase (, beta-fucosidase) is an enzyme with systematic name beta- D-fucoside fucohydrolase. This enzyme catalyses the following chemical reaction : Hydrolysis of terminal non-reducing beta-D-fucose residues in beta- D-fucosides Enzymes from some sources also hydrolyse beta-D-galactosides, beta-D-glucosides and alpha-L-arabinosides.
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.
Anthranilate phosphoribosyltransferase (AnPRT) is a transferase enzyme which catalyses one of the most fundamental biochemical reactions: the transfer of a ribose group between an aromatic base and phosphate groups. More specifically, AnPRT facilitates the formation of a carbon-nitrogen bond between 5-phospho-alpha-D- ribose 1-diphosphate (PRPP) and anthranilate.
Benzil is a standard building block in organic synthesis. It condenses with amines to give diketimine ligands. A classic organic reaction of benzil is the benzilic acid rearrangement, in which base catalyses the conversion of benzil to benzilic acid. This reactivity is exploited in the preparation of the drug phenytoin.
Gly-Xaa carboxypeptidase (, glycine carboxypeptidase, carboxypeptidase a, carboxypeptidase S, peptidase alpha, yeast carboxypeptidase) is an enzyme. This enzyme catalyses the following chemical reaction : Release of a C-terminal amino acid from a peptide in which glycine is the penultimate amino acid, e.g. Z-Gly!Leu This enzyme is isolated from yeast.
Venombin AB (, gabonase, okinaxobin II, Bitis gabonica venom serine proteinase, afaâ, cytin) is an enzyme. This enzyme catalyses the following chemical reaction : Selective cleavage at Arg- bonds in fibrinogen to form fibrin and release fibrinopeptides A and B This enzyme is isolated from the venom of the Gaboon viper Bitis gabonica.
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.
Rhizopuspepsin (, Rhizopus aspartic proteinase, neurase, Rhizopus acid protease, Rhizopus acid proteinase) is an enzyme. This enzyme catalyses the following chemical reaction : Hydrolysis of proteins with broad specificity similar to that of pepsin A, preferring hydrophobic residues at P1 and P1'. Clots milk and activates trypsinogen. From the zygomycete fungus Rhizopus chinensis.
A dihydropteroate synthase inhibitor is a drug that inhibits the action of dihydropteroate synthase. Most are sulfonamides. Tetrahydrofolate synthesis pathway In bacteria, antibacterial sulfonamides act as competitive inhibitors of the enzyme dihydropteroate synthase, DHPS. DHPS catalyses the conversion of PABA (para-aminobenzoate) to dihydropteroate, a key step in folate synthesis.
Dimethylglycine N-methyltransferase (, BsmB, DMT) is an enzyme with systematic name S-adenosyl-L-methionine:N,N-dimethylglycine N-methyltransferase (betaine- forming). This enzyme catalyses the following chemical reaction : S-adenosyl- L-methionine + N,N-dimethylglycine \rightleftharpoons S-adenosyl-L- homocysteine + betaine This enzyme is purified from the marine cyanobacterium Synechococcus sp. WH8102.
Phosphinothricin acetyltransferase (, PAT, PPT acetyltransferase, Pt-N- acetyltransferase, ac-Pt) is an enzyme with systematic name acetyl- CoA:phosphinothricin N-acetyltransferase. This enzyme catalyses the following chemical reaction : acetyl-CoA + phosphinothricin \rightleftharpoons CoA + N-acetylphosphinothricin The substrate phosphinothricin is used as a nonselective herbicide and is a potent inhibitor of EC 6.3.1.2. Reaction.
Beta-ketodecanoyl-(acyl-carrier-protein) synthase () is an enzyme with systematic name octanoyl-CoA:malonyl-(acyl-carrier protein) C-heptanoylltransferase (decarboxylating, CoA-forming). This enzyme catalyses the following chemical reaction : octanoyl-CoA + malonyl-[acyl-carrier protein] \rightleftharpoons 3-oxodecanoyl-[acyl-carrier protein] + CoA + CO2 This enzyme is purified from the bacterium Pseudomonas aeruginosa PAO1.
S-methyl-5'-thioadenosine deaminase (, MTA deaminase, 5-methylthioadenosine deaminase) is an enzyme with systematic name S-methyl-5'-thioadenosine amidohydrolase. This enzyme catalyses the following chemical reaction : S-methyl-5'-thioadenosine + H2O \rightleftharpoons 5'-S-methyl-5'-thioinosine + NH3 The enzyme from Thermotoga maritima also functions as S-adenosylhomocysteine deaminase (EC 3.5.4.28).
Fibrolase (, fibrinolytic proteinase, Agkistrodon contortrix contortrix metalloproteinase, Agkistrodon contortrix contortrix venom metalloproteinase) is an enzyme. This enzyme catalyses the following chemical reaction : Hydrolysis of -Ala14-Leu- in insulin B chain and -Lys413-Leu- in alpha-chain of fibrinogen This enzyme is present in the venom of the southern copperhead snake (Agkistrodon contortrix contortrix).
Sulfoacetaldehyde dehydrogenase (, SafD) is an enzyme with systematic name 2-sulfoacetaldehyde:NAD+ oxidoreductase. This enzyme catalyses the following chemical reaction : 2-sulfoacetaldehyde + H2O + NAD+ \rightleftharpoons sulfoacetate + NADH + 2 H+ This reaction is part of a bacterial pathway that can make use the amino group of taurine as a sole source of nitrogen for growth.
Pyruvate dehydrogenase (quinone) (, pyruvate dehydrogenase, pyruvic dehydrogenase, pyruvic (cytochrome b1) dehydrogenase, pyruvate:ubiquinone-8-oxidoreductase, pyruvate oxidase (ambiguous)) is an enzyme with systematic name pyruvate:ubiquinone oxidoreductase. This enzyme catalyses the following chemical reaction : pyruvate + ubiquinone + H2O \rightleftharpoons acetate + CO2 \+ ubiquinol This bacterial enzyme is located on the inner surface of the cytoplasmic membrane.
2,6-dihydroxypseudooxynicotine hydrolase () is an enzyme with systematic name 1-(2,6-dihydroxypyridin-3-yl)-4-(methylamino)butan-1-one hydrolase. This enzyme catalyses the following chemical reaction : 1-(2,6-dihydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O \rightleftharpoons 2,6-dihydroxypyridine + 4-methylaminobutanoate The enzyme is present in the soil bacterium Arthrobacter nicotinovorans.
It also interacts with the C-terminal region of the E1-like atg7 enzyme. Autophagocytosis is a starvation-induced process responsible for transport of cytoplasmic proteins to the lysosome/vacuole. Atg3 is a ubiquitin like modifier that is topologically similar to the canonical E2 enzyme. It catalyses the conjugation of Atg8 and phosphatidylethanolamine.
1-deoxypentalenic acid 11beta-hydroxylase (, PTLH (gene), SAV2991 (gene), PNTH (gene)) is an enzyme with systematic name 1-deoxypentalenic acid,2-oxoglutarate:oxygen oxidoreductase. This enzyme catalyses the following chemical reaction : 1-deoxypentalenate + 2-oxoglutarate + O2 \rightleftharpoons 1-deoxy-11beta-hydroxypentalenate + succinate + CO2 1-Deoxypentalenic acid 11beta-hydroxylase contains Fe(II) and ascorbate.
Mannosylglycerate synthase () is an enzyme with systematic name GDP- mannose:D-glycerate 2-alpha-D-mannosyltransferase. This enzyme catalyses the following chemical reaction : GDP-mannose + D-glycerate \rightleftharpoons GDP + 2-O-(alpha-D-mannopyranosyl)-D-glycerate Depending on conditions mannosylglycerate synthase is more or less specific for the GDP-mannose and D-glycerate.
Nigerose phosphorylase (, cphy1874 (gene)) is an enzyme with systematic name 3-O-alpha-D-glucopyranosyl-D-glucopyranose:phosphate beta-D- glucosyltransferase. This enzyme catalyses the following chemical reaction : 3-O-alpha-D-glucopyranosyl-D-glucopyranose + phosphate \rightleftharpoons D-glucose + beta-D-glucose 1-phosphate The enzymes from Clostridium phytofermentans is specific for nigerose.
2-deoxystreptamine glucosyltransferase (, kanF (gene)) is an enzyme with systematic name UDP-alpha-D-glucose:2-deoxystreptamine 6-alpha-D- glucosyltransferase. This enzyme catalyses the following chemical reaction : UDP-alpha-D-glucose + 2-deoxystreptamine \rightleftharpoons UDP + 2'-deamino-2'-hydroxyparomamine This enzyme is involved in the biosynthesis of kanamycin B and kanamycin C.
Pycnoporopepsin (, proteinase Ia, Pycnoporus coccineus aspartic proteinase, Trametes acid proteinase) is an enzyme. This enzyme catalyses the following chemical reaction : Similar to pepsin A, but narrower, cleaving only three bonds in the B chain of insulin: Ala14-Leu, Tyr16-Leu, and Phe24-Phe This enzyme is isolated from the basidiomycete Pycnoporus sanguineus.
Nodavirus endopeptidase (, Black Beetle virus endopeptidase, Flock House virus endopeptidase) is an enzyme. This enzyme catalyses the following chemical reaction : Hydrolysis of an asparaginyl bond involved in the maturation of the structural protein of the virus, typically -Asn-Ala- or -Asn-Phe- The enzyme is coded by several nodaviruses that are insect pathogens.
7-Hydroxymethyl chlorophyll a reductase (, HCAR) is an enzyme with systematic name 71-hydroxychlorophyll a:ferredoxin oxidoreductase. This enzyme catalyses the following chemical reaction : 71-hydroxychlorophyll a + 2 reduced ferredoxin + 2 H+ \rightleftharpoons chlorophyll a + 2 oxidized ferredoxin + H2O 7-Hydroxymethyl chlorophyll is a reductase that contains FAD and an iron- sulfur center.
Costunolide synthase () is an enzyme with systematic name germacra-1(10),4,11(13)-trien-12-oate,NADPH:oxygen oxidoreductase (6alpha- hydroxylating). This enzyme catalyses the following chemical reaction : germacra-1(10),4,11(13)-trien-12-oate + NADPH + H+ \+ O2 \rightleftharpoons (+)-costunolide + NADP+ \+ 2 H2O Costunolide synthase is a heme-thiolate protein (P-450).
Zeaxanthin 7,8-dioxygenase (, zeaxanthin 7,8(7',8')-cleavage dioxygenase, CsZCD) is an enzyme with systematic name zeaxanthin:oxygen oxidoreductase (7,8-cleaving). This enzyme catalyses the following chemical reaction : zeaxanthin + 2 O2 \rightleftharpoons crocetin dialdehyde + 2 (3S)-3-hydroxycyclocitral Zeaxanthin 7,8-dioxygenase acts twice on zeaxanthin cleaving 3-hydroxycyclocitral off each 3-hydroxy end group.
Thermospermine synthase (, TSPMS, ACL5 (ACAULIS5), SAC51) is an enzyme with systematic name S-adenosylmethioninamine:spermidine 3-aminopropyltransferase (thermospermine synthesizing). This enzyme catalyses the following chemical reaction : S-adenosylmethioninamine + spermidine \rightleftharpoons S-methyl-5'-thioadenosine + thermospermine + H+ This enzyme is required for correct xylem specification through regulation of the lifetime of the xylem elements.
Leachianone-G 2-dimethylallyltransferase (, LG 2-dimethylallyltransferase, leachianone G 2-dimethylallyltransferase, LGDT) is an enzyme with systematic name dimethylallyl-diphosphate:leachianone-G 2-dimethylallyltransferase. This enzyme catalyses the following chemical reaction: : dimethylallyl diphosphate + leachianone G \rightleftharpoons diphosphate + sophoraflavanone G This membrane-bound enzyme is located in the plastids and requires Mg2+ for activity.
Indole-3-pyruvate monooxygenase (, YUC2 (gene), spi1 (gene)) is an enzyme with systematic name indole-3-pyruvate,NADPH:oxygen oxidoreductase (1-hydroxylating, decarboxylating). This enzyme catalyses the following chemical reaction : (indol-3-yl)pyruvate + NADPH + H+ \+ O2 \rightleftharpoons (indol-3-yl)acetate + NADP+ \+ H2O + CO2 Indole-3-pyruvate monooxygenase is a plant enzyme.
Sphinganine C4-monooxygenase (, sphingolipid C4-hydroxylase, SUR2 (gene), SBH1 (gene), SBH2 (gene)) is an enzyme with systematic name sphinganine,NADPH:oxygen oxidoreductase (C4-hydroxylating). This enzyme catalyses the following chemical reaction : sphinganine + NADPH + H+ \+ O2 \rightleftharpoons phytosphingosine + NADP+ \+ H2O Sphinganine C4-monooxygenase is involved in the biosynthesis of sphingolipids in yeast and plants.
Vitamin D3 24-hydroxylase (, CYP24A1) is an enzyme with systematic name calcitriol,NADPH:oxygen oxidoreductase (24-hydroxylating). This enzyme catalyses the following chemical reaction : (1) calcitriol + NADPH + H+ \+ O2 \rightleftharpoons calcitetrol + NADP+ \+ H2O : (2) calcidiol + NADPH + H+ \+ O2 \rightleftharpoons secalciferol + NADP+ \+ H2O Vitamin D3 24-hydroxylase is a heme-thiolate enzyme (P-450).
2-hydroxyisoflavanone synthase (, CYT93C, IFS, isoflavonoid synthase) is an enzyme with systematic name liquiritigenin,NADPH:oxygen oxidoreductase (hydroxylating, aryl migration). This enzyme catalyses the following chemical reactions: : liquiritigenin + O2 \+ NADPH + H+ \rightleftharpoons 2,4',7-trihydroxyisoflavanone + H2O + NADP+ and : (2S)-naringenin + O2 \+ NADPH + H+ \rightleftharpoons 2,4',5,7-tetrahydroxyisoflavanone + H2O + NADP+ Isoflavonoid synthase requires cytochrome P450.
2-iminoacetate synthase (, thiH (gene)) is an enzyme with systematic name L-tyrosine 4-methylphenol-lyase (2-iminoacetate-forming). This enzyme catalyses the following chemical reaction : L-tyrosine + S-adenosyl-L- methionine + reduced acceptor \rightleftharpoons 2-iminoacetate + 4-methylphenol + 5'-deoxyadenosine + L-methionine + acceptor + 2 H+ This enzyme binds a 4Fe-4S cluster.
Syn-pimara-7,15-diene synthase (, 9beta-pimara-7,15-diene synthase, OsDTS2, OsKS4) is an enzyme with systematic name 9alpha-copalyl-diphosphate diphosphate-lyase (9beta-pimara-7,15-diene-forming). This enzyme catalyses the following chemical reaction : 9alpha-copalyl diphosphate \rightleftharpoons 9beta-pimara-7,15-diene + diphosphate This enzyme is a class I terpene synthase.
Alpha-eudesmol synthase () is an enzyme with systematic name (2E,6E)-farnesyl- diphosphate diphosphate-lyase (alpha-eudesmol-forming). This enzyme catalyses the following chemical reaction : (2E,6E)-farnesyl diphosphate + H2O \rightleftharpoons alpha-eudesmol + diphosphate The recombinant enzyme from ginger (Zingiber zerumbet) gives beta-eudesmol, 10-epi-gamma-eudesmol, alpha- eudesmol and aristolene.
7-epi-alpha-selinene synthase () is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate diphosphate-lyase (7-epi-alpha-selinene-forming). This enzyme catalyses the following chemical reaction : (2E,6E)-farnesyl diphosphate \rightleftharpoons 7-epi-alpha-selinene + diphosphate The recombinant enzyme from Vitis vinifera forms (+)-valencene and (-)-7-epi- alpha-selinene.
Beta-eudesmol synthase () is an enzyme with systematic name (2E,6E)-farnesyl- diphosphate diphosphate-lyase (beta-eudesmol-forming). This enzyme catalyses the following chemical reaction : (2E,6E)-farnesyl diphosphate + H2O \rightleftharpoons beta-eudesmol + diphosphate The recombinant enzyme from ginger (Zingiber zerumbet) gives beta-eudesmol, 10-epi-gamma-eudesmol, alpha- eudesmol and aristolene.
Diacetyl reductase ((R)-acetoin forming) (, (R)-acetoin dehydrogenase) is an enzyme with systematic name (R)-acetoin:NAD+ oxidoreductase. This enzyme catalyses the following chemical reaction : (R)-acetoin + NAD+ \rightleftharpoons diacetyl + NADH + H+ The reaction is catalysed in the reverse direction. This activity is usually associated with butanediol dehydrogenase activity (EC 1.1.1.4 or EC 1.1.1.76).
Diacetyl reductase ((S)-acetoin forming) (, (S)-acetoin dehydrogenase) is an enzyme with systematic name (S)-acetoin:NAD+ oxidoreductase. This enzyme catalyses the following chemical reaction : (S)-acetoin + NAD+ \rightleftharpoons diacetyl + NADH + H+ The reaction is catalysed in the reverse direction. This activity is usually associated with butanediol dehydrogenase activity (EC 1.1.1.4 or EC 1.1.1.76).
Beta-phellandrene synthase (neryl-diphosphate-cyclizing) (, phellandrene synthase 1, PHS1, monoterpene synthase PHS1) is an enzyme with systematic name neryl-diphosphate diphosphate-lyase (cyclizing; beta-phellandrene-forming). This enzyme catalyses the following chemical reaction : neryl diphosphate \rightleftharpoons beta-phellandrene + diphosphate The enzyme from Solanum lycopersicum has very poor affinity with geranyl diphosphate.
Alcohol dehydrogenase (cytochrome c) (, type I quinoprotein alcohol dehydrogenase, quinoprotein ethanol dehydrogenase) is an enzyme with systematic name alcohol:cytochrome c oxidoreductase. This enzyme catalyses the following chemical reaction : a primary alcohol + 2 ferricytochrome c \rightleftharpoons an aldehyde + 2 ferrocytochrome c + 2 H+ A periplasmic PQQ- containing quinoprotein is present in Pseudomonas and Rhodopseudomonas.
Mitochondrial tRNA pseudouridine27/28 synthase (, Pus2, Pus2p, RNA:pseudouridine synthases 2) is an enzyme with systematic name mitochondrial tRNA-uridine27/28 uracil mutase. This enzyme catalyses the following chemical reaction : mitochondrial tRNA uridine27/28 \rightleftharpoons mitochondrial tRNA pseudouridine27/28 The mitochondrial enzyme Pus2p is specific for position 27 or 28 in mitochondrial tRNA.
N-acetylneuraminate epimerase (, sialic acid epimerase, N-acetylneuraminate mutarotase, sialic acid mutarotase, YjhT, NanM) is an enzyme with systematic name N-acetyl-alpha-neuraminate 2-epimerase. This enzyme catalyses the following chemical reaction : N-acetyl-alpha-neuraminate \rightleftharpoons N-acetyl-beta-neuraminate Sialoglycoconjugates present in vertebrates are linked exclusively by alpha-linkages.
Halimadienyl-diphosphate synthase (, Rv3377c, halimadienyl diphosphate synthase, tuberculosinol diphosphate synthase, halima-5(6),13-dien-15-yl- diphosphate lyase (cyclizing)) is an enzyme with systematic name halima-5,13-dien-15-yl-diphosphate lyase (decyclizing). This enzyme catalyses the following chemical reaction : geranylgeranyl diphosphate \rightleftharpoons tuberculosinyl diphosphate This enzyme requires Mg2+ for activity.
Lycopene beta-cyclase (, CrtL, CrtL-b, CrtY) is an enzyme with systematic name carotenoid beta-end group lyase (decyclizing). This enzyme catalyses the following chemical reaction : carotenoid psi-end group \rightleftharpoons carotenoid beta-end group This enzyme requires NAD(P)H. It converts Lycopene (2 psi ends) into Beta-Carotene (2 beta ends).
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.
Archaeosine synthase (, ArcS, TgtA2, MJ1022 (gene), glutamine:preQ0-tRNA amidinotransferase) is an enzyme with systematic name L-glutamine:7-cyano-7-carbaguanine aminotransferase. This enzyme catalyses the following chemical reaction : L-glutamine + 7-cyano-7-carbaguanine15 in tRNA + H2O \rightleftharpoons L-glutamate + archaeine15 in tRNA In Euryarchaeota the reaction is catalysed by ArcS.
Formate dehydrogenase (acceptor) (, FDHH, FDH-H, FDH-O, formate dehydrogenase H, formate dehydrogenase O) is an enzyme with systematic name formate:acceptor oxidoreductase. This enzyme catalyses the following chemical reaction : formate + acceptor \rightleftharpoons CO2 \+ reduced acceptor Formate dehydrogenase H is a cytoplasmic enzyme that oxidizes formate without oxygen transfer] transferring electrons to a hydrogenase.
Nicotinate riboside kinase (, ribosylnicotinic acid kinase, nicotinic acid riboside kinase, NRK1) is an enzyme with systematic name ATP:beta-D- ribosylnicotinate 5-phosphotransferase. This enzyme catalyses the following chemical reaction : ATP + beta-D-ribosylnicotinate \rightleftharpoons ADP + nicotinate beta-D-ribonucleotide The enzyme from yeast and human also acts as EC 2.7.1.22 (ribosylnicotinamide kinase).
Diacylglycerol kinase (CTP dependent) (, DAG kinase, CTP-dependent diacylglycerol kinase, diglyceride kinase) is an enzyme with systematic name CTP:1,2-diacyl-sn-glycerol 3-phosphotransferase. This enzyme catalyses the following chemical reaction : CTP + 1,2-diacyl-sn-glycerol \rightleftharpoons CDP + 1,2-diacyl-sn-glycerol 3-phosphate This enzyme requires Ca2+ or Mg2+ for activity.
Propionyl-CoA carboxylase (PCC) catalyses the carboxylation reaction of propionyl CoA in the mitochondrial matrix. The enzyme is biotin-dependent. The product of the reaction is (S)-methylmalonyl CoA. Propionyl CoA is the end product of metabolism of odd-chain fatty acids, and is also a metabolite of most methyl-branched fatty acids.
TRNA (pseudouridine54-N1)-methyltransferase (, TrmY, m1Psi methyltransferase) is an enzyme with systematic name S-adenosyl-L-methionine:tRNA (pseudouridine54-N1)-methyltransferase. This enzyme catalyses the following chemical reaction : S-adenosyl-L-methionine + pseudouridine54 in tRNA \rightleftharpoons S-adenosyl-L-homocysteine + N1-methylpseudouridine54 in tRNA This archaeal enzyme is specific for the 54 position.
TRNA (guanine6-N2)-methyltransferase (, methyltransferase Trm14, m2G6 methyltransferase) is an enzyme with systematic name S-adenosyl-L- methionine:tRNA (guanine6-N2)-methyltransferase. This enzyme catalyses the following chemical reaction : S-adenosyl-L-methionine + guanine6 in tRNA \rightleftharpoons S-adenosyl-L-homocysteine + N2-methylguanine6 in tRNA The enzyme specifically methylates guanine6 at N2 in tRNA.
Lipoate–protein ligase (, LplA, lipoate protein ligase, lipoate–protein ligase A, LPL, LPL-B) is an enzyme with systematic name ATP:lipoate adenylyltransferase. This enzyme catalyses the following chemical reaction : (1) ATP + lipoate \rightleftharpoons diphosphate + lipoyl-AMP : (2) lipoyl-AMP + apoprotein \rightleftharpoons protein N6-(lipoyl)lysine + AMP This enzyme requires Mg2+ as a cofactor.
GDP-D-glucose phosphorylase () is an enzyme with systematic name GDP:alpha-D- glucose 1-phosphate guanylyltransferase. This enzyme catalyses the following chemical reaction : GDP-alpha-D-glucose + phosphate \rightleftharpoons alpha- D-glucose 1-phosphate + GDP The enzyme may be involved in prevention of misincorporation of glucose in place of mannose residues into glycoconjugates.
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.
Carboxypeptidase U (, arginine carboxypeptidase, carboxypeptidase R, plasma carboxypeptidase B, thrombin-activatable fibrinolysis inhibitor) is an enzyme. This enzyme catalyses the following chemical reaction : Release of C-terminal Arg and Lys from a polypeptide Pro-carboxypeptidase U in (human) plasma is activated by thrombin or plasmin during clotting to form the unstable carboxypeptidase U.
Pimelyl-(acyl-carrier protein) methyl ester esterase (, BioH) is an enzyme with systematic name pimelyl-(acyl-carrier protein) methyl ester hydrolase. This enzyme catalyses the following chemical reaction : pimelyl-[acyl-carrier protein] methyl ester + H2O \rightleftharpoons pimelyl-[acyl-carrier protein] + methanol This enzyme takes part in biotin biosynthesis in Gram-negative bacteria.
The gene responsible for this disorder is DHODH located at chromosome 16q22. This gene encodes an enzyme – dihydroorotate dehydrogenase – which catalyses the ubiquinone-mediated oxidation of dihydroorotate to orotate, the fourth enzymatic step in de novo pyrimidine biosynthesis. The protein is normally located on the outer surface of the inner mitochondrial membrane.
Baicalin-beta-D-glucuronidase (, baicalinase) is an enzyme with systematic name 5,6,7-trihydroxyflavone-7-O-beta-D-glucupyranosiduronate glucuronosylhydrolase. This enzyme catalyses the following chemical reaction : baicalin + H2O \rightleftharpoons baicalein + D-glucuronate The enzyme also hydrolyses wogonin 7-O-beta-D-glucuronide and oroxylin 7-O-beta-D-glucuronide with lower efficiency.
Methionyl aminopeptidase (, methionine aminopeptidase, peptidase M, L-methionine aminopeptidase, MAP) is an enzyme. This enzyme catalyses the following chemical reaction : Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides This membrane-bound enzymatic activity is present in both prokaryotes and eukaryotes. Proteins possessing this activity include METAP1 and METAP2.
Pyruvate kinase type M2 or PKM2 is present in embryonic, adult stem cells. It is also expressed by many tumor cells. The alterations to metabolism by PKM2 increases ATP resources, stimulates macromolecular biosynthesis and redox control. Pyruvate kinase catalyses the ATP-generating step of glycolysis in which phosphoenolpyruvate (PEP) is converted to pyruvate.
7-cyano-7-deazaguanine synthase (, preQ0 synthase, 7-cyano-7-carbaguanine synthase, queC (gene)) is an enzyme with systematic name 7-carboxy-7-carbaguanine:ammonia ligase (ADP-forming). This enzyme catalyses the following chemical reaction : 7-carboxy-7-carbaguanine + NH3 \+ ATP \rightleftharpoons 7-cyano-7-carbaguanine + ADP + phosphate + H2O This enzyme binds Zn2+.
Nitrogenase (flavodoxin) () is an enzyme with systematic name reduced flavodoxin:dinitrogen oxidoreductase (ATP-hydrolysing). This enzyme catalyses the following chemical reaction : 6 reduced flavodoxin + 6 H+ \+ N2 \+ n ATP \rightleftharpoons 6 oxidized flavodoxin + 2 NH3 \+ n ADP + n phosphate The enzyme is a complex of two proteins containing iron-sulfur centres and molybdenum.
AKR1A1 is shown to demonstrate characteristically high specific activity towards many aromatic and aliphatic aldehydes, and preferentially catalyses the NADPH-dependent reduction of aliphatic aldehydes, aromatic aldehydes and biogenic amines. It is also reported to be involved in the metabolism of 4-hydroxynonenal and play a role in the resistance to oxidative stress.
Muramoyltetrapeptide carboxypeptidase (, carboxypeptidase IIW, carboxypeptidase II, lysyl-D-alanine carboxypeptidase, L-lysyl-D-alanine carboxypeptidase, LD-carboxypeptidase) is an enzyme. This enzyme catalyses the following chemical reaction : Hydrolysis of the bond: N-acetyl-D-glucosaminyl- N-acetylmuramoyl-L-Ala-D-glutamyl-6-carboxy-L-lysyl--D-alanine Variants are known from various microorganisms.
Togavirin (, Sindbis virus protease, Sindbis virus core protein, NsP2 proteinase) is an enzyme. This enzyme catalyses the following chemical reaction : Autocatalytic release of the core protein from the N-terminus of the togavirus structural polyprotein by hydrolysis of a -Trp-Ser- bond This enzyme is isolated from the Sindbis and Semliki forest togaviruses.
C5a peptidase (, streptococcal C5a peptidase, ScpA, ScpB, SCPA) is an enzyme. This enzyme catalyses the following chemical reaction : The primary cleavage site is at His67-Lys68 in human C5a with a minor secondary cleavage site at Ala58-Ser59 This enzyme is a surface-associated subtilisin-like serine peptidase with very specific substrate preference.
Cerevisin (, yeast proteinase B, proteinase yscB, baker's yeast proteinase B, brewer's yeast proteinase, peptidase beta) is an enzyme. This enzyme catalyses the following chemical reaction : Hydrolysis of proteins with broad specificity, and of Bz-Arg-OEt Ac-Tyr-OEt. Does not hydrolyse peptide amides This enzyme is isolated from Saccharomyces cerevisiae (baker's yeast).
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.
Tricetin 3',4',5'-O-trimethyltransferase (, FOMT, TaOMT1, TaCOMT1, TaOMT2) is an enzyme with systematic name S-adenosyl-L-methionine:tricetin 3',4',5'-O-trimethyltransferase. This enzyme catalyses the following chemical reaction : 3 S-adenosyl-L-methionine + tricetin \rightleftharpoons 3 S-adenosyl-L-homocysteine + 3',4',5'-O-trimethyltricetin (overall reaction) :(1a) S-adenosyl-L-methionine + tricetin \rightleftharpoons S-adenosyl-L- homocysteine + 3'-O-methyltricetin :(1b) S-adenosyl-L-methionine + 3'-O-methyltricetin \rightleftharpoons S-adenosyl-L-homocysteine + 3',5'-O-dimethyltricetin :(1c) S-adenosyl-L-methionine + 3',5'-O-dimethyltricetin \rightleftharpoons S-adenosyl-L-homocysteine + 3',4',5'-O-trimethyltricetin The enzyme from Triticum aestivum catalyses the sequential O-methylation of tricetin via 3'-O-methyltricetin, 3',5'-O-methyltricetin to 3',4',5'-O-trimethyltricetin.
Malonyl CoA reductase (malonate semialdehyde-forming) (, NADP-dependent malonyl CoA reductase, malonyl CoA reductase (NADP)) is an enzyme with systematic name malonate semialdehyde:NADP+ oxidoreductase (malonate semialdehyde-forming). This enzyme catalyse the following chemical reaction : malonate semialdehyde + CoA + NADP+ \rightleftharpoons malonyl-CoA + NADPH + H+ Requires Mg2+. Catalyses the reduction of malonyl-CoA to malonate semialdehyde.
Nitrate reductase (quinone) (, nitrate reductase A, nitrate reductase Z, quinol/nitrate oxidoreductase, quinol-nitrate oxidoreductase, quinol:nitrate oxidoreductase, NarA, NarZ, NarGHI) is an enzyme with systematic name nitrite:quinone oxidoreductase. This enzyme catalyses the following chemical reaction : nitrate + a quinol \rightleftharpoons nitrite + a quinone + H2O This is a membrane-bound enzyme which supports [anaerobic respiration] on nitrate.
Menaquinol oxidase (H+-transporting) (, cytochrome aa3-600 oxidase) is an enzyme with systematic name menaquinol:O2 oxidoreductase (H+-transporting). This enzyme catalyses the following chemical reaction : 2 menaquinol + O2 \rightleftharpoons 2 menaquinone + 2 H2O Cytochrome aa3-600, one of the respiratory oxidases from Bacillus subtilis, is a member of the heme-copper family of oxygen reductases.
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.
Tropine acyltransferase (, tropine:acyl-CoA transferase, acetyl- CoA:tropan-3-ol acyltransferase, tropine acetyltransferase, tropine tigloyltransferase, TAT) is an enzyme with systematic name acyl-CoA:tropine O-acyltransferase. This enzyme catalyses the following chemical reaction : acyl-CoA + tropine \rightleftharpoons CoA + O-acyltropine This enzyme exhibits absolute specificity for the endo/3alpha configuration found in tropine as pseudotropine.
O-sialoglycoprotein endopeptidase (, glycoprotease, glycophorin A proteinase, glycoproteinase, sialoglycoprotease, sialoglycoproteinase, "OSGE") is an enzyme. This enzyme catalyses the following chemical reaction : Hydrolysis of O-sialoglycoproteins; cleaves -Arg31-Asp- bond in glycophorin A. Does not cleave unglycosylated proteins, desialylated glycoproteins or glycoproteins that are only N-glycosylated This enzyme is secreted by the bacterium Pasteurella haemolytica.
Alcohol-forming fatty acyl-CoA reductase (, FAR (gene)) is an enzyme with systematic name long-chain acyl-CoA:NADPH reductase. This enzyme catalyses the following chemical reaction : a long-chain acyl-CoA + 2 NADPH + 2 H+ \rightleftharpoons a long-chain alcohol + 2 NADP+ \+ coenzyme A The enzyme has been characterized from the plant Simmondsia chinensis.
N8-acetylspermidine oxidase (propane-1,3-diamine-forming) () is an enzyme with systematic name N8-acetylspermidine:oxygen oxidoreductase (propane-1,3-diamine-forming). This enzyme catalyses the following chemical reaction : N8-acetylspermidine + O2 \+ H2O \rightleftharpoons propane-1,3-diamine + 4-acetamidobutanal + H2O2 This enzyme is also active n N1-acetylspermine, and it has weak activity on N1,N12-diacetylspermine.
Deoxyribonuclease IV (phage-T4-induced) (, endodeoxyribonuclease IV (phage T4-induced), E. coli endonuclease IV, endodeoxyribonuclease, redoxyendonuclease, deoxriboendonuclease, Escherichia coli endonuclease II, endonuclease II, DNA-adenine-transferase) is an enzyme. This enzyme catalyses the following chemical reaction : Endonucleolytic cleavage to 5'-phosphooligonucleotide end-products Deoxyribonuclease IV is a type of deoxyribonuclease that functions at AP-sites.
Glutathione amide-dependent peroxidase () is an enzyme with systematic name glutathione amide:hydrogen-peroxide oxidoreductase. This enzyme catalyses the following chemical reaction : 2 glutathione amide + H2O2 \rightleftharpoons glutathione amide disulfide + 2 H2O This enzyme from the proteobacterium Marichromatium gracile is a chimeric protein. It contains a peroxiredoxin-like N-terminus and a glutaredoxin-like C terminus.
Hydroquinone 1,2-dioxygenase (, hydroquinone dioxygenase) is an enzyme with systematic name benzene-1,4-diol:oxygen 1,2-oxidoreductase (decyclizing). This enzyme catalyses the following chemical reaction : benzene-1,4-diol + O2 \rightleftharpoons (2E,4Z)-4-hydroxy-6-oxohexa-2,4-dienoate The enzyme is an extradiol-type dioxygenase. It belongs to the nonheme-iron(II)-dependent dioxygenase family.
Carlactone synthase (, CCD8 (gene), MAX4 (gene), NCED8 (gene)) is an enzyme with systematic name 9-cis-10'-apo-beta-carotenal:O2 oxidoreductase (14,15-cleaving, carlactone-forming). This enzyme catalyses the following chemical reaction : 9-cis-10'-apo-beta-carotenal + 2 O2 \rightleftharpoons carlactone + (2E,4E,6E)-7-hydroxy-4-methylhepta-2,4,6-trienal Carlactone synthase contains Fe2+.
Carotenoid-9',10'-cleaving dioxygenase (, BCO2 (gene), beta-carotene 9',10'-monooxygenase (misleading)) is an enzyme with systematic name all- trans-beta-carotene:O2 oxidoreductase (9',10'-cleaving). This enzyme catalyses the following chemical reaction : all-trans-beta-carotene + O2 \rightleftharpoons all-trans-10'-apo-beta-carotenal + beta-ionone Carotenoid-9',10'-cleaving dioxygenase contains Fe2+.
Ascorbate ferrireductase (transmembrane) (, cytochrome b561) is an enzyme with systematic name Fe(III):ascorbate oxidorectuctase (electron-translocating). This enzyme catalyses the following chemical reaction center ascorbate[in] \+ Fe(III)[out] \rightleftharpoons monodehydroascorbate radical[in] \+ Fe(II)[out] \+ H+[in] Ascorbate ferrireductase is a diheme cytochrome that acts on hexacyanoferrate(III) and other ferric chelates.
Bile-acid 7alpha-dehydroxylase (, cholate 7alpha-dehydroxylase, 7alpha- dehydroxylase, bile acid 7-dehydroxylase) is an enzyme with systematic name deoxycholate:NAD+ oxidoreductase. This enzyme catalyses the following chemical reaction : (1) deoxycholate + NAD+ \+ H2O \rightleftharpoons cholate + NADH + H+ : (2) lithocholate + NAD+ \+ H2O \rightleftharpoons chenodeoxycholate + NADH + H+ Bile-acid 7alpha-dehydroxylase is highly specific for bile acid substrates.
This gene encodes a membrane-bound adenylyl cyclase that catalyses the formation of cyclic AMP from ATP and is inhibitable by calcium. The product of this gene is a member of the adenylyl cyclase class-4/guanylyl cyclase enzyme family that is characterized by the presence of twelve membrane-spanning domains in its sequences.
Taurochenodeoxycholate 6alpha-hydroxylase (, CYP3A4, CYP4A21, taurochenodeoxycholate 6alpha-monooxygenase) is an enzyme with systematic name taurochenodeoxycholate,NADPH:oxygen oxidoreductase (6alpha-hydroxylating). This enzyme catalyses the following chemical reaction : (1) taurochenodeoxycholate + NADPH + H+ \+ O2 \rightleftharpoons taurohyocholate + NADP+ \+ H2O : (2) lithocholate + NADPH + H+ \+ O2 \rightleftharpoons hyodeoxycholate + NADP+ \+ H2O Taurochenodeoxycholate 6α-hydroxylase is a heme-thiolate protein (P-450).
Ferric-chelate reductase (NADPH) (, ferric chelate reductase, iron chelate reductase, NADPH:Fe3+-EDTA reductase, NADPH-dependent ferric reductase, yqjH (gene)) is an enzyme with systematic name Fe(II):NADP+ oxidoreductase. This enzyme catalyses the following chemical reaction : 2 Fe(II) + 2 apo- siderophore + NADP+ \+ H+ \rightleftharpoons 2 Fe(III)-siderophore + NADPH Ferric-chelate reductase contains FAD.
1,8-Cineole 2-endo-monooxygenase (, Formerly , P450cin, CYP176A, CYP176A1) is an enzyme with systematic name 1,8-cineole,NADPH:oxygen oxidoreductase (2-endo-hydroxylating). This enzyme catalyses the following chemical reaction : 1,8-cineole + NADPH + H+ \+ O2 \rightleftharpoons 2-endo-hydroxy-1,8-cineole + NADP+ \+ H2O 1,8-Cineole 2-endo-monooxygenase is a heme-thiolate protein (P-450).
Geraniol 8-hydroxylase (, Formerly , CYP76B6, G10H, CrG10H, SmG10H) is an enzyme with systematic name geraniol,NADPH:oxygen oxidoreductase (8-hydroxylating). This enzyme catalyses the following chemical reaction : geraniol + NADPH + H+ \+ O2 \rightleftharpoons (6E)-8-hydroxygeraniol + NADP+ \+ H2O Geraniol 8-hydroxylase is a cytochrome P450 and therefore requires a partner cytochrome P450 reductase for functional expression.
Stemod-13(17)-ene synthase (, OsKSL11, stemodene synthase) is an enzyme with systematic name 9alpha-copalyl-diphosphate diphosphate-lyase (stemod-13(17)-ene-forming). This enzyme catalyses the following chemical reaction : 9alpha-copalyl diphosphate \rightleftharpoons stemod-13(17)-ene + diphosphate This enzyme takes part in the biosynthesis of the stemodane family of diterpenoid secondary metabolites.
Carotenoid 1,2-hydratase (, CrtC) is an enzyme with systematic name lycopene hydro-lyase (1-hydroxy-1,2-dihydrolycopene-forming). This enzyme catalyses the following chemical reaction : (1) 1-hydroxy-1,2-dihydrolycopene \rightleftharpoons lycopene + H2O : (2) 1,1'-dihydroxy-1,1',2,2'-tetrahydrolycopene \rightleftharpoons 1-hydroxy-1,2-dihydrolycopene + H2O In Rubrivivax gelatinosus and Thiocapsa roseopersicina both products are formed.
Ent-pimara-8(14),15-diene synthase (, OsKS5) is an enzyme with systematic name ent-copalyl-diphosphate diphosphate-lyase (ent-pimara-8(14),15-diene-forming). This enzyme catalyses the following chemical reaction : ent-copalyl diphosphate \rightleftharpoons ent-pimara-8(14),15-diene + diphosphate This diterpene cyclase produces only ent-pimara-8(14),15-diene.
3-hydroxy-D-aspartate aldolase (, D-3-hydroxyaspartate aldolase) is an enzyme with systematic name 3-hydroxy-D-aspartate glyoxylate-lyase (glycine-forming). This enzyme catalyses the following chemical reaction : (1) threo-3-hydroxy-D- aspartate \rightleftharpoons glycine + glyoxylate : (2) D-erythro-3-hydroxyaspartate \rightleftharpoons glycine + glyoxylate This enzyme is a pyridoxal-phosphate protein.
Exo-alpha-bergamotene synthase (, trans-alpha-bergamotene synthase, LaBERS (gene)) is an enzyme with systematic name (2E,6E)-farnesyl diphosphate lyase (cyclizing, (-)-exo-alpha-bergamotene-forming). This enzyme catalyses the following chemical reaction: : (2E,6E)-farnesyl diphosphate \rightleftharpoons (-)-exo-alpha-bergamotene + diphosphate The enzyme synthesizes a mixture of sesquiterpenoids from (2E,6E)-farnesyl diphosphate.
5-epiaristolochene synthase (, 5-epi-aristolochene synthase, tobacco epiaristolochene synthase, farnesyl pyrophosphate cyclase, EAS, TEAS) is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate diphosphate-lyase ((+)-5-epiaristolochene-forming). This enzyme catalyses the following chemical reaction : (2E,6E)-farnesyl diphosphate \rightleftharpoons (+)-5-epiaristolochene + diphosphate Initial cyclization gives (+)-germacrene A in an enzyme bound form.
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.
Beta-amyrin synthase (, 2,3-oxidosqualene beta-amyrin cyclase, AsbAS1, BPY, EtAS, GgbAS1, LjAMY1, MtAMY1, PNY, BgbAS) is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualene mutase (cyclizing, beta-amyrin-forming). This enzyme catalyses the following chemical reaction : (3S)-2,3-epoxy-2,3-dihydrosqualene \rightleftharpoons beta-amyrin Some organism possess a monofunctional beta-amyrin synthase.
Achilleol B synthase () is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualene mutase (cyclizing, achilleol-B-forming). This enzyme catalyses the following chemical reaction : (3S)-2,3-epoxy-2,3-dihydrosqualene \rightleftharpoons achilleol B Achilleol B is probably formed by cleavage of the 8-14 and 9-10 bonds of (3S)-2,3-epoxy-2,3-dihydrosqualene.
23S rRNA pseudouridine1911/1915/1917 synthase (, RluD, pseudouridine synthase RluD) is an enzyme with systematic name 23S rRNA-uridine1911/1915/1917 uracil mutase. This enzyme catalyses the following chemical reaction : 23S rRNA uridine1911/uridine1915/uridine1917 \rightleftharpoons 23S rRNA pseudouridine1911/pseudouridine1915/pseudouridine1917 These nucleotides are located in the functionally important helix-loop 69 of 23S rRNA.
O-phosphoseryl-tRNASec kinase (, PSTK, phosphoseryl-tRNA[Ser]Sec kinase, phosphoseryl-tRNASec kinase) is an enzyme with systematic name ATP:L-seryl- tRNASec O-phosphotransferase. This enzyme catalyses the following chemical reaction : ATP + L-seryl-tRNASec \rightleftharpoons ADP + O-phospho-L-seryl- tRNASec In archaea and eukarya selenocysteine formation is achieved by a two- step process.
Glycerate 2-kinase (, D-glycerate-2-kinase, glycerate kinase (2-phosphoglycerate forming), ATP:(R)-glycerate 2-phosphotransferase) is an enzyme with systematic name ATP:D-glycerate 2-phosphotransferase. This enzyme catalyses the following chemical reaction : ATP + D-glycerate \rightleftharpoons ADP + 2-phospho-D-glycerate A key enzyme in the nonphosphorylative Entner-Doudoroff pathway in archaea.
16S rRNA (cytidine1409-2'-O)-methyltransferase (, TlyA) is an enzyme with systematic name S-adenosyl-L-methionine:16S rRNA (cytidine1409-2'-O)-methyltransferase. This enzyme catalyses the following chemical reaction : S-adenosyl-L-methionine + cytidine1409 in 16S rRNA \rightleftharpoons S-adenosyl-L-homocysteine + 2'-O-methylcytidine1409 in 16S rRNA The bifunctional enzyme from Mycobacterium tuberculosis.
Trans-o-hydroxybenzylidenepyruvate hydratase-aldolase (, 2'-hydroxybenzalpyruvate aldolase, NsaE, tHBPA hydratase-aldolase) is an enzyme with systematic name (3E)-4-(2-hydroxyphenyl)-2-oxobut-3-enoate hydro- lyase. This enzyme catalyses the following chemical reaction : (3E)-4-(2-hydroxyphenyl)-2-oxobut-3-enoate + H2O \rightleftharpoons salicylaldehyde + pyruvate This enzyme is involved in naphthalene degradation.
TRNA (adenine22-N1)-methyltransferase (, TrmK, YqfN, Sp1610 (gene), tRNA: m1A22 methyltransferase) is an enzyme with systematic name S-adenosyl-L- methionine:tRNA (adenine22-N1)-methyltransferase. This enzyme catalyses the following chemical reaction : S-adenosyl-L-methionine + adenine22 in tRNA \rightleftharpoons S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA The enzyme specifically methylates adenine22 in tRNA.
CMP-N,N'-diacetyllegionaminic acid synthase (, CMP-N,N'-diacetyllegionaminic acid synthetase, neuA (gene), legF (gene)) is an enzyme with systematic name CTP:N,N'-diacetyllegionaminate cytidylyltransferase. This enzyme catalyses the following chemical reaction : CTP + N,N'-diacetyllegionaminate \rightleftharpoons CMP-N,N'-diacetyllegionaminate + diphosphate This enzyme is isolated from the bacteria Legionella pneumophila and Campylobacter jejuni.
2-oxo-3-(5-oxofuran-2-ylidene)propanoate lactonase (, naaC (gene)) is an enzyme with systematic name 2-oxo-3-(5-oxofuran-2-ylidene)propanoate lactonohydrolase. This enzyme catalyses the following chemical reaction : 2-oxo-3-(5-oxofuran-2-ylidene)propanoate + H2O \rightleftharpoons maleylpyruvate This enzyme is isolated from the soil bacterium Bradyrhizobium sp. JS329.
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.
Galactan 1,3-beta-galactosidase (, galactan (1->3)-beta-D-galactosidase) is an enzyme with systematic name galactan 3-beta-D-galactosidase. This enzyme catalyses the following chemical reaction : Hydrolysis of terminal, non- reducing beta-D-galactose residues in (1->3)-beta-D-galactopyranans This enzyme removes not only free galactose, but also 6-glycosylated residues.
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.
Peptidyl-dipeptidase Dcp (, dipeptidyl carboxypeptidase (Dcp), dipeptidyl carboxypeptidase) is an enzyme. It catalyses the following chemical reaction : Hydrolysis of unblocked, C-terminal dipeptides from oligopeptides, with broad specificity. Does not hydrolyse bonds in which P1' is Pro, or both P1 and P1' are Gly This zinc metallopeptidase is isolated from Escherichia coli and Salmonella typhimurium.
3',5'-cyclic-AMP phosphodiesterase (, cAMP-specific phosphodiesterase, cAMP- specific PDE, PDE1, PDE2A, PDE2B, PDE4, PDE7, PDE8, PDEB1, PDEB2) is an enzyme with systematic name 3',5'-cyclic-AMP 5'-nucleotidohydrolase. This enzyme catalyses the following chemical reaction : adenosine 3',5'-cyclic phosphate + H2O \rightleftharpoons AMP This enzyme requires Mg2+ or Mn2+ for activity.
In molecular biology, the DHH phosphatase family is a family of phosphoesterases. The family includes Drosophila prune protein and bacterial RecJ exonuclease. The RecJ protein of Escherichia coli plays an important role in a number of DNA repair and recombination pathways. RecJ catalyses processive degradation of single-stranded DNA in a 5'-to-3' direction.
This enzyme participates in folate biosynthesis. This enzyme catalyses the first step in a three-step pathway leading to 7,8 dihydrofolate. Bacterial HPPK (gene folK or sulD) is a protein of 160 to 270 amino acids. In the lower eukaryote Pneumocystis carinii, HPPK is the central domain of a multifunctional folate synthesis enzyme (gene fas).
Skeletal structure of succinate Succinate is formed in E. coli in several steps. Phosphoenolpyruvate (PEP), a glycolysis pathway intermediate, is carboxylated by the enzyme PEP carboxylase to form oxaloacetate. This is followed by the conversion of oxaloacetate to malate by the enzyme malate dehydrogenase. Fumarate hydratase then catalyses the dehydration of malate to produce fumarate.
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.
Brachyurin (, Uca pugilator collagenolytic proteinase, crab protease I, crab protease II) is an enzyme. This enzyme catalyses the Hydrolysis of proteins, with broad specificity for peptide bonds. Native collagen is cleaved about 75% of the length of the molecule from the N-terminus. This enzyme is isolated from hepatopancreas of the fiddler crab, Uca pugilator.
Pancreatic endopeptidase E (, cholesterol-binding proteinase, proteinase E, cholesterol-binding serine proteinase, pancreatic protease E, pancreatic proteinase E, cholesterol-binding pancreatic proteinase, CBPP, pancreas E proteinase) is an enzyme. This enzyme catalyses the following chemical reaction : Preferential cleavage: Ala-. Does not hydrolyse elastin This enzyme is peptidase of family S1 (trypsin family) from pancreatic juice.
The C-terminal region of the light chain of one molecule binds to the active site cleft of another molecule in the manner of a substrate. This enzyme catalyses the following chemical reaction : Preferential cleavage in B chain of insulin: Asn3-Gln, Gly13-Ala, Tyr26-Thr This enzyme is isolated from Aspergillus niger var. macrosporus.
Ubiquitinyl hydrolase 1 (, ubiquitin C-terminal hydrolase, yeast ubiquitin hydrolase) is an enzyme. This enzyme catalyses the following chemical reaction : Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin This enzyme hydrolyses links to polypeptides smaller than 60 residues faster than those to larger polypeptides.
This is the enzyme which catalyses Pyruvate decarboxylation, the reaction of Pyruvate with Coenzyme A and the major entry point into the TCA cycle: :Pyruvate + Coenzyme A + NAD+ ⇒ acetyl-CoA + NADH + H+ \+ CO2 Pyruvate dehydrogenase has three chemical compartments; E1 (pyruvate decarboxylase), E2 (dihydrolipoyl transacetylase) and E3 (dihydrolipoyl dehydrogenase). Each one of the compartments has its own specific function.
23S rRNA (guanine2445-N2)-methyltransferase (, ycbY (gene), rlmL (gene)) is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (guanine2445-N2)-methyltransferase. This enzyme catalyses the following chemical reaction : S-adenosyl-L-methionine + guanine2445 in 23S rRNA \rightleftharpoons S-adenosyl-L-homocysteine + N2-methylguanine2445 in 23S rRNA The enzyme methylates 23S rRNA in vitro.
Malonyl-CoA O-methyltransferase (, BioC) is an enzyme with systematic name S-adenosyl-L-methionine:malonyl-CoA O-methyltransferase. This enzyme catalyses the following chemical reaction : S-adenosyl-L-methionine + malonyl-CoA \rightleftharpoons S-adenosyl-L-homocysteine + malonyl-CoA methyl ester Malonyl-CoA O-methyltransferase is involved in an early step of biotin biosynthesis in Gram-negative bacteria.
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.
Peptidyl-glutamate 4-carboxylase (, vitamin K-dependent carboxylase, gamma- glutamyl carboxylase) is an enzyme with systematic name peptidyl-glutamate 4-carboxylase (2-methyl-3-phytyl-1,4-naphthoquinone-epoxidizing). This enzyme catalyses the following chemical reaction : peptidyl-4-carboxyglutamate + 2,3-epoxyphylloquinone + H2O \rightleftharpoons peptidyl-glutamate + CO2 \+ O2 \+ phylloquinone The enzyme can use various vitamin-K derivatives, including menaquinone.
Ubiquinol oxidase (H+-transporting) (, cytochrome bb3 oxidase, cytochrome bo oxidase, cytochrome bd-I oxidase) is an enzyme with systematic name ubiquinol:O2 oxidoreductase (H+-transporting). This enzyme catalyses the following chemical reaction : 2 ubiquinol + O2 \+ n H+in \rightleftharpoons 2 ubiquinone + 2 H2O + n H+out Ubiquinol oxidase contains a dinuclear centre comprising two hemes, or heme and copper.
Methionine-S-oxide reductase (, methyl sulfoxide reductase I and II, acetylmethionine sulfoxide reductase, methionine sulfoxide reductase, L-methionine:oxidized-thioredoxin S-oxidoreductase) is an enzyme with systematic name L-methionine:thioredoxin-disulfide S-oxidoreductase. This enzyme catalyses the following chemical reaction : L-methionine + thioredoxin disulfide + H2O \rightleftharpoons L-methionine S-oxide + thioredoxin In the reverse reaction, dithiothreitol can replace reduced thioredoxin.
Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 3 is an enzyme that in humans is encoded by the NDST3 gene. It catalyses the reaction: > 3'-phosphoadenylyl sulfate + α-D-glucosaminyl-[heparan sulfate](n) = > adenosine 3',5'-bisphosphate + 2 H+ \+ N-sulfo-α-D-glucosaminyl-[heparan > sulfate](n) This is a step in the production of heparin.
Pseudotropine acyltransferase (, pseudotropine:acyl-CoA transferase, tigloyl- CoA:pseudotropine acyltransferase, acetyl-CoA:pseudotropine acyltransferase, pseudotropine acetyltransferase, pseudotropine tigloyltransferase, PAT) is an enzyme with systematic name acyl-CoA:pseudotropine O-acyltransferase. This enzyme catalyses the following chemical reaction : acyl-CoA + pseudotropine \rightleftharpoons CoA + O-acylpseudotropine This enzyme exhibits absolute specificity for the exo/3beta configuration found in pseudotropine as tropine (tropan-3alpha-ol).
TRNAMet cytidine acetyltransferase (, YpfI, TmcA) is an enzyme with systematic name acetyl-CoA:(elongator tRNAMet)-cytidine34 N4-acetyltransferase (ATP- hydrolysing). This enzyme catalyses the following chemical reaction : [elongator tRNAMet]-cytidine34 \+ ATP + acetyl-CoA \rightleftharpoons CoA + [elongator tRNAMet]-N4-acetylcytidine34 \+ ADP + phosphate The enzyme acetylates the wobble base C34 of the CAU anticodon of elongation-specific tRNAMet.
Benzyl alcohol O-benzoyltransferase (, benzoyl-CoA:benzyl alcohol benzoyltransferase, benzoyl-CoA:benzyl alcohol/phenylethanol benzoyltransferase, benzoyl-coenzyme A:benzyl alcohol benzoyltransferase, benzoyl-coenzyme A:phenylethanol benzoyltransferase) is an enzyme with systematic name benzoyl-CoA:benzyl alcohol O-benzoyltransferase. This enzyme catalyses the following chemical reaction : benzoyl-CoA + benzyl alcohol \rightleftharpoons CoA + benzyl benzoate The enzyme is involved in benzenoid and benzoic acid biosynthesis.
3,5,7-Trioxododecanoyl-CoA synthase (, TKS) is an enzyme with systematic name malonyl-CoA:hexanoyl-CoA malonyltransferase (3,5,7-trioxododecanoyl-CoA- forming). This enzyme catalyses the following chemical reaction : 3 malonyl- CoA + hexanoyl-CoA \rightleftharpoons 3 CoA + 3,5,7-trioxododecanoyl-CoA + 3 CO2 This polyketide synthase catalyse the first step in the cannabinoids biosynthetic pathway of the plant Cannabis sativa.
"SARS" and it’s enzyme product seryl- tRNA synthetase are involved in protein translation; specifically, seryl-tRNA synthetase catalyses the transfer of L-serine to tRNA (Ser). The cytosolic enzyme recognises its cognate tRNA species and binds with a high level of specificity, allowing the accurate interaction between corresponding codons and anticodons on mRNA and tRNA during protein translation.
Magnolysin (, bovine neurosecretory granule protease cleaving pro- oxytocin/neurophysin, pro-oxytocin/neurophysin convertase, prooxyphysin proteinase, pro-oxytocin convertase) is an enzyme. This enzyme catalyses the following chemical reaction : Hydrolysis of polypeptides with Arg or Lys in P1 and P2, e.g. to hydrolyse pro-oxytocin at -Lys-Arg-Ala-Val-. This endopeptidase is present in bovine pituitary neurosecretory granules.
Pitrilysin (, Escherichia coli protease III, protease Pi, proteinase Pi, PTR, Escherichia coli metalloproteinase Pi) is an enzyme. This enzyme catalyses the following chemical reaction: : Preferential cleavage of -Tyr16\- Leu- and -Phe25\- Tyr-bonds of oxidized insulin B chain. Also acts on other substrates of less than 7 kDa such as glucagon This enzyme is present in bacteria Escherichia coli.
Atrolysin F (, Crotalus atrox metalloendopeptidase, hemorrhagic toxin f, Crotalus atrox metalloendopeptidase f) is an enzyme. This enzyme catalyses the following chemical reaction : Cleavage of Val2-Asn, Gln4-His, Leu6-Cys, His10-Leu, Ala14-Leu and Tyr16-Leu bonds in insulin B chain This endopeptidase is present in the venom of the western diamondback rattlesnake (Crotalus atrox).
Bacillolysin (, Bacillus metalloendopeptidase, Bacillus subtilis neutral proteinase, anilozyme P 10, Bacillus metalloproteinase, Bacillus neutral proteinase, megateriopeptidase) is an enzyme. This enzyme catalyses the following chemical reaction : Similar, but not identical, to that of thermolysin This enzyme is present in many Bacillus species, including B. subtilis, B. amyloliquefaciens, B. megaterium, B. mesentericus, B. cereus and B. stearothermophilus.
Serralysin (, Pseudomonas aeruginosa alkaline proteinase, Escherichia freundii proteinase, Serratia marcescens extracellular proteinase, Serratia marcescens metalloproteinase, Pseudomonas aeruginosa alk. protease, Serratia marcescens metalloprotease) is an enzyme. This enzyme catalyses the following chemical reaction : Preferential cleavage of bonds with hydrophobic residues in P1' This extracellular endopeptidase is present in Pseudomonas aeruginosa, Escherichia freundii, Serratia marcescens and Erwinia chrysanthemi.
Leucolysin (, Leucostoma neutral proteinase, Leucostoma peptidase A) is an enzyme. This enzyme catalyses the following chemical reaction : Cleavage of Phe1-Val, His5-Leu, Ala14-Leu, Gly20-Glu, Gly23-Phe and Phe24-Phe bonds in insulin B chain as well as N-blocked dipeptides This enzyme is isolated from the venom of the western cottonmouth moccasin snake (Agkistrodon piscivorus leucostoma).
2'-N-acetylparomamine deacetylase (, btrD (gene), neoL (gene), kanN (gene)) is an enzyme with systematic name 2'-N-acetylparomamine hydrolase (acetate- forming). This enzyme catalyses the following chemical reaction : 2'-N-acetylparomamine + H2O \rightleftharpoons paromamine + acetate This enzyme takes part in the biosynthetic pathways of several clinically important aminocyclitol antibiotics, including kanamycin, butirosin, neomycin and ribostamycin.
2-acetyl-6-hydroxyneomycin C deacetylase (, neoL (gene)) is an enzyme with systematic name 2-acetyl-6-hydroxyneomycin C hydrolase (acetate-forming). This enzyme catalyses the following chemical reaction : 2-acetyl-6-deamino-6-hydroxyneomycin C + H2O \rightleftharpoons 6-deamino-6-hydroxyneomycin C + acetate This enzyme is involved in biosynthesis of aminoglycoside antibiotics of the [neomycin] family.
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.
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.
NPP catalyses the nucleophilic substitution of one ester bond on a phosphodiester substrate. It has a nucleoside binding pocket that excludes phospholipid substrates from the active site. A threonine nucleophile has been identified through site-directed mutagenesis, and the reaction inverts the stereochemistry of the phosphorus center. The sequence of bond breakage and formation has yet to be resolved.
Succinate-semialdehyde dehydrogenase (NADP+) (, succinic semialdehyde dehydrogenase (NADP+), succinyl semialdehyde dehydrogenase (NADP+), succinate semialdehyde:NADP+ oxidoreductase, NADP-dependent succinate-semialdehyde dehydrogenase, GabD) is an enzyme with systematic name succinate- semialdehyde:NADP+ oxidoreductase. This enzyme catalyses the following chemical reaction : succinate semialdehyde + NADP+ \+ H2O \rightleftharpoons succinate + NADPH + 2 H+ This enzyme participates in the degradation of glutamate and 4-aminobutyrate.
Beta-apo-4'-carotenal oxygenase (, beta-apo-4'-carotenal dehydrogenase, YLO-1, carD (gene)) is an enzyme with systematic name 4'-apo-beta,psi-carotenal:NAD+ oxidoreductase. This enzyme catalyses the following chemical reaction: : 4'-apo-beta, psi-caroten-4'-al + NAD+ \+ H2O \rightleftharpoons neurosporaxanthin + NADH + 2 H+ Neurosporaxanthin is responsible for the orange color of Neurospora.
3-Succinoylsemialdehyde-pyridine dehydrogenase () is an enzyme with systematic name 4-oxo-4-(pyridin-3-yl)butanal:NADP+ oxidoreductase. This enzyme catalyses the following chemical reaction : 4-oxo-4-(pyridin-3-yl)butanal + NADP+ \+ H2O \rightleftharpoons 4-oxo-4-(pyridin-3-yl)butanoate + NADPH + H+ The enzyme has been characterized from the soil bacterium Pseudomonas sp. HZN6.
Mn2+-dependent ADP-ribose/CDP-alcohol diphosphatase (, Mn2+-dependent ADP- ribose/CDP-alcohol pyrophosphatase, ADPRibase-Mn) is an enzyme with systematic name CDP-choline phosphohydrolase. This enzyme catalyses the following chemical reaction : (1) CDP-choline + H2O \rightleftharpoons CMP + phosphocholine : (2) ADP-ribose + H2O \rightleftharpoons AMP + D-ribose 5-phosphate This enzyme requires Mn2+, which cannot be replaced by Mg2+.
Alpha-D-ribose 1-methylphosphonate 5-triphosphate diphosphatase (, phnM (gene)) is an enzyme with systematic name alpha-D- ribose-1-methylphosphonate-5-triphosphate diphosphohydrolase. This enzyme catalyses the following chemical reaction : alpha-D-ribose 1-methylphosphonate 5-triphosphate + H2O \rightleftharpoons alpha-D-ribose 1-methylphosphonate 5-phosphate + diphosphate This enzyme is isolated from the bacterium Escherichia coli.
Very-long-chain acyl-CoA dehydrogenase (, ACADVL (gene).) is an enzyme with systematic name very-long-chain acyl-CoA:electron-transfer flavoprotein 2,3-oxidoreductase. This enzyme catalyses the following chemical reaction : a very-long-chain acyl-CoA + electron-transfer flavoprotein \rightleftharpoons a very-long-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein This enzyme contains FAD as prosthetic group.
Dipeptidyl-peptidase III (, dipeptidyl aminopeptidase III, dipeptidyl arylamidase III, enkephalinase B, red cell angiotensinase) is an enzyme. This enzyme catalyses the following chemical reaction : Release of an N-terminal dipeptide from a peptide comprising four or more residues, with broad specificity. Also acts on dipeptidyl 2-naphthylamides. This cytosolic peptidase that is active at neutral pH.
Pseudooxynicotine oxidase () is an enzyme with systematic name 4-(methylamino)-1-(pyridin-3-yl)butan-1-one:oxygen oxidoreductase (methylamine releasing). This enzyme catalyses the following chemical reaction : 4-(methylamino)-1-(pyridin-3-yl)butan-1-one + H2O + O2 \rightleftharpoons 4-oxo-4-(pyridin-3-yl)butanal + methylamine + H2O2 This enzyme contains one non-covalently bound FAD.
Carboxynorspermidine synthase (, carboxynorspermidine dehydrogenase, carboxyspermidine dehydrogenase, CASDH, CANSDH) is an enzyme with systematic name carboxynorspermidine:NADP+ oxidoreductase. This enzyme catalyses the following chemical reactions : (1) carboxynorspermidine + H2O + NADP+ \rightleftharpoons L-aspartate 4-semialdehyde + propane-1,3-diamine + NADPH + H+ : (2) carboxyspermidine + H2O + NADP+ \rightleftharpoons L-aspartate 4-semialdehyde + putrescine + NADPH + H+ The reaction takes place in the opposite direction.
Hypoxia-inducible factor-asparagine dioxygenase (, HIF hydroxylase) is an enzyme with systematic name hypoxia-inducible factor-L-asparagine, 2-oxoglutarate:oxygen oxidoreductase (4-hydroxylating). This enzyme catalyses the following chemical reaction : hypoxia-inducible factor-L-asparagine + 2-oxoglutarate + O2 \rightleftharpoons hypoxia-inducible factor-(3S)-3-hydroxy-L-asparagine + succinate + CO2 Hypoxia-inducible factor- asparagine dioxygenase contains iron, and requires ascorbate.
DNA oxidative demethylase (, alkylated DNA repair protein, alpha- ketoglutarate-dependent dioxygenase ABH1, alkB (gene)) is an enzyme with systematic name methyl DNA-base, 2-oxoglutarate:oxygen oxidoreductase (formaldehyde-forming). This enzyme catalyses the following chemical reaction : DNA-base-CH3 \+ 2-oxoglutarate + O2 \rightleftharpoons DNA-base + formaldehyde + succinate + CO2 DNA oxidative demethylase contains iron; activity is somewhat stimulated by ascorbate.
Benzoyl-CoA 2,3-dioxygenase (, benzoyl-CoA dioxygenase/reductase, BoxBA, BoxA/BoxB system) is an enzyme with systematic name benzoyl-CoA,NADPH:oxygen oxidoreductase (2,3-hydroxylating). This enzyme catalyses the following chemical reaction : benzoyl-CoA + NADPH + H+ \+ O2 \rightleftharpoons 2,3-dihydro-2,3-dihydroxybenzoyl-CoA + NADP+ Benzoyl-CoA 2,3-dioxygenase is involved in aerobic benzoate metabolism in Azoarcus evansii.
Desosaminyl transferase EryCIII (, EryCIII) is an enzyme with systematic name dTDP-3-dimethylamino-4,6-dideoxy-alpha-D-glucopyranose:3-alpha- mycarosylerythronolide B 3-dimethylamino-4,6-dideoxy-alpha-D- glucosyltransferase. This enzyme catalyses the following chemical reaction : dTDP-3-dimethylamino-4,6-dideoxy-alpha-D-glucopyranose + 3-alpha- mycarosylerythronolide B \rightleftharpoons dTDP + erythromycin D The enzyme is involved in erythromycin biosynthesis.
Carotenoid isomerooxygenase (, ninaB (gene)) is an enzyme with systematic name zeaxanthin:oxygen 15,15'-oxidoreductase (bond-cleaving, cis-isomerizing). This enzyme catalyses the following chemical reaction : zeaxanthin + O2 \rightleftharpoons (3R)-11-cis-3-hydroxyretinal + (3R)-all- trans-3-hydroxyretinal The enzyme from the moth Galleria mellonella and the fruit fly Drosophila melanogaster takes part in the synthesis of retinal .
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.
Dye-decolorizing peroxidase (, DyP, DyP-type peroxidase) is an enzyme with systematic name Reactive-Blue-5:hydrogen-peroxide oxidoreductase. This enzyme catalyses the following chemical reaction : Reactive Blue 5 + H2O2 \rightleftharpoons phthalate + 2,2'-disulfonyl azobenzene + 3-[(4-amino-6-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonate These heme proteins are secreted by basidiomycetous fungi and eubacteria.
9-cis-beta-carotene 9',10'-cleaving dioxygenase (, CCD7 (gene), MAX3 (gene), NCED7 (gene)) is an enzyme with systematic name 9-cis-beta-carotene:O2 oxidoreductase (9',10'-cleaving). This enzyme catalyses the following chemical reaction : 9-cis-beta-carotene + O2 \rightleftharpoons 9-cis-10'-apo-beta- carotenal + beta-ionone 9-cis-beta-carotene 9',10'-cleaving dioxygenase contains Fe2+.
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.
Plasmepsin II (, aspartic hemoglobinase II, PFAPD) is an enzyme. This enzyme catalyses the following chemical reaction : Hydrolysis of the bonds linking certain hydrophobic residues in hemoglobin or globin. Also cleaves the small molecule substrates such as Ala-Leu-Glu-Arg-Thr-Phe-Phe(NO2)-Ser-Phe-Pro-Thr This enzyme is present in malaria organism, Plasmodium.
Phytepsin () is an enzyme. This enzyme catalyses the following chemical reaction : Prefers hydrophobic residues Phe, Val, Ile, Leu, and Ala at P1 and P1', but also cleaves -Phe-Asp- and -Asp-Asp- bonds in 2S albumin from plant seeds This enzyme is present in barley grain and other plants. It is an aspartic protease with a plant-specific insert.
Plasminogen activator Pla () is an enzyme. This enzyme catalyses the following chemical reaction : Converts human Glu-plasminogen to plasmin by cleaving the Arg560-Val peptide bond that is also hydrolysed by the mammalian u-plasminogen activator and t-plasminogen activator. Also cleaves arginyl bonds in other proteins This enzyme is isolated from the bacterium Yersinia pestis that causes plague.
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.
Steroid 15beta-monooxygenase (, cytochrome P-450meg, cytochrome P450meg, steroid 15beta-hydroxylase, CYP106A2, BmCYP106A2) is an enzyme with systematic name progesterone,reduced-ferredoxin:oxygen oxidoreductase (15beta- hydroxylating) . This enzyme catalyses the following chemical reaction : progesterone + reduced ferredoxin + O2 \rightleftharpoons 15beta- hydroxyprogesterone + oxidized ferredoxin + H2O The enzyme from Bacillus megaterium hydroxylates a variety of 3-oxo-Delta4-steroids in position 15beta.
Uracil/thymine dehydrogenase (, uracil oxidase, uracil-thymine oxidase, uracil dehydrogenase) is an enzyme with systematic name uracil:acceptor oxidoreductase. This enzyme catalyses the following chemical reaction : (1) uracil + H2O + acceptor \rightleftharpoons barbiturate + reduced acceptor : (2) thymine + H2O + acceptor \rightleftharpoons 5-methylbarbiturate + reduced acceptor Uracil/thymine dehydrogenase forms part of the oxidative pyrimidine- degrading pathway in some microorganisms.
5-epiaristolochene 1,3-dihydroxylase (, 5-epi-aristolochene 1,3-dihydroxylase, EAH) is an enzyme with systematic name 5-epiaristolochene,NADPH:oxygen oxidoreductase (1- and 3-hydroxylating). This enzyme catalyses the following chemical reaction : 5-epiaristolochene + 2 NADPH + 2 H+ \+ 2 O2 \rightleftharpoons capsidiol + 2 NADP+ \+ 2 H2O 5-epiaristolochene 1,3-dihydroxylase is a heme-thiolate protein (P-450).
Adenylyl cyclase is a membrane bound enzyme that catalyses the formation of cyclic AMP from ATP. It is regulated by a family of G protein-coupled receptors, protein kinases, and calcium. The type 9 adenylyl cyclase is a widely distributed adenylyl cyclase, and it is stimulated by beta-adrenergic receptor activation but is insensitive to forskolin, calcium, and somatostatin.
Limonene 1,2-monooxygenase () is an enzyme with systematic name limonene,NAD(P)H:oxygen oxidoreductase. This enzyme catalyses the following chemical reaction : (1) (S)-limonene + NAD(P)H + H+ \+ O2 \rightleftharpoons 1,2-epoxymenth-8-ene + NAD(P)+ \+ H2O : (2) (R)-limonene + NAD(P)H + H+ \+ O2 \rightleftharpoons 1,2-epoxymenth-8-ene + NAD(P)+ \+ H2O Limonene 1,2-monooxygenase flavoprotein (FAD).
Beta-amyrin 24-hydroxylase (, sophoradiol 24-hydroxylase, CYP93E1) is an enzyme with systematic name beta-amyrin,AH2:oxygen oxidoreductase (24-hydroxylating). This enzyme catalyses the following chemical reaction : (1) beta-amyrin + AH2 \+ O2 \rightleftharpoons 24-hydroxy-beta-amyrin + A + H2O : (2) sophoradiol + AH2 \+ O2 \rightleftharpoons 24-hydroxysophoradiol + A + H2O Beta-amyrin 24-hydroxylase is heme-thiolate protein (P-450).
Pyrimidine oxygenase (, RutA) is an enzyme with systematic name uracil,FMNH2:oxygen oxidoreductase (uracil hydroxylating, ring-opening) . This enzyme catalyses the following chemical reaction : (1) uracil + FMNH2 \+ O2 \rightleftharpoons (Z)-3-ureidoacrylate peracid + FMN : (2) thymine + FMNH2 \+ O2 \rightleftharpoons (Z)-2-methylureidoacrylate peracid + FMN In vitro the product (Z)-3-ureidoacrylate peracid is spontaneously reduced to ureidoacrylate.
Ammonia monooxygenase (, AMO) is an enzyme, which catalyses the following chemical reaction : ammonia + AH2 \+ O2 \rightleftharpoons NH2OH + A + H2O Ammonia monooxygenase contains copper and possibly nonheme iron. AMO is the first enzyme in ammonia oxidation. Aerobic oxidation of ammonia to hydroxylamine via AMO is an endergonic reaction. So, all aerobic ammonia oxidizing organisms conserve energy by further oxidizing hydroxylamine.
Indole-2-monooxygenase (, BX2 (gene), CYP71C4 (gene)) is an enzyme with systematic name indole,NAD(P)H:oxygen oxidoreductase (2-hydroxylating). This enzyme catalyses the following chemical reaction : indole + NAD(P)H + H+ \+ O2 \rightleftharpoons indolin-2-one + NAD(P)+ + H2O Indole-2-monooxygenase is involved in the biosynthesis of protective and allelopathic benzoxazinoids in some plants.
Ent-isokaurene C2-hydroxylase (, CYP71Z6) is an enzyme with systematic name ent-isokaurene,NADPH:oxygen oxidoreductase (hydroxylating). This enzyme catalyses the following chemical reaction : ent-isokaurene + O2 \+ NADPH + H+ \rightleftharpoons ent-2alpha-hydroxyisokaurene + H2O + NADP+ Ent-isokaurene C2-hydroxylase performs the initial step in the conversion of ent-isokaurene to the antibacterial oryzalides in rice, Oryza sativa.
Ent-cassa-12,15-diene 11-hydroxylase (, Formerly , ent-cassadiene C11alpha- hydroxylase, CYP76M7) is an enzyme with systematic name ent- cassa-12,15-diene,NADPH:oxygen 11-oxidoreductase. This enzyme catalyses the following chemical reaction : ent-cassa-12,15-diene + O2 \+ NADPH + H+ \rightleftharpoons ent-11beta-hydroxycassa-12,15-diene + NADP+ \+ H2O Ent- cassa-12,15-diene 11-hydroxylase requires cytochrome P450.
Taxoid 14beta-hydroxylase () is an enzyme with systematic name 10beta- hydroxytaxa-4(20),11-dien-5alpha-yl-acetate,NADPH:oxygen 14-oxidoreductase. This enzyme catalyses the following chemical reaction : 10beta- hydroxytaxa-4(20),11-dien-5alpha-yl acetate + O2 \+ NADPH + H+ \rightleftharpoons 10beta,14beta-dihydroxytaxa-4(20),11-dien-5alpha-yl acetate + NADP+ \+ H2O Taxoid 14beta-hydroxylase requires cytochrome P450.
Pectate trisaccharide-lyase (, exopectate-lyase, pectate lyase A, PelA) is an enzyme with systematic name (1->4)-alpha-D-galacturonan reducing-end- trisaccharide-lyase. This enzyme catalyses the following chemical reaction: : eliminative cleavage of unsaturated trigalacturonate as the major product from the reducing end of polygalacturonic acid/pectate The predominant action of this enzyme is removal of a trisaccharide.
Ent-cassa-12,15-diene synthase (, OsDTC1, OsKS7) is an enzyme with systematic name ent-copalyl-diphosphate diphosphate-lyase (ent-cassa-12,15-diene- forming). This enzyme catalyses the following chemical reaction : ent-copalyl diphosphate \rightleftharpoons ent-cassa-12,15-diene + diphosphate This class I diterpene cyclase produces ent-cassa-12,15-diene, a precursor of the rice phytoalexins (-)-phytocassanes A-E.
Ent-sandaracopimaradiene synthase (, OsKS10, ent- sandaracopimara-8(14),15-diene synthase) is an enzyme with systematic name ent-copalyl-diphosphate diphosphate-lyase (ent-sandaracopimara-8(14),15-diene- forming). This enzyme catalyses the following chemical reaction : ent-copalyl diphosphate \rightleftharpoons ent-sandaracopimara-8(14),15-diene + diphosphate ent-Sandaracopimaradiene is a precursor of the rice oryzalexins A-F.
Dammarenediol II synthase (, dammarenediol synthase, 2,3-oxidosqualene (20S)-dammarenediol cyclase, DDS, (S)-squalene-2,3-epoxide hydro-lyase (dammarenediol-II forming)) is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualene hydro-lyase (dammarenediol-II forming). This enzyme catalyses the following chemical reaction : dammarenediol II \rightleftharpoons (3S)-2,3-epoxy-2,3-dihydrosqualene + H2O The reaction occurs in the reverse direction.
10-epi-gamma-eudesmol synthase () is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate diphosphate-lyase (10-epi-gamma-eudesmol- forming). This enzyme catalyses the following chemical reaction: : (2E,6E)-farnesyl diphosphate + H2O \rightleftharpoons 10-epi-gamma-eudesmol + diphosphate The recombinant enzyme from ginger (Zingiber zerumbet) forms beta- eudesmol, 10-epi-gamma-eudesmol, alpha-eudesmol and aristolene.
2-methylisoborneol synthase (, sco7700, 2-MIB cyclase, MIB synthase, MIBS) is an enzyme with systematic name (E)-2-methylgeranyl-diphosphate diphosphate- lyase (cyclizing, 2-methylisoborneol-forming). This enzyme catalyses the following chemical reaction : (E)-2-methylgeranyl diphosphate + H2O \rightleftharpoons 2-methylisoborneol + diphosphate The product, 2-methylisoborneol, is a characteristic odiferous compound with a musty smell produced by soil microorganisms.
3,4-dihydroxyphenylalanine reductive deaminase (, reductive deaminase, DOPA- reductive deaminase, DOPARDA) is an enzyme with systematic name 3,4-dihydroxy- L-phenylalanine ammonia-lyase (3,4-dihydroxyphenylpropanoate-forming). This enzyme catalyses the following chemical reaction : L-dopa + 2 NADH \rightleftharpoons 3,4-dihydroxyphenylpropanoate + 2 NAD+ \+ NH3 This enzyme participates in the L-phenylalanine-catabolism in the anaerobic phototrophic bacterium Rhodobacter sphaeroides OU5.
Carboxybiotin decarboxylase (, MadB, carboxybiotin protein decarboxylase) is an enzyme with systematic name carboxybiotinyl-(protein) carboxy-lyase. This enzyme catalyses the following chemical reaction : a carboxybiotinyl-[protein] + n Na+in \+ H+out \rightleftharpoons CO2 \+ a biotinyl-[protein] + n Na+out (n = 1--2) This enzyme is an integral membrane protein MadB from the anaerobic bacterium Malonomonas rubra.
7-carboxy-7-deazaguanine synthase (, 7-carboxy-7-carbaguanine synthase, queE (gene)) is an enzyme with systematic name 6-carboxy-5,6,7,8-tetrahydropterin ammonia-lyase. This enzyme catalyses the following chemical reaction : 6-carboxy-5,6,7,8-tetrahydropterin \rightleftharpoons 7-carboxy-7-carbaguanine + NH3 The enzyme is a member of the superfamily of S-adenosyl-L-methionine- dependent radical enzymes.
Nucleoside oxidase () is an enzyme with systematic name nucleoside:oxygen 5'-oxidoreductase. This enzyme catalyses the following chemical reaction : inosine + O2 \rightleftharpoons 9-riburonosylhypoxanthine + H2O : (1a) 2 inosine + O2 \rightleftharpoons 2 5'-dehydroinosine + 2 H2O : (1b) 2 5'-dehydroinosine + O2 \rightleftharpoons 2 9-riburonosylhypoxanthine This enzyme could use other purine and pyrimidine nucleosides (as well as 2'-deoxynucleosides) are substrates.
Nucleoside oxidase (H2O2-forming) () is an enzyme with systematic name nucleoside:oxygen 5'-oxidoreductase (H2O2-forming). This enzyme catalyses the following chemical reaction : adenosine + 2 O2 \+ H2O \rightleftharpoons 9-riburonosyladenine + 2 H2O2 (overall reaction) :(1a) adenosine + O2 \rightleftharpoons 5'-dehydroadenosine + H2O2 :(1b) 5'-dehydroadenosine + O2 \+ H2O \rightleftharpoons 9-riburonosyladenine + H2O2 This enzyme contains Heme and belongs to a flavoprotein family.
Formate dehydrogenase-N (, Fdh-N, FdnGHI, nitrate-inducible formate dehydrogenase, formate dehydrogenase N, FDH-N, nitrate inducible Fdn, nitrate inducible formate dehydrogenase) is an enzyme with systematic name formate:quinone oxidoreductase. This enzyme catalyses the following chemical reaction : formate + quinone \rightleftharpoons CO2 \+ quinol This enzyme contains molybdopterin-guanine dinucleotides, five [4Fe-4S] clusters and two heme b groups.
Nicotine blue oxidoreductase (, nboR (gene)) is an enzyme with systematic name 3,3'-bipyridine-2,2',5,5',6,6'-hexol:NADP+ 11-oxidoreductase. This enzyme catalyses the following chemical reaction : 3,3'-bipyridine-2,2',5,5',6,6'-hexol + NAD(P)+ \rightleftharpoons (E)-2,2',5,5'-tetrahydroxy-6H,6'H-[3,3'-bipyridinylidene]-6,6'-dione + NAD(P)H + H+ This enzyme is extracted from bacterium Arthrobacter nicotinovorans.
1-deoxy-11beta-hydroxypentalenate dehydrogenase (, 1-deoxy-11beta- hydroxypentalenic acid dehydrogenase, ptlF (gene), penF (gene name)) is an enzyme with systematic name 1-deoxy-11beta-hydroxypentalenate:NAD+ oxidoreductase. This enzyme catalyses the following chemical reaction : 1-deoxy-11beta-hydroxypentalenate + NAD+ \rightleftharpoons 1-deoxy-11-oxopentalenate + NADH + H+ This enzyme from the bacterium Streptomyces avermitilis participates in pentalenolactone biosynthesis.
All DNA polymerases contain three domains. The first domain, which is known as the "fingers domain", interacts with the dNTP and the paired template base. The "fingers domain" also interacts with the template to position it correctly at the active site. Known as the "palm domain", the second domain catalyses the reaction of the transfer of the phosphoryl group.
DTDP-L-rhamnose 4-epimerase (, dTDP-4-L-rhamnose 4-epimerase, wbiB (gene)) is an enzyme with systematic name dTDP-6-deoxy-beta-L-talose 4-epimerase. This enzyme catalyses the following chemical reaction : dTDP-6-deoxy-beta-L-talose \rightleftharpoons dTDP-6-deoxy-beta-L-mannose The equilibrium is strongly towards dTDP-6-deoxy-beta-L-mannose.
In prokaryotes such as bacteria, diphosphatidylglycerol synthase catalyses a transfer of the phosphatidyl moiety of one phosphatidylglycerol to the free 3'-hydroxyl group of another, with the elimination of one molecule of glycerol, via the action of an enzyme related to phospholipase D. The enzyme can operate in reverse under some physiological conditions to remove cardiolipin.
23S rRNA pseudouridine746 synthase (, RluA, 23S RNA PSI746 synthase, 23S rRNA pseudouridine synthase, pseudouridine synthase RluA) is an enzyme with systematic name 23S rRNA-uridine746 uracil mutase. This enzyme catalyses the following chemical reaction : 23S rRNA uridine746 \rightleftharpoons 23S rRNA pseudouridine746 RluA is the only protein responsible for the in vivo formation of 23S RNA pseudouridine746.
16S rRNA pseudouridine516 synthase (, 16S RNA pseudouridine516 synthase, 16S PsiI516 synthase, 16S RNA Psi516 synthase, RNA pseudouridine synthase RsuA, RsuA, 16S RNA pseudouridine 516 synthase) is an enzyme with systematic name 16S rRNA-uridine516 uracil mutase. This enzyme catalyses the following chemical reaction : 16S rRNA uridine516 \rightleftharpoons 16S rRNA pseudouridine516 The enzyme is specific for uridine516 in 16S rRNA.
23S rRNA pseudouridine955/2504/2580 synthase (, RluC, pseudouridine synthase RluC) is an enzyme with systematic name 23S rRNA-uridine955/2504/2580 uracil mutase. This enzyme catalyses the following chemical reaction : 23S rRNA uridine955/uridine2504/uridine2580 \rightleftharpoons 23S rRNA pseudouridine955/pseudouridine2504/pseudouridine2580 The enzyme converts uridines at position 955, 2504 and 2580 of 23S rRNA to pseudouridines.
N,N'-diacetyllegionaminate synthase (, neuB (gene), legI (gene)) is an enzyme with systematic name phosphoenolpyruvate:2,4-diacetamido-2,4,6-trideoxy-alpha- D-mannopyranose 1-(2-carboxy-2-oxoethyl)transferase. This enzyme catalyses the following chemical reaction : 2,4-diacetamido-2,4,6-trideoxy-alpha-D- mannopyranose + phosphoenolpyruvate + H2O \rightleftharpoons N,N'-diacetyllegionaminate + phosphate This enzyme requires a divalent metal such as Mn2+.
Soluble quinoprotein glucose dehydrogenase (, soluble glucose dehydrogenase, sGDH, glucose dehydrogenase (PQQ-dependent)) is an enzyme with systematic name D-glucose:acceptor oxidoreductase. This enzyme catalyses the following chemical reaction : D-glucose + acceptor \rightleftharpoons D-glucono-1,5-lactone + reduced acceptor This soluble periplasmic enzyme contains PQQ as prosthetic group, and is bound to a calcium ion. Electron acceptor is not known.
Tritrans,polycis-undecaprenyl-diphosphate synthase (geranylgeranyl-diphosphate specific) () is an enzyme with systematic name geranylgeranyl- diphosphate:isopentenyl-diphosphate cistransferase (adding 7 isopentenyl units). This enzyme catalyses the following chemical reaction : geranylgeranyl diphosphate + 7 isopentenyl diphosphate \rightleftharpoons 7 diphosphate + tritrans,heptacis-undecaprenyl diphosphate This enzyme is involved in the biosynthesis of the glycosyl carrier lipid in some archaebacteria.
2-amino-4-deoxychorismate synthase (, ADIC synthase, 2-amino-2-deoxyisochorismate synthase, SgcD) is an enzyme with systematic name (2S)-2-amino-4-deoxychorismate:2-oxoglutarate aminotransferase. This enzyme catalyses the following chemical reaction : (2S)-2-amino-4-deoxychorismate + L-glutamate \rightleftharpoons chorismate + L-glutamine This enzyme requires Mg2+. The reaction occurs in the reverse direction.
Anhydro-N-acetylmuramic acid kinase (, anhMurNAc kinase, AnmK) is an enzyme with systematic name ATP:1,6-anhydro-N-acetyl-beta-muramate 6-phosphotransferase. This enzyme catalyses the following chemical reaction : ATP + 1,6-anhydro-N-acetyl-beta-muramate + H2O \rightleftharpoons ADP + N-acetylmuramate 6-phosphate This enzyme is required for the utilization of anhydro-N-acetylmuramic acid in proteobacteria.
Protein-fructosamine 3-kinase (, FN3K, fructosamine 3-kinase) is an enzyme with systematic name ATP:(protein)-N6-D-fructosyl-L-lysine 3-phosphotransferase. This enzyme catalyses the following chemical reaction : ATP + [protein]-N6-D-fructosyl-L-lysine \rightleftharpoons ADP + [protein]-N6-(3-O-phospho-D-fructosyl)-L-lysine Nonenzymatic glycation is a factor in the pathogenesis of diabetes.
L-tryptophan—pyruvate aminotransferase (, TAA1 (gene), vt2 (gene)) is an enzyme with systematic name L-tryptophan:pyruvate aminotransferase. This enzyme catalyses the following chemical reaction : L-tryptophan + pyruvate \rightleftharpoons indole-3-pyruvate + L-alanine This plant enzyme, along with EC 1.14.13.168, indole-3-pyruvate monooxygenase, is responsible for the biosynthesis of the plant hormone indole-3-acetate from L-tryptophan.
23S rRNA (cytidine1920-2'-O)-methyltransferase (, TlyA) is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (cytidine1920-2'-O)-methyltransferase. This enzyme catalyses the following chemical reaction : S-adenosyl-L-methionine + cytidine1920 in 23S rRNA \rightleftharpoons S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA This is a bifunctional enzyme from Mycobacterium tuberculosis.
Molybdopterin-synthase adenylyltransferase (, MoeB, adenylyltransferase and sulfurtransferase MOCS3) is an enzyme with systematic name ATP:molybdopterin- synthase adenylyltransferase. This enzyme catalyses the following chemical reaction : ATP + [molybdopterin-synthase sulfur-carrier protein]-Gly-Gly \rightleftharpoons diphosphate + [molybdopterin-synthase sulfur-carrier protein]-Gly-Gly-AMP This enzyme adenylates the C-terminus of the small subunit of the molybdopterin synthase.
UDP-N-acetylgalactosamine diphosphorylase () is an enzyme with systematic name UTP:N-acetyl-alpha-D-galactosamine-1-phosphate uridylyltransferase. This enzyme catalyses the following chemical reaction : UTP + N-acetyl-alpha-D- galactosamine 1-phosphate \rightleftharpoons diphosphate + UDP-N-acetyl-alpha- D-galactosamine The enzyme from plants and animals also acts on N-acetyl- alpha-D-glucosamine 1-phosphate.
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.
Acetylajmaline esterase (, AAE, 2beta(R)-17-O-acetylajmalan:acetylesterase, acetylajmalan esterase) is an enzyme with systematic name 17-O-acetylajmaline O-acetylhydrolase. This enzyme catalyses the following chemical reaction : (1) 17-O-acetylajmaline + H2O \rightleftharpoons ajmaline + acetate : (2) 17-O-acetylnorajmaline + H2O \rightleftharpoons norajmaline + acetate This plant enzyme mediates the last stages in the biosynthesis of the indole alkaloid ajmaline.
Demethylspheroidene O-methyltransferase (, 1-hydroxycarotenoid O-methylase, 1-hydroxycarotenoid methylase, 1-HO-carotenoid methylase, CrtF) is an enzyme with systematic name S-adenosyl-L-methionine:demethylspheroidene O-methyltransferase. This enzyme catalyses the following chemical reaction : S-adenosyl-L-methionine + demethylspheroidene \rightleftharpoons S-adenosyl-L- homocysteine + spheroidene In Rhodopseudomonas capsulata and Rubrivivax gelatinosus the enzyme is involved in biosynthesis of spheroidene.
TRNASer (uridine44-2'-O)-methyltransferase (, TRM44) is an enzyme with systematic name S-adenosyl-L-methionine:tRNASer (uridine44-2'-O)-methyltransferase. This enzyme catalyses the following chemical reaction : S-adenosyl-L-methionine + uridine44 in tRNASer \rightleftharpoons S-adenosyl-L-homocysteine + 2'-O-methyluridine44 in tRNASer The 2'-O-methylation of uridine44 contributes to stability of tRNASer(CGA).
In biochemistry, a synthase is an enzyme that catalyses a synthesis process. Following the EC number classification, they belong to the group of lyases. Note that, originally, biochemical nomenclature distinguished synthetases and synthases. Under the original definition, synthases do not use energy from nucleoside triphosphates (such as ATP, GTP, CTP, TTP, and UTP), whereas synthetases do use nucleoside triphosphates.
Glucan 1,4-alpha-maltotriohydrolase (, exo-maltotriohydrolase, maltotriohydrolase, 1,4-alpha-D-glucan maltotriohydrolase) is an enzyme with systematic name 4-alpha-D-glucan maltotriohydrolase. This enzyme catalyses the following chemical reaction : Hydrolysis of (1->4)-alpha-D-glucosidic linkages in amylaceous polysaccharides, to remove successive maltotriose residues from the non-reducing chain ends The products have the alpha-configuration.
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.
UDP-N,N'-diacetylbacillosamine 2-epimerase (hydrolysing) (, UDP-Bac2Ac4Ac 2-epimerase, NeuC) is an enzyme with systematic name UDP-N,N'-diacetylbacillosamine hydrolase (2-epimerising). This enzyme catalyses the following chemical reaction : UDP-N,N'-diacetylbacillosamine + H2O \rightleftharpoons UDP + 2,4-diacetamido-2,4,6-trideoxy-D-mannopyranose This enzyme requires Mg2+. It is involved in biosynthesis of legionaminic acid.
Fructan beta-fructosidase (, exo-beta-D-fructosidase, exo-beta-fructosidase, polysaccharide beta-fructofuranosidase, fructan exohydrolase) is an enzyme with systematic name beta-D-fructan fructohydrolase. This enzyme catalyses the following chemical reaction : Hydrolysis of terminal, non-reducing (2->1)- and (2->6)-linked beta-D-fructofuranose residues in fructans Hydrolyses inulin and levan, and also sucrose.
Mycodextranase (, 1,3-1,4-alpha-D-glucan 4-glucanohydrolase) is an enzyme with systematic name (1->3)-(1->4)-alpha-D-glucan 4-glucanohydrolase. This enzyme catalyses the following chemical reaction : Endohydrolysis of (1->4)-alpha-D- glucosidic linkages in alpha-D-glucans containing both (1->3)- and (1->4)-bonds Products are nigerose and 4-alpha-D-nigerosylglucose.
Glucuronoarabinoxylan endo-1,4-beta-xylanase (, feraxan endoxylanase, feraxanase, endoarabinoxylanase, glucuronoxylan xylohydrolase, glucuronoxylanase, glucuronoxylan xylanohydrolase, glucuronoarabinoxylan 1,4-beta-D-xylanohydrolase) is an enzyme with systematic name glucuronoarabinoxylan 4-beta-D-xylanohydrolase. This enzyme catalyses the following chemical reaction : Endohydrolysis of (1->4)-beta-D-xylosyl links in some glucuronoarabinoxylans This enzyme has high activity towards feruloylated arabinoxylans.
Iota-carrageenase () is an enzyme with systematic name iota-carrageenan 4-beta-D-glycanohydrolase (configuration-inverting). This enzyme catalyses the following chemical reaction : Endohydrolysis of (1->4)-beta-D-linkages between D-galactose 4-sulfate and 3,6-anhydro-D-galactose-2-sulfate in iota- carrageenans The main products of hydrolysis are iota-neocarratetraose sulfate and iota-neocarrahexaose sulfate.
Glucan 1,6-alpha-glucosidase (, exo-1,6-beta-glucosidase, glucodextrinase, glucan alpha-1,6-D-glucohydrolase) is an enzyme with systematic name glucan 6-alpha-D-glucohydrolase. This enzyme catalyses the following chemical reaction: : Hydrolysis of (1->6)-alpha-D-glucosidic linkages in (1->6)-alpha- D-glucans and derived oligosaccharides Hydrolysis is accompanied by inversion at C-1.
Capsular-polysaccharide endo-1,3-alpha-galactosidase (, polysaccharide depolymerase, capsular polysaccharide galactohydrolase) is an enzyme with systematic name Aerobacter-capsular-polysaccharide galactohydrolase. This enzyme catalyses the following chemical reaction : Random hydrolysis of (1->3)-alpha-D-galactosidic linkages in Aerobacter aerogenes capsular polysaccharide Hydrolyses the galactosyl-alpha-1,3-D-galactose linkages only in the complex substrate, bringing about depolymerization.
Glucan 1,4-alpha-maltohexaosidase (, exo-maltohexaohydrolase, 1,4-alpha-D- glucan maltohexaohydrolase) is an enzyme with systematic name 4-alpha-D-glucan maltohexaohydrolase. This enzyme catalyses the following chemical reaction : Hydrolysis of (1->4)-alpha-D-glucosidic linkages in amylaceous polysaccharides, to remove successive maltohexaose residues from the non- reducing chain ends The products have the alpha-configuration.
Membrane dipeptidase (, renal dipeptidase, dehydropeptidase I (DPH I), dipeptidase, aminodipeptidase, dipeptide hydrolase, dipeptidyl hydrolase, nonspecific dipeptidase, glycosyl-phosphatidylinositol-anchored renal dipeptidase, MBD, MDP, leukotriene D4 hydrolase) is an enzyme. This enzyme catalyses the following chemical reaction : Hydrolysis of dipeptides (e.g., leukotriene D4, cystinyl-bis-glycine, some β-lactam antibiotics (e.g., carbapenem)) This membrane-bound, zinc enzyme has broad specificity.
Aminopeptidase S (, Mername-AA022 peptidase, SGAP, aminopeptidase (Streptomyces griseus), Streptomyces griseus aminopeptidase, S. griseus AP, double-zinc aminopeptidase) is an enzyme. This enzyme catalyses the following chemical reaction : Release of an N-terminal amino acid with a preference for large hydrophobic amino-terminus residues This enzyme contains two zinc molecules in its active site and is activated by Ca2+.
Beta-peptidyl aminopeptidase (, BapA) is an enzyme. This enzyme catalyses the following chemical reaction : Cleaves N-terminal beta-homoamino acids from peptides composed of 2 to 6 amino acids Sphingosinicella xenopeptidilytica strain 3-2W4 could use beta-peptides beta-homoVal-beta-homoAla-beta-homoLeu and beta-homoAla-beta-homoLeu as only source of carbon and energy.
AntM catalyses the reduction of the β-keto group, which precedes the AntD TE domain – promoted release of the nine- membered dilactone 8\. A lipase homologue, AntO, and acyltransferase homologue, AntB, catalyze the installation of the N-formyl group and the transesterification of the C-8 hydroxyl group, respectively, resulting in the backbone for the Antimycin family.
Pyrrolysine—tRNAPyl ligase (, PylS, pyrrolysyl-tRNA synthetase) is an enzyme with systematic name L-pyrrolysine:tRNAPyl ligase (AMP-forming). This enzyme catalyses the following chemical reaction : ATP + L-pyrrolysine + tRNAPyl \rightleftharpoons AMP + diphosphate + L-pyrrolysyl-tRNAPyl This enzyme is specific for pyrrolysine as substrate as it cannot be replaced by lysine or any of the other natural amino acids.
Ribonuclease M5 (, RNase M5, 5S ribosomal maturation nuclease, 5S ribosomal RNA maturation endonuclease) is an enzyme. This enzyme catalyses the following chemical reaction : Endonucleolytic cleavage of RNA, removing 21 and 42 nucleotides, respectively, from the 5'- and 3'-termini of a 5S-rRNA precursor This enzyme converts the 5S-rRNA precursor from Bacillus subtilis into 5S-rRNA.
Diacylglycerol diphosphate phosphatase (, DGPP phosphatase, DGPP phosphohydrolase, DPP1, DPPL1, DPPL2, PAP2, pyrophosphate phosphatase) is an enzyme with systematic name 1,2-diacyl-sn-glycerol 3-phosphate phosphohydrolase. This enzyme catalyses the following chemical reaction : 1,2-diacyl-sn-glycerol 3-diphosphate + H2O \rightleftharpoons 1,2-diacyl-sn- glycerol 3-phosphate + phosphate The phosphatase activity of this enzyme is Mg2+-independent.
N-acetylphosphatidylethanolamine-hydrolysing phospholipase D (, NAPE-PLD, anandamide-generating phospholipase D, N-acyl phosphatidylethanolamine phospholipase D, NAPE-hydrolyzing phospholipase D) is an enzyme with systematic name N-acetylphosphatidylethanolamine phosphatidohydrolase. This enzyme catalyses the following chemical reaction : N-acylphosphatidylethanolamine + H2O \rightleftharpoons N-acylethanolamine + a 1,2-diacylglycerol 3-phosphate This enzyme is involved in the biosynthesis of anandamide.
This enzyme participates in streptomycin biosynthesis and inositol phosphate metabolism. It employs one cofactor, NAD+. The reaction this enzyme catalyses represents the first committed step in the production of all inositol-containing compounds, including phospholipids, either directly or by salvage. The enzyme exists in a cytoplasmic form in a wide range of plants, animals, and fungi.
M. bovis is similar in structure and metabolism to M. tuberculosis. M. bovis is a Gram- positive, acid-fast, rod-shaped, aerobic bacteria. Unlike M. tuberculosis, M. bovis lacks pyruvate kinase activity, due to pykA containing a point mutation that affects binding of Mg2+ cofactor. Pyruvate kinase catalyses the final step of glycolysis, the dephosphorylation of phosphorenolpyruvate to pyruvate.
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.
Flavivirin (, Yellow fever virus (flavivirus) protease, NS2B-3 proteinase) is an enzyme. This enzyme catalyses the following chemical reaction : Selective hydrolysis of -Xaa-Xaa-Yaa- bonds in which each of the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala This enzyme is present in classical flaviviruses (yellow fever, dengue fever).
Caricain (, papaya peptidase A, papaya peptidase II, papaya proteinase, papaya proteinase III, papaya proteinase 3, proteinase omega, papaya proteinase A, chymopapain S, Pp) is an enzyme. This enzyme catalyses the following chemical reaction : Hydrolysis of proteins with broad specificity for peptide bonds, similar to those of papain and chymopapain This enzyme is isolated from papaya plant, Carica papaya.
L-peptidase () is an enzyme. This enzyme catalyses the following chemical reaction : Autocatalytically cleaves itself from the polyprotein of the foot- and-mouth disease virus by hydrolysis of a Lys-Gly bond. Subsequently, it cleaves host cell initiation factor eIF-4G at bonds -Gly-Arg- and -Lys-Arg- This enzyme is coded bz foot-and-mouth disease virus.
Histolysain (, histolysin, Entamoeba histolytica cysteine proteinase, amebapain, Entamoeba histolytica cysteine protease, Entamoeba histolytica neutral thiol proteinase) is an enzyme. This enzyme catalyses the following chemical reaction : Hydrolysis of proteins, including basement membrane collagen and azocasein. Preferential cleavage: Arg-Arg- in small molecule substrates including Z-Arg-Arg-!NHMec This enzyme is present in the protozoan, Entamoeba histolytica.
Adenain () is an enzyme. This enzyme catalyses the following chemical reaction : Cleaves proteins of the adenovirus and its host cell at two consensus sites: -Yaa-Xaa-Gly-Gly-Xaa- and -Yaa-Xaa-Gly-Xaa-Gly- (in which Yaa is Met, Ile or Leu, and Xaa is any amino acid) This cysteine endopeptidase is coded by adenoviruses.
Ornithine carbamoyltransferase (OTCase) catalyses the conversion of ornithine and carbamoyl phosphate to citrulline. In mammals this enzyme participates in the urea cycle and is located in the mitochondrial matrix. In prokaryotes and eukaryotic microorganisms it is involved in the biosynthesis of arginine. In some bacterial species it is also involved in the degradation of arginine (the arginine deaminase pathway).
Cathepsin X (, cathepsin B2, cysteine-type carboxypeptidase, cathepsin IV, cathepsin Z, acid carboxypeptidase, lysosomal carboxypeptidase B) is an enzyme. This enzyme catalyses the following chemical reaction : Release of C-terminal amino acid residues with broad specificity, but lacks action on C-terminal proline. Shows weak endopeptidase activity Cathepsin X is a lysosomal cysteine peptidase of family C1 (papain family).
Adamalysin (, Crotalus adamanteus metalloendopeptidase, proteinase I and II, Crotalus adamanteus venom proteinase II, adamalysin II) is an enzyme. This enzyme catalyses the following chemical reaction : Cleavage of Phe1-Val, His5-Leu, His10-Leu, Ala14-Leu, Leu15-Tyr, and Tyr16-Leu of insulin B chain This enzyme is present in the venom of the eastern diamondback rattlesnake (Crotalus adamanteus).
Endo-α-N-acetylgalactosaminidase (, endo-α-acetylgalactosaminidase, endo-α-N- acetyl-D-galactosaminidase, mucinaminylserine mucinaminidase, D-galactosyl-3-(N-acetyl-α-D-galactosaminyl)-L-serine mucinaminohydrolase, endo-α-GalNAc-ase, D-galactosyl-N-acetyl-α-D-galactosamine D-galactosyl-N- acetyl-galactosaminohydrolase) is an enzyme with systematic name glycopeptide- D-galactosyl-N-acetyl-α-D-galactosamine D-galactosyl-N-acetyl- galactosaminohydrolase. This enzyme catalyses the following chemical reaction : 3-O-beta-D-galactosyl-N-acetyl-alpha-D-galactosaminyl-L-serine-[protein] + H2O \rightleftharpoons 3-O-beta-D-galactosyl-N-acetyl-alpha-D-galactosamine + L-serine-[protein] The enzyme catalyses the release of Gal-(1->3)-beta-GalNAc alpha-linked to serine or threonine residues of mucin-type glycoproteins. Glycopeptide α-N-acetylgalactosaminidases belong to family GH101 of glycoside hydrolases.
16S rRNA (guanine966-N2)-methyltransferase (, yhhF (gene), rsmD (gene), m2G966 methyltransferase) is an enzyme with systematic name S-adenosyl-L- methionine:16S rRNA (guanine966-N2)-methyltransferase. This enzyme catalyses the following chemical reaction : S-adenosyl-L-methionine + guanine966 in 16S rRNA \rightleftharpoons S-adenosyl-L-homocysteine + N2-methylguanine966 in 16S rRNA The enzyme efficiently methylates guanine966 of the assembled 30S subunits in vitro.
16S rRNA (cytosine967-C5)-methyltransferase (, rsmB (gene), fmu (gene), 16S rRNA m5C967 methyltransferase) is an enzyme with systematic name S-adenosyl-L- methionine:16S rRNA (cytosine967-C5)-methyltransferase. This enzyme catalyses the following chemical reaction : S-adenosyl-L-methionine + cytosine967 in 16S rRNA \rightleftharpoons S-adenosyl-L-homocysteine + 5-methylcytosine967 in 16S rRNA The enzyme specifically methylates cytosine967 at C5 in 16S rRNA.
16S rRNA (cytosine1407-C5)-methyltransferase (, RNA m5C methyltransferase YebU, RsmF, YebU) is an enzyme with systematic name S-adenosyl-L- methionine:16S rRNA (cytosine1407-C5)-methyltransferase. This enzyme catalyses the following chemical reaction : S-adenosyl-L-methionine + cytosine1407 in 16S rRNA \rightleftharpoons S-adenosyl-L-homocysteine + 5-methylcytosine1407 in 16S rRNA The enzyme specifically methylates cytosine1407 at C5 in 16S rRNA.
16S rRNA (uracil1498-N3)-methyltransferase (, DUF558 protein, YggJ, RsmE, m3U1498 specific methyltransferase) is an enzyme with systematic name S-adenosyl-L-methionine:16S rRNA (uracil1498-N3)-methyltransferase. This enzyme catalyses the following chemical reaction : S-adenosyl-L-methionine + uracil1498 in 16S rRNA \rightleftharpoons S-adenosyl-L-homocysteine + N3-methyluracil1498 in 16S rRNA The enzyme specifically methylates uracil1498 at N3 in 16S rRNA.
23S rRNA (adenine2503-C2,C8)-dimethyltransferase (, Cfr, Cfr methyltransferase, Cfr rRNA methyltransferase) is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (adenine2503-C2,C8)-dimethyltransferase. This enzyme catalyses the following chemical reaction : 2 S-adenosyl-L- methionine + adenine2503 in 23S rRNA \rightleftharpoons 2 S-adenosyl-L- homocysteine + 2,8-dimethyladenine2503 in 23S rRNA This enzyme contains an [4Fe-S] cluster.
23S rRNA (uracil747-C5)-methyltransferase (, YbjF, RumB, RNA uridine methyltransferase B) is an enzyme with systematic name S-adenosyl-L- methionine:23S rRNA (uracil747-C5)-methyltransferase. This enzyme catalyses the following chemical reaction : S-adenosyl-L-methionine + uracil747 in 23S rRNA \rightleftharpoons S-adenosyl-L-homocysteine + 5-methyluracil747 in 23S rRNA The enzyme specifically methylates uracil747 at C5 in 23S rRNA.
23S rRNA (uracil1939-C5)-methyltransferase (, RumA, RNA uridine methyltransferase A, YgcA) is an enzyme with systematic name S-adenosyl-L- methionine:23S rRNA (uracil1939-C5)-methyltransferase. This enzyme catalyses the following chemical reaction : S-adenosyl-L-methionine + uracil1939 in 23S rRNA \rightleftharpoons S-adenosyl-L-homocysteine + 5-methyluracil1939 in 23S rRNA The enzyme specifically methylates uracil1939 at C5 in 23S rRNA.
23S rRNA (cytosine1962-C5)-methyltransferase (, RlmI, rRNA large subunit methyltransferase I, YccW) is an enzyme with systematic name S-adenosyl-L- methionine:23S rRNA (cytosine1962-C5)-methyltransferase. This enzyme catalyses the following chemical reaction : S-adenosyl-L-methionine + cytosine1962 in 23S rRNA \rightleftharpoons S-adenosyl-L-homocysteine + 5-methylcytosine1962 in 23S rRNA The enzyme specifically methylates cytosine1962 at C5 in 23S rRNA.
23S rRNA (adenine2503-C2)-methyltransferase (, RlmN, YfgB, Cfr) is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (adenine2503-C2)-methyltransferase. This enzyme catalyses the following chemical reaction : 2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA \rightleftharpoons S-adenosyl-L-homocysteine \+ L-methionine + 5'-deoxyadenosine + 2-methyladenine2503 in 23S rRNA 23S rRNA (adenine2503-C2)-methyltransferase contains an [4Fe-4S] cluster.
TRNA (cytosine34-C5)-methyltransferase (, hTrm4 Mtase, hTrm4 methyltransferase, hTrm4 (gene), tRNA:m5C-methyltransferase) is an enzyme with systematic name S-adenosyl-L-methionine:tRNA (cytosine34-C5)-methyltransferase. This enzyme catalyses the following chemical reaction : S-adenosyl-L-methionine + cytosine34 in tRNA precursor \rightleftharpoons S-adenosyl-L-homocysteine + 5-methylcytosine34 in tRNA precursor The human enzyme is specific for C5-methylation of cytosine34 in tRNA precursors.
Adenosine phosphate-isopentenyltransferase (IPT) catalyses the first reaction in the biosynthesis of isoprene cytokinins. It may use ATP, ADP, or AMP as substrates and may use dimethylallyl pyrophosphate (DMAPP) or hydroxymethylbutenyl pyrophosphate (HMBPP) as prenyl donors. This reaction is the rate-limiting step in cytokinin biosynthesis. DMADP and HMBDP used in cytokinin biosynthesis are produced by the methylerythritol phosphate pathway (MEP).
Hydroxylamine dehydrogenase (, HAO (ambiguous)) is an enzyme with systematic name hydroxylamine:ferricytochrome-c oxidoreductase. This enzyme catalyses the following chemical reaction : (1) hydroxylamine + H2O + 2 ferricytochrome c \rightleftharpoons nitrite + 2 ferrocytochrome c + 5 H+ : (2) hydroxylamine + ferricytochrome c \rightleftharpoons nitric oxide + ferrocytochrome c + 3 H+ The enzymes from the nitrifying bacterium Nitrosomonas europaea and the methylotrophic bacterium Methylococcus capsulatus are hemoproteins.
Plastoquinol/plastocyanin reductase (, plastoquinol/plastocyanin oxidoreductase, cytochrome f/b6 complex) is an enzyme with systematic name plastoquinol:oxidized-plastocyanin oxidoreductase. This enzyme catalyses the following chemical reaction : plastoquinol + 2 oxidized plastocyanin + 2 H+ [side 1] \rightleftharpoons plastoquinone + 2 reduced plastocyanin + 2 H+ [side 2] Plastoquinol reductase contains two b-type cytochromes, two c-type cytochromes (cn and f), and a [2Fe-2S] Rieske cluster.
Deuterolysin (, Penicillium roqueforti protease II, microbial neutral proteinase II, acid metalloproteinase, neutral proteinase II, Penicillium roqueforti metalloproteinase) is an enzyme. This enzyme catalyses the following chemical reaction : Preferential cleavage of bonds with hydrophobic residues in P1'; also Asn3-Gln and Gly8-Ser bonds in insulin B chain This enzyme is present in Penicillium roqueforti, P. caseicolum, Pyricularia oryzae, Aspergillus sojae and A. oryzae.
Trimerelysin II (, Trimeresurus metalloendopeptidase II, proteinase H2, H2-proteinase) is an enzyme. This enzyme catalyses the following chemical reaction : Cleavage of Asn3-Gln, His10-Leu and Ala14-Leu in the insulin B chain, and the bond Z-Gly-Pro-Leu-Gly-Pro in a small molecule substrate of microbial collagenase This endopeptidase is present in the venom of the habu snake (Trimeresurus flavoviridis).
Beta-lytic metalloendopeptidase (, Myxobacter beta-lytic proteinase, achromopeptidase component, beta-lytic metalloproteinase, beta-lytic protease, Myxobacterium sorangium beta-lytic proteinase, Myxobacter495 beta-lytic proteinase) is an enzyme. This enzyme catalyses the following chemical reaction : Cleavage of N-acetylmuramoyl-Ala, and of the insulin B chain at Gly23-Phe > Val18-Cya This enzyme is present in Achromobacter lyticus and Lysobacter enzymogenes.
Ste24 endopeptidase () is an enzyme. This enzyme catalyses the following chemical reaction : The peptide bond hydrolysed can be designated -C-aaX in which C is an S-isoprenylated cysteine residue, a is usually aliphatic and X is the C-terminal residue of the substrate protein, and may be any of several amino acids This enzyme belongs to the peptidase family M48.
Proteasome endopeptidase complex (, ingensin, macropain, multicatalytic endopeptidase complex, prosome, multicatalytic proteinase (complex), MCP, proteasome, large multicatalytic protease, proteasome organelle, alkaline protease, 26S protease, tricorn proteinase, tricorn protease) is an enzyme. This enzyme catalyses the following chemical reaction : Cleavage of peptide bonds with very broad specificity This 20-S protein is composed of 28 subunits arranged in four rings of seven.
Flavastacin () is an enzyme. This enzyme catalyses the following chemical reaction : Hydrolyses polypeptides on the amino-side of Asp in -Xaa-Asp-. Acts very slowly on -Xaa-Glu This zinc metalloendopeptidase belong to the peptidase family M12. It has recently been described as cleaving specifically after N-glycosylated asparagine, making it a potentially useful as a tool to analytically characterize glycoproteins.
2-Amino-4-deoxychorismate dehydrogenase (, ADIC dehydrogenase, 2-amino-2-deoxyisochorismate dehydrogenase, SgcG) is an enzyme with systematic name (2S)-2-amino-4-deoxychorismate:FMN oxidoreductase. This enzyme catalyses the following chemical reaction : (2S)-2-amino-4-deoxychorismate + FMN \rightleftharpoons 3-(1-carboxyvinyloxy)anthranilate + FMNH2 This enzyme participates in the formation of the benzoxazolinate moiety of the enediyne antitumour antibiotic C-1027].
1-Hydroxycarotenoid 3,4-desaturase (, CrtD, hydroxyneurosporene desaturase, carotenoid 3,4-dehydrogenase, 1-hydroxy-carotenoid 3,4-dehydrogenase) is an enzyme with systematic name 1-hydroxy-1,2-dihydrolycopene:acceptor oxidoreductase. This enzyme catalyses the following chemical reaction : 1-hydroxy-1,2-dihydrolycopene + acceptor \rightleftharpoons 1-hydroxy-3,4-didehydro-1,2-dihydrolycopene + reduced acceptor The enzymes from Rubrivivax gelatinosus and Rhodobacter sphaeroides acts primarily on acyclic carotenoids.
3-dehydroquinate synthase II (, DHQ synthase II, MJ1249 (gene), aroB' (gene)) is an enzyme with systematic name 2-amino-3,7-dideoxy-D-threo- hept-6-ulosonate:NAD+ oxidoreductase (deaminating). This enzyme catalyses the following chemical reaction : 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate + H2O + NAD+ \rightleftharpoons 3-dehydroquinate + NH3 \+ NADH + H+ The enzyme was isolated from the archaeon Methanocaldococcus jannaschii.
6-hydroxypseudooxynicotine dehydrogenase () is an enzyme with systematic name 1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one:acceptor 6-oxidoreductase (hydroxylating). This enzyme catalyses the following chemical reaction: : 1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + acceptor + H2O \rightleftharpoons 1-(2,6-dihydroxypyridin-3-yl)-4-(methylamino)butan-1-one + reduced acceptor This enzyme contains a cytidylyl molybdenum cofactor.
Glycolipid transfer protein is a cytosolic protein that catalyses the transfer of glycolipids between different intracellular membranes. It was discovered by Raymond J. Metz and Norman S. Radin in 1980 and partially purified and characterized in 1982. Recent reviews on structure and possible function are available. This protein transports primarily different glycosphingolipids and glyceroglycolipids between intracellular membranes, but not phospholipids.
Clavaminate synthase (, clavaminate synthase 2, clavaminic acid synthase) is an enzyme with systematic name deoxyamidinoproclavaminate,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating). This enzyme catalyses the following chemical reaction :(1) deoxyamidinoproclavaminate + 2-oxoglutarate + O2 \rightleftharpoons amidinoproclavaminate + succinate + CO2 :(2) proclavaminate + 2-oxoglutarate + O2 \rightleftharpoons dihydroclavaminate + succinate + CO2 \+ H2O :(3) dihydroclavaminate + 2-oxoglutarate + O2 \rightleftharpoons clavaminate + succinate + CO2 \+ H2O Clavaminate synthase contains nonheme iron.
Xylogalacturonan beta-1,3-xylosyltransferase (, xylogalacturonan xylosyltransferase, XGA xylosyltransferase) is an enzyme with systematic name UDP-D-xylose:xylogalacturonan 3-beta-D-xylosyltransferase. This enzyme catalyses the following chemical reaction : Transfers a xylosyl residue from UDP-D-xylose to a D-galactose residue in xylogalacturonan, forming a beta-1,3-D-xylosyl-D-galactose linkage. This enzyme is involved in plant cell wall synthesis.
2-deoxystreptamine N-acetyl-D-glucosaminyltransferase (, btrM (gene), neoD (gene), kanF (gene)) is an enzyme with systematic name UDP-N-acetyl-alpha-D- glucosamine:2-deoxystreptamine N-acetyl-D-glucosaminyltransferase. This enzyme catalyses the following chemical reaction : UDP-N-acetyl-alpha-D-glucosamine + 2-deoxystreptamine \rightleftharpoons UDP + 2'-N-acetylparomamine Involved in the biosynthetic pathways of several clinically important aminocyclitol antibiotics.
Sulfur dioxygenase (, sulfur oxygenase, sulfur:oxygen oxidoreductase) is an enzyme with systematic name S-sulfanylglutathione:oxygen oxidoreductase. This enzyme catalyses the following chemical reaction : sulfur + O2 \+ H2O \rightleftharpoons sulfite + 2 H+ (overall reaction) : (1a) glutathione + sulfur \rightleftharpoons S-sulfanylglutathione (spontaneous reaction) : (1b) S-sulfanylglutathione + O2 \+ H2O \rightleftharpoons glutathione + sulfite + 2 H+ This enzyme contains iron. In humans, sulfur dioxygenase is needed to detoxify sulfide.
Globotriosylceramide beta-1,6-N-acetylgalactosaminyl-transferase (, globoside N-acetylgalactosaminyltransferase, uridine diphosphoacetylgalactosamine- glycosphingolipid acetylgalactosaminyltransferase, glycosphingolipid beta-N- acetylgalactosaminyltransferase, GalNAc transferase) is an enzyme with systematic name UDP-N-acetyl-D-galactosamine-globotriosylceramide beta-1,6-N-acetylgalactosaminyltransferase. This enzyme catalyses the following chemical reaction : UDP-N-acetyl-D-galactosamine + globotriosylceramide \rightleftharpoons UDP + globotetraosylceramide The product has a terminal beta-N-acetylgalactosamine residue.
N-acetylneuraminylgalactosylglucosylceramide beta-1,4-N-acetylgalactosaminyltransferase (, is an enzyme that catalyses the following chemical reaction: : UDP-N-acetyl-D-galactosamine + N-acetylneuraminyl-(2->3)-alpha-D-galactosyl-(1->4)-beta-D- glucosyl-(1<->1)-ceramide \rightleftharpoons UDP + N-acetyl-D- galactosaminyl-(1->4)-beta-N-acetylneuraminyl-(2->3)-alpha-D- galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide This enzyme requires Mn2+.
Wilkinson's catalyst, based on the transition metal rhodium, also effectively catalyses PK reactions but requires silver triflate as a co-catalyst.Nakcheol Jeong, Byung Ki Sung, Jin Sung Kim, Soon Bong Park,Sung Deok Seo, Jin Young Shin, Kyu Yeol In, Yoon Kyung Choi Pauson–Khand-type reaction mediated by Rh(I) catalysts Pure Appl. Chem., Vol. 74, No. 1, pp.
8'-apo-beta-carotenoid 14',13'-cleaving dioxygenase () is an enzyme with systematic name 8'-apo-beta-carotenol:O2 oxidoreductase (14',13'-cleaving). This enzyme catalyses the following chemical reaction : 8'-apo-beta-carotenol + O2 \rightleftharpoons 14'-apo-beta-carotenal + an uncharacterized product 8'-apo-beta-carotenoid 14',13'-cleaving dioxygenase is a thiol-dependent enzyme isolated from rat and rabbit.
All-trans-10'-apo-beta-carotenal 13,14-cleaving dioxygenase (, CCD8 (gene), MAX4 (gene), NCED8 (gene)) is an enzyme with systematic name all- trans-10'-apo-beta-carotenal:O2 oxidoreductase (13,14-cleaving). This enzyme catalyses the following chemical reaction : all-trans-10'-apo-beta-carotenal + O2 \rightleftharpoons 13-apo-beta-carotenone + (2E,4E,6E)-4-methylocta-2,4,6-trienedial The enzyme contains Fe2+.
Abscisate beta-glucosyltransferase (, ABA-glucosyltransferase, ABA-GTase, AOG) is an enzyme with systematic name UDP-D-glucose:abscisate beta-D- glucosyltransferase. This enzyme catalyses the following chemical reaction : UDP-D-glucose + abscisate \rightleftharpoons UDP + beta-D-glucopyranosyl abscisate The enzyme acts better on (S)-2-trans-abscisate than the natural (S)-2-cis isomer, abscisate, or its enantiomer, the (R)-2-cis isomer.
Prepilin peptidase () is an enzyme. This enzyme catalyses the following chemical reaction : Typically cleaves a -Gly-Phe- bond to release an N-terminal, basic peptide of 5-8 residues from type IV prepilin, and then N-methylates the new N-terminal amino group, the methyl donor being S-adenosyl-L-methionine. This enzyme is present on the surface of many species of bacteria.
3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase (, paaZ (gene)) is an enzyme with systematic name 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde:NADP+ oxidoreductase. This enzyme catalyses the following chemical reaction : 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde + NADP+ \+ H2O \rightleftharpoons 3-oxo-5,6-dehydrosuberyl-CoA + NADPH + H+ The enzyme from Escherichia coli is a bifunctional protein that also acts as EC 3.7.1.16, oxepin-CoA hydrolase.
Previous studies have demostrated that treatment of mouse oocytes with IMPDH inhibitors induced gonadotropin-independent meiotic resumption in vivo. IMPDH is a rate limiting enzyme that catalyses IMP to xanthosine monophosphate (XMP). It can induce meiotic resumption as XMP produced is ultimately be converted to cGMP through a series of enzymatic activities. In addition, IMPDH maintains hypoxanthine (HX) levels in the follicular fluid.
Indolin-2-one monooxygenase (, BX3 (gene), CYP71C2 (gene)) is an enzyme with systematic name indolin-2-one,NAD(P)H:oxygen oxidoreductase (3-hydroxylating). This enzyme catalyses the following chemical reaction : indolin-2-one + NAD(P)H + H+ \+ O2 \rightleftharpoons 3-hydroxyindolin-2-one + NAD(P)+ \+ H2O Indolin-2-one monooxygenase is involved in the biosynthesis of protective and allelopathic benzoxazinoids in some plants.
3-ketosteroid 9alpha-monooxygenase (, KshAB, 3-ketosteroid 9alpha-hydroxylase) is an enzyme with systematic name androsta-1,4-diene-3,17-dione,NADH:oxygen oxidoreductase (9alpha-hydroxylating). This enzyme catalyses the following chemical reaction : androsta-1,4-diene-3,17-dione + NADH + H+ \+ O2 \rightleftharpoons 9alpha-hydroxyandrosta-1,4-diene-3,17-dione + NAD+ \+ H2O 3-Ketosteroid 9alpha-monooxygenase is involved in the cholesterol degradation in several bacterial pathogens.
S-specific spore photoproduct lyase (, SAM, SP lyase, SPL, SplB, SplG) is an enzyme with systematic name S-specific spore photoproduct pyrimidine-lyase. This enzyme catalyses the following chemical reaction : (5S)-5,6-dihydro-5-(thymidin-7-yl)thymidine (in DNA) + S-adenosyl-L-methionine \rightleftharpoons thymidylyl-(3'->5')-thymidylate (in DNA) + 5'-deoxyadenosine + L-methionine This enzyme is an iron-sulfur protein.
Sodium phosphorothiolate decomposes at neutral pH. Silicone grease catalyses the hydrolysis of the phosphorothioate ion, so it is recommended that it is not used in the glass joints. In the anhydrous material, the P-S bond is 211 pm and the three equivalent P-O bonds are short at 151 pm. These disparate values suggest that the P-S bond is single.
Stemar-13-ene synthase (, OsDTC2, OsK8, OsKL8, OsKS8, stemarene synthase, syn- stemar-13-ene synthase) is an enzyme with systematic name 9alpha-copalyl- diphosphate diphosphate-lyase (stemar-13-ene-forming). This enzyme catalyses the following chemical reaction : 9alpha-copalyl diphosphate \rightleftharpoons stemar-13-ene + diphosphate This diterpene cyclase produces stemar-13-ene, a putative precursor of the rice phytoalexin oryzalexin S.
Alpha-bisabolene synthase (, bisabolene synthase) is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate diphosphate-lyase ((E)-alpha-bisabolene- forming). This enzyme catalyses the following chemical reaction : (2E,6E)-farnesyl diphosphate \rightleftharpoons (E)-alpha-bisabolene + diphosphate This synthase requires a divalent cation cofactor (Mg2+ or, to a lesser extent, Mn2+) to neutralize the negative charge of the diphosphate leaving group.
Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase (, PHS1 (gene), PAS2 (gene)) is an enzyme with systematic name very-long-chain (3R)-3-hydroxyacyl- CoA hydro-lyase. This enzyme catalyses the following chemical reaction : a very-long-chain (3R)-3-hydroxyacyl-CoA \rightleftharpoons a very-long-chain trans-2,3-dehydroacyl-CoA + H2O This is the third component of the elongase.
5-phosphonooxy-L-lysine phospho-lyase (, 5-phosphohydroxy-L-lysine ammoniophospholyase, AGXT2L2 (gene)) is an enzyme with systematic name (5R)-5-phosphonooxy-L-lysine phosphate-lyase (deaminating; (S)-2-amino-6-oxohexanoate-forming). This enzyme catalyses the following chemical reaction : (5R)-5-phosphonooxy-L-lysine + H2O \rightleftharpoons (S)-2-amino-6-oxohexanoate + NH3 \+ phosphate This enzyme is a pyridoxal- phosphate protein.
Cis-abienol synthase (, Z-abienol synthase, CAS, ABS) is an enzyme with systematic name (13E)-8alpha-hydroxylabd-13-en-15-yl-diphosphate-lyase (cis- abienol forming). This enzyme catalyses the following chemical reaction : (13E)-8alpha-hydroxylabd-13-en-15-yl diphosphate \rightleftharpoons cis- abienol + diphosphate This enzyme is isolated from the plants Abies balsamea (balsam fir) and Nicotiana tabacum (tobacco).
Labdatriene synthase (, OsKSL10 (gene)) is an enzyme with systematic name 9alpha-copalyl-diphosphate diphosphate-lyase ((12E)-9alpha- labda-8(17),12,14-triene-forming). This enzyme catalyses the following chemical reaction : 9alpha-copalyl diphosphate \rightleftharpoons (12E)-9alpha-labda-8(17),12,14-triene + diphosphate The enzyme from rice (Oryza sativa) also produces ent-sandaracopimara-8(14),15-diene from ent- copalyl diphosphate.
Phenylalanine/tyrosine ammonia-lyase (, PTAL, bifunctional PAL) is an enzyme with systematic name L-phenylalanine(or L-tyrosine):trans-cinnamate(or trans- p-hydroxycinnamate) ammonia-lyase. This enzyme catalyses the following chemical reaction : (1) L-phenylalanine \rightleftharpoons trans-cinnamate + NH3 : (2) L-tyrosine \rightleftharpoons trans-p-hydroxycinnamate + NH3 This enzyme is a member of the aromatic amino acid lyase family.
Endopeptidase Clp (, endopeptidase Ti, caseinolytic protease, protease Ti, ATP-dependent Clp protease, ClpP, Clp protease). This enzyme catalyses the following chemical reaction : Hydrolysis of proteins to small peptides in the presence of ATP and Mg2+. This bacterial enzyme contains subunits of two types, ClpP, with peptidase activity, and the protein ClpA, with AAA+ ATPase activity. ClpP and ClpA are not evolutionarily related.
NADP-retinol dehydrogenase (, all-trans retinal reductase, all-trans-retinol dehydrogenase, NADP(H)-dependent retinol dehydrogenase/reductase, RDH11, RDH12, RDH13, RDH14, retinol dehydrogenase 12, retinol dehydrogenase 14, retinol dehydrogenase (NADP+), RalR1, PSDR1) is an enzyme with systematic name retinol:NADP+ oxidoreductase. This enzyme catalyses the following chemical reaction : retinol + NADP+ \rightleftharpoons retinal + NADPH + H+ This enzyme has greater catalytic efficiency in the reductive direction.
Trans-2,3-dihydro-3-hydroxyanthranilate isomerase (, phzF (gene)) is an enzyme with systematic name (5S,6S)-6-amino-5-hydroxycyclohexane-1,3-diene-1-carboxyate isomerase. This enzyme catalyses the following chemical reaction : (5S,6S)-6-amino-5-hydroxycyclohexane-1,3-diene-1-carboxyate \rightleftharpoons (1R,6S)-6-amino-5-oxocyclohex-2-ene-1-carboxylate The enzyme is involved in phenazine biosynthesis.
D-threonine aldolase (, D-TA, DTA, low specificity D-TA, low specificity D-threonine aldolase) is an enzyme with systematic name D-threonine acetaldehyde-lyase (glycine-forming). This enzyme catalyses the following chemical reaction : (1) D-threonine \rightleftharpoons glycine + acetaldehyde : (2) D-allothreonine \rightleftharpoons glycine + acetaldehyde This pyridoxal-phosphate protein is activated by divalent metal cations (e.g. Co2+, Ni2+, Mn2+ or Mg2+).
L-olivosyl-oleandolide 3-O-methyltransferase (, OleY) is an enzyme with systematic name S-adenosyl-L-methionine:L-olivosyl-oleandolide B 3-O-methyltransferase. This enzyme catalyses the following chemical reaction : S-adenosyl-L-methionine + L-olivosyl-oleandolide \rightleftharpoons S-adenosyl-L-homocysteine + L-oleandrosyl-oleandolide The enzyme is involved in the biosynthesis of the macrolide antibiotic oleandomycin in Streptomyces antibioticus.
16S rRNA (guanine1516-N2)-methyltransferase (, yhiQ (gene), rsmJ (gene), m2G1516 methyltransferase) is an enzyme with systematic name S-adenosyl-L- methionine:16S rRNA (guanine1516-N2)-methyltransferase. This enzyme catalyses the following chemical reaction : S-adenosyl-L-methionine + guanine1516 in 16S rRNA \rightleftharpoons S-adenosyl-L-homocysteine + N2-methylguanine1516 in 16S rRNA The enzyme specifically methylates guanine1516 at N2 in 16S rRNA.
2-Ketoarginine methyltransferase (, mrsA (gene)) is an enzyme with systematic name S-adenosyl-L-methionine:5-carbamimidamido-2-oxopentanoate S-methyltransferase. This enzyme catalyses the following chemical reaction : S-adenosyl-L-methionine + 5-guanidino-2-oxopentanoate \rightleftharpoons S-adenosyl-L-homocysteine + 5-guanidino-3-methyl-2-oxopentanoate The enzyme is involved in production of the rare amino acid 3-methylarginine.
6-carboxytetrahydropterin synthase (, CPH4 synthase, queD (gene), ToyB , ykvK (gene)) is an enzyme with systematic name 7,8-dihydroneopterin 3'-triphosphate acetaldehyde-lyase (6-carboxy-5,6,7,8-tetrahydropterin and triphosphate- forming). This enzyme catalyses the following reversible chemical reaction. : 7,8-dihydroneopterin 3'-triphosphate + H2O 6-carboxy-5,6,7,8-tetrahydropterin + acetaldehyde + triphosphate This enzyme binds Zn2+. It is isolated from the bacteria Bacillus subtilis and Escherichia coli.
23S rRNA (guanine2069-N7)-methyltransferase (, rlmK (gene), 23S rRNA m7G2069 methyltransferase) is an enzyme with systematic name S-adenosyl-L- methionine:23S rRNA (guanine2069-N7)-methyltransferase. This enzyme catalyses the following chemical reaction : S-adenosyl-L-methionine + guanine2069 in 23S rRNA \rightleftharpoons S-adenosyl-L-homocysteine + N7-methylguanine2069 in 23S rRNA The enzyme specifically methylates guanine2069 at position N7 in 23S rRNA.
Geranyl diphosphate 2-C-methyltransferase (, SCO7701, GPP methyltransferase, GPPMT, 2-methyl-GPP synthase, MGPPS, geranyl pyrophosphate methyltransferase) is an enzyme with systematic name S-adenosyl-L-methionine:geranyl-diphosphate 2-C-methyltransferase. This enzyme catalyses the following chemical reaction : S-adenosyl-L-methionine + geranyl diphosphate \rightleftharpoons S-adenosyl-L- homocysteine + (E)-2-methylgeranyl diphosphate This enzyme takes part in synthesis of 2-methylisoborneol.
TRNA (adenine58-N1)-methyltransferase (, tRNA m1A58 methyltransferase, tRNA (m1A58) methyltransferase, TrmI, tRNA (m1A58) Mtase, Rv2118cp, Gcd10p-Gcd14p, Trm61p-Trm6p) is an enzyme with systematic name S-adenosyl-L-methionine:tRNA (adenine58-N1)-methyltransferase. This enzyme catalyses the following chemical reaction : S-adenosyl-L-methionine + adenine58 in tRNA \rightleftharpoons S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNA The enzyme specifically methylates adenine58 in tRNA.
TRNA (guanine26-N2)-dimethyltransferase (, Trm1p, TRM1, tRNA (m22G26)dimethyltransferase) is an enzyme with systematic name S-adenosyl-L- methionine:tRNA (guanine26-N2)-dimethyltransferase. This enzyme catalyses the following chemical reaction : 2 S-adenosyl-L-methionine + guanine26 in tRNA \rightleftharpoons 2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNA The enzyme dissociates from its tRNA substrate between the two consecutive methylation reactions.
Undecaprenyl phosphate N,N'-diacetylbacillosamine 1-phosphate transferase (, PglC) is an enzyme with systematic name UDP-N,N'-diacetylbacillosamine:tritrans,heptacis-undecaprenyl-phosphate N,N'-diacetylbacillosamine transferase. This enzyme catalyses the following chemical reaction : UDP-N,N'-diacetylbacillosamine + tritrans,heptacis- undecaprenyl phosphate \rightleftharpoons UMP + N,N'-diacetyl-alpha-D- bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol This enzyme is isolated from Campylobacter jejuni.
Membrane-type matrix metalloproteinase-1 (, matrix metalloproteinase 14) is an enzyme. This enzyme catalyses the following chemical reaction : Endopeptidase activity. Activates progelatinase A by cleavage of the propeptide at Asn37-Leu. Other bonds hydrolysed include Gly35-Ile in the propeptide of collagenase 3, and Asn341-Phe, Asp441-Leu and Gln354-Thr in the aggrecan interglobular domain This enzyme belongs to peptidase family M10.
Myeloblastin (, leukocyte proteinase 3, leukocyte proteinase 4, Wegener's granulomatosis autoantigen, proteinase PR-3, proteinase-3, PMNL proteinase) is an enzyme. This enzyme catalyses the following chemical reaction: Hydrolysis of proteins, including elastin, by preferential cleavage: -Ala- > -Val- This enzyme is present in polymorphonuclear leukocyte granules. Downregulation of myeloblastin in promyelocytic leukemia cells was shown to induce their growth arrest and differentiation.
Pheophorbidase (, phedase, PPD) is an enzyme with systematic name pheophorbide-a hydrolase. This enzyme catalyses the following chemical reaction : pheophorbide a + H2O \rightleftharpoons pyropheophorbide a + methanol + CO2 (overall reaction) : (1a) pheophorbide a + H2O \rightleftharpoons C-132-carboxypyropheophorbide a + methanol : (1b) C-132-carboxypyropheophorbide a \rightleftharpoons pyropheophorbide a + CO2 (spontaneous) This enzyme participates in the chlorophyll degradation in higher plants and algae.
Geranylfarnesyl diphosphate synthase (, FGPP synthase, (all-E) geranylfarnesyl diphosphate synthase, GFPS, Fgs) is an enzyme with systematic name geranylgeranyl-diphosphate:isopentenyl-diphosphate transtransferase (adding 1 isopentenyl unit). This enzyme catalyses the following chemical reaction : geranylgeranyl diphosphate + isopentenyl diphosphate \rightleftharpoons (2E,6E,10E,14E)-geranylfarnesyl diphosphate + diphosphate The enzyme from Methanosarcina mazei is involved in biosynthesis of the polyprenyl side-chain of methanophenazine.
All-trans-nonaprenyl diphosphate synthase (geranylgeranyl-diphosphate specific) (, nonaprenyl diphosphate synthase, solanesyl diphosphate synthase, At-SPS2, At-SPS1, SPS1, SPS2) is an enzyme with systematic name geranylgeranyl-diphosphate:isopentenyl-diphosphate transtransferase (adding 5 isopentenyl units). This enzyme catalyses the following chemical reaction : geranylgeranyl diphosphate + 5 isopentenyl diphosphate \rightleftharpoons 5 diphosphate + all-trans-nonaprenyl diphosphate Geranylgeranyl diphosphate is preferred over farnesyl diphosphate as allylic substrate.
2,7,4'-Trihydroxyisoflavanone 4'-O-methyltransferase (, SAM:2,7,4'-trihydroxyisoflavanone 4'-O-methyltransferase, HI4'OMT, HMM1, MtIOMT5) is an enzyme with systematic name S-adenosyl-L- methionine:2,7,4'-trihydroxyisoflavanone 4'-O-methyltransferase . This enzyme catalyses the following chemical reaction : S-adenosyl-L-methionine + 2,7,4'-trihydroxyisoflavanone \rightleftharpoons S-adenosyl-L-homocysteine + 2,7-dihydroxy-4'-methoxyisoflavanone This enzyme specifically methylates 2,7,4'-trihydroxyisoflavanone on the 4'-position.
Oligoxyloglucan reducing-end-specific cellobiohydrolase () is an enzyme with systematic name oligoxyloglucan reducing-end cellobiohydrolase. This enzyme catalyses the following chemical reaction : Hydrolysis of cellobiose from the reducing end of xyloglucans consisting of a (1->4)-beta-linked glucan carrying alpha-D-xylosyl groups on O-6 of the glucose residues. The enzyme is found in the fungus Geotrichum sp. M128.
DNA-3-methyladenine glycosylase I (, deoxyribonucleate 3-methyladenine glycosidase I, 3-methyladenine DNA glycosylase I, DNA-3-methyladenine glycosidase I) is an enzyme with systematic name alkylated-DNA glycohydrolase (releasing methyladenine and methylguanine). This enzyme catalyses the following chemical reaction : Hydrolysis of alkylated DNA, releasing 3-methyladenine This enzyme is involved in the removal of alkylated bases from DNA in Escherichia coli.
Kappa-carrageenase (, kappa-carrageenan 4-beta-D-glycanohydrolase) is an enzyme with systematic name kappa-carrageenan 4-beta-D-glycanohydrolase (configuration-retaining). This enzyme catalyses the following chemical reaction : Endohydrolysis of (1->4)-beta-D-linkages between D-galactose 4-sulfate and 3,6-anhydro-D-galactose in kappa-carrageenans The main products of hydrolysis are neocarrabiose-sulfate and neocarratetraose-sulfate.
Intermediate cleaving peptidase 55 (, Icp55, mitochondrial intermediate cleaving peptidase 55 kDa) is an enzyme. This enzyme catalyses the following chemical reaction : The enzyme cleaves the Pro36-Pro37 bond of cysteine desulfurase (EC 2.8.1.7) removing three amino acid residues (Tyr-Ser-Pro) from the N-terminus after cleavage by mitochondrial processing peptidase. Icp55 removes the destabilizing N-terminal amino acid residues.
Dipeptidyl-peptidase II (, dipeptidyl aminopeptidase II, dipeptidyl arylamidase II, carboxytripeptidase, dipeptidyl peptidase II, DAP II, dipeptidyl(amino)peptidase II, dipeptidylarylamidase) is an enzyme. This enzyme catalyses the following chemical reaction : Release of an N-terminal dipeptide, Xaa-Yaa!, preferentially when Yaa is Ala or Pro. Substrates are oligopeptides, preferentially tripeptides This lysosomal serine-type peptidase is maximally active at acidic pH.
Rhodopsin kinase (, rod opsin kinase, G-protein-coupled receptor kinase 1, GPCR kinase 1, GRK1, opsin kinase, opsin kinase (phosphorylating), rhodopsin kinase (phosphorylating), RK, STK14) is a serine/threonine-specific protein kinase involved in phototransduction. This enzyme catalyses the following chemical reaction: : ATP + rhodopsin \rightleftharpoons ADP + phospho- rhodopsin Mutations in rhodopsin kinase are associated with a form of night blindness called Oguchi disease.
EIGA, and other agencies. Copper catalyses the decomposition of acetylene, and as a result acetylene should not be transported in copper pipes. Cylinders should be stored in an area segregated from oxidizers to avoid exacerbated reaction in case of fire/leakage. Acetylene cylinders should not be stored in confined spaces, enclosed vehicles, garages, and buildings, to avoid unintended leakage leading to explosive atmosphere.
The glycosylated form develops from glucosyltransferase activity and increases the solubility of polyphenols. Polyphenol oxidase (PPO) is an enzyme that catalyses the oxidation of o-diphenols to produce o-quinones. It is the rapid polymerisation of o-quinones to produce black, brown or red polyphenolic pigments that is the cause of fruit browning. In insects, PPO serves for the cuticle hardening.
4-phosphopantoate—beta-alanine ligase (, phosphopantothenate synthetase, TK1686 protein) is an enzyme with systematic name (R)-4-phosphopantoate:beta- alanine ligase (AMP-forming). This enzyme catalyses the following chemical reaction : ATP + (R)-4-phosphopantoate + beta-alanine \rightleftharpoons AMP + diphosphate + (R)-4'-phosphopantothenate The conversion of (R)-pantoate to (R)-4'-phosphopantothenate is part of the pathway leading to biosynthesis of 4'-phosphopantetheine.
3-hydroxybenzoate—CoA ligase (, 3-hydroxybenzoyl-CoA synthetase, 3-hydroxybenzoate-coenzyme A ligase (AMP-forming), 3-hydroxybenzoyl coenzyme A synthetase, 3-hydroxybenzoyl-CoA ligase) is an enzyme with systematic name 3-hydroxybenzoate:CoA ligase (AMP-forming). This enzyme catalyses the following chemical reaction : ATP + 3-hydroxybenzoate + CoA \rightleftharpoons AMP + diphosphate + 3-hydroxybenzoyl-CoA The enzyme works equally well with 4-hydroxybenzoate.
D-alanine—(R)-lactate ligase (, VanA, VanB, VanD) is an enzyme with systematic name D-alanine:(R)-lactate ligase (ADP-forming). This enzyme catalyses the following chemical reaction : D-alanine + (R)-lactate + ATP \rightleftharpoons D-alanyl-(R)-lactate + ADP + phosphate The product of this enzyme can be incorporated into the peptidoglycan pentapeptide instead of the usual D-alanyl-D-alanine dipeptide.
O-phospho-L-serine---tRNA ligase (, O-phosphoseryl-tRNA ligase, non-canonical O-phosphoseryl-tRNA synthetase, SepRS) is an enzyme with systematic name O-phospho-L-serine:tRNACys ligase (AMP-forming). This enzyme catalyses the following chemical reaction: : ATP + O-phospho-L-serine + tRNACys \rightleftharpoons AMP + diphosphate + O-phospho-L-seryl-tRNACys In organisms like Archaeoglobus fulgidus, this enzyme ligates O-phosphoserine to tRNACys.
Mechanism for how sucrase-isomaltase catalyzes the conversion of isomaltose to two glucose molecules This enzyme catalyses the following chemical reaction : Hydrolysis of (1->6)-alpha-D- glucosidic linkages in some oligosaccharides produced from starch and glycogen by enzyme EC 3.2.1.1. Hydrolysis uses water to cleave chemical bonds. Sucrase- isomaltase’s mechanism results in a net retention of configuration at the anomeric center.
Phospholipase C (, lipophosphodiesterase I, Clostridium welchii alpha-toxin, Clostridium oedematiens beta- and gamma-toxins, lipophosphodiesterase C, phosphatidase C, heat-labile hemolysin, alpha-toxin) is an enzyme with systematic name phosphatidylcholine cholinephosphohydrolase. This enzyme catalyses the following chemical reaction : a phosphatidylcholine + H2O \rightleftharpoons 1,2-diacyl-sn-glycerol + phosphocholine The bacterial enzyme is a zinc protein. It also acts on sphingomyelin and phosphatidylinositol.
Glucosyl-3-phosphoglycerate phosphatase (, GpgP protein) is an enzyme with systematic name alpha-D-glucosyl-3-phospho-D-glycerate phosphohydrolase. This enzyme catalyses the following chemical reaction : 2-O-(alpha-D- glucopyranosyl)-3-phospho-D-glycerate + H2O \rightleftharpoons 2-O-(alpha-D- glucopyranosyl)-D-glycerate + phosphate The enzyme is involved in biosynthesis of 2-O-(alpha-D-glucopyranosyl)-D-glycerate.
Pitavastatin (usually as a calcium salt) is a member of the blood cholesterol lowering medication class of statins. Like other statins, it is an inhibitor of HMG-CoA reductase, the enzyme that catalyses the first step of cholesterol synthesis. It was patented in 1987 and approved for medical use in 2003. It is available in Japan, South Korea and in India.
Gold(III) salts, especially Na[AuCl4] (prepared from AuCl3 \+ NaCl), provide an alternative to mercury(II) salts as catalysts for reactions involving alkynes. An illustrative reaction is the hydration of terminal alkynes to produce acetyl compounds. :300px Some alkynes undergo amination in the presence of gold(III) catalysts. Gold catalyses the alkylation of certain aromatic rings and a conversion of furans to phenols.
Crime scene investigators use luminol to find traces of blood, even if someone has cleaned or removed it. The investigator sprays a solution of luminol and the oxidant. The iron in blood catalyses the luminescence. The amount of catalyst necessary to cause the reaction is very small relative to the amount of luminol, allowing detection of even trace amounts of blood.
Quinapril inhibits angiotensin converting enzyme, an enzyme which catalyses the formation of angiotensin II from its precursor, angiotensin I. Angiotensin II is a powerful vasoconstrictor and increases blood pressure through a variety of mechanisms. Due to reduced angiotensin production, plasma concentrations of aldosterone are also reduced, resulting in increased excretion of sodium in the urine and increased concentrations of potassium in the blood.
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.
Picornain 2A (, picornavirus endopeptidase 2A, poliovirus protease 2A, rhinovirus protease 2A, 2A protease, 2A proteinase, protease 2A, proteinase 2Apro, picornaviral 2A proteinase, Y-G proteinase 2A, poliovirus proteinase 2A, poliovirus protease 2Apro) is a protease enzyme. This enzyme catalyses the following chemical reaction: : Selective cleavage of Tyr-Gly bond in picornavirus polyprotein This enzyme is coded by entero-, rhino-, aphto- and cardioviruses.
Nuclear-inclusion-a endopeptidase (, potyvirus NIa protease) is a protease enzyme found in potyviruses. This enzyme catalyses the following chemical reaction: : Hydrolyses glutaminyl bonds, and activity is further restricted by preferences for the amino acids in P6 - P1' that vary with the species of potyvirus. : e.g. Glu-Xaa-Xaa-Tyr-Xaa-Gln \ (Ser or Gly) for the enzyme from tobacco etch virus.
Saccharopepsin (, yeast endopeptidase A, Saccharomyces aspartic proteinase, aspartic proteinase yscA, proteinase A, proteinase yscA, yeast proteinase A, Saccharomyces cerevisiae aspartic proteinase A, PRA) is an enzyme. This enzyme catalyses the following chemical reaction : Hydrolysis of proteins with broad specificity for peptide bonds. Cleaves -Leu-Leu-Val-Tyr bond in a synthetic substrate. This enzyme is present in baker's yeast (Saccharomyces cerevisiae).
Acrocylindropepsin (, Acrocylindrium proteinase, Acrocylindrium acid proteinase) is an enzyme. This enzyme catalyses the following chemical reaction : Preference for hydrophobic residues at P1 and P1'. Action on the B chain of insulin is generally similar to that of pepsin A, but it also cleaves Leu6-Cys(SO3H), Glu21-Arg and Asn3-Gln, although not Gln4-His This enzyme is present in fungus Acrocylindrium sp.
Gamma-glutamyl hydrolase is an enzyme that catalyses the following chemical reaction: : Hydrolysis of a gamma-glutamyl bond This lysosomal or secreted, thiol-dependent peptidase, most active at acidic pH. In humans, gamma-glutamyl hydrolase is encoded by the GGH gene. This gene catalyzes the hydrolysis of folylpoly-gamma-glutamates and antifolylpoly-gamma-glutamates by the removal of gamma-linked polyglutamates and glutamate.
Dipeptidyl peptidase I (, cathepsin C, dipeptidyl aminopeptidase I, dipeptidyl transferase, dipeptide arylamidase I, DAP I) is an enzyme. This enzyme catalyses the following chemical reaction : Release of an N-terminal dipeptide, Xaa-Yaa!Zaa-, except when Xaa is Arg or Lys, or Yaa or Zaa is Pro This Cl-dependent, lysosomal cysteine-type peptidase is maximally active at acidic pH.
Pectinesterase (PE) () is a ubiquitous cell-wall-associated enzyme that presents several isoforms that facilitate plant cell wall modification and subsequent breakdown. It is found in all higher plants as well as in some bacteria and fungi. Pectinesterase functions primarily by altering the localised pH of the cell wall resulting in alterations in cell wall integrity. Pectinesterase catalyses the de-esterification of pectin into pectate and methanol.
Methyl halide transferase (, MCT, methyl chloride transferase, S-adenosyl-L- methionine:halide/bisulfide methyltransferase, AtHOL1, AtHOL2, AtHOL3, HMT, S-adenosyl-L-methionine: halide ion methyltransferase, SAM:halide ion methyltransferase) is an enzyme with systematic name S-adenosylmethionine:iodide methyltransferase. This enzyme catalyses the following chemical reaction : S-adenosyl-L-methionine + iodide \rightleftharpoons S-adenosyl-L-homocysteine + methyl iodide This enzyme contributes to the methyl halide emissions from Arabidopsis thaliana.
23S rRNA (pseudouridine1915-N3)-methyltransferase (, YbeA, RlmH, pseudouridine methyltransferase, m3Psi methyltransferase, Psi1915-specific methyltransferase, rRNA large subunit methyltransferase H) is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (pseudouridine1915-N3)-methyltransferase. This enzyme catalyses the following chemical reaction : S-adenosyl-L-methionine + pseudouridine1915 in 23S rRNA \rightleftharpoons S-adenosyl-L-homocysteine + N3-methylpseudouridine1915 in 23S rRNA YbeA does not methylate uridine at position 1915.
Part A, D. Dolphin, R. Poulson, and O. Avramovic, eds. (New York: John Wiley & Sons), pp. 597-641. This system has been studied in both bacteria and eukaryotes. This detoxification is accomplished by the sequential action of two thiol-dependent enzymes; firstly glyoxalase І, which catalyses the isomerisation of the spontaneously formed hemithioacetal adduct between GSH and 2-oxoaldehydes (such as methylglyoxal) into S-2-hydroxyacylglutathione.
23S rRNA (uridine2479-2'-O)-methyltransferase (, AviRb) is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (uridine2479-2'-O)-methyltransferase. This enzyme catalyses the following chemical reaction : S-adenosyl-L-methionine + uridine2479 in 23S rRNA \rightleftharpoons S-adenosyl-L-homocysteine + 2'-O-methyluridine2479 in 23S rRNA Streptomyces viridochromogenes produces the antibiotic avilamycin A which binds to the 50S ribosomal subunit to inhibit protein synthesis.
TRNA-dihydrouridine20a/20b synthase (NAD(P)+) (, Dus4p) is an enzyme with systematic name tRNA-5,6-dihydrouracil20a/20b:NAD(P)+ oxidoreductase. This enzyme catalyses the following chemical reaction : (1) 5,6-dihydrouracil20a in tRNA + NAD(P)+ \rightleftharpoons uracil20a in tRNA + NAD(P)H + H+ : (2) 5,6-dihydrouracil20b in tRNA + NAD(P)+ \rightleftharpoons uracil20b in tRNA + NAD(P)H + H+ A flavoenzyme. The enzyme specifically modifies uracil20a and uracil20b in tRNA.
Glycerol-3-phosphate 2-O-acyltransferase (, sn-2-glycerol-3-phosphate O-acyltransferase, glycerol-3-phosphate O-acyltransferase) is an enzyme with systematic name acyl-CoA:sn-glycerol 3-phosphate 2-O-acyltransferase. This enzyme catalyses the following chemical reaction : acyl-CoA + sn-glycerol 3-phosphate \rightleftharpoons CoA + a 2-acyl-sn-glycerol 3-phosphate This membrane-associated enzyme is required for suberin or cutin synthesis in plants.
Leishmanolysin (, promastigote surface endopeptidase, glycoprotein gp63, Leishmania metalloproteinase, surface acid proteinase, promastigote surface protease) is an enzyme. This enzyme catalyses the following chemical reaction : Preference for hydrophobic residues at P1 and P1' and basic residues at P2' and P3'. A model nonapeptide is cleaved at -Ala-Tyr-Leu-Lys-Lys- This membrane-bound glycoprotein is present in the promastigote of various species of Leishmania protozoans.
Atrolysin B (, Crotalus atrox metalloendopeptidase b, hemorrhagic toxin b, Ht-b) is an enzyme. This enzyme catalyses the following chemical reaction : Cleavage of His5-Leu, His10-Leu, Ala14-Leu, Tyr16-Leu and Gly23-Phe of insulin B chain; identical to the cleavage of insulin B chain by atrolysin C. Also cleaves -Ser bonds in glucagon This enzyme is present in the western diamondback rattlesnake (Crotalus atrox).
Dactylysin (, peptide hormone inactivating endopeptidase, PHIE) is an enzyme. This enzyme catalyses the following chemical reaction : Hydrolysis of peptides of at least six residues, with bulky hydrophobic residues in the P1' position. Shows a preference for hydrophobic doublets such as -Phe-Phe- and -Phe-Leu- in somatostatin-(1-14)-peptide and dynorphin A-(1-6)-peptide, respectively This endopeptidase in the skin of the amphibian, Xenopus laevis.
Ruberlysin (, Crotalus ruber metalloendopeptidase II, hemorrhagic toxin II) is an enzyme. This enzyme catalyses the following chemical reaction : Cleavage of His10-Leu, Ala14-Leu, Tyr16-Leu and Gly23-Phe bonds in the B chain of insulin; His-Pro, Pro-Phe, and Trp-Ser of angiotensin I; and Gly-Phe of Met enkephalin This endopeptidase is present in the venom of the red rattlesnake (Crotalus ruber ruber).
Pseudolysin (, Pseudomonas elastase, Pseudomonas aeruginosa neutral metalloproteinase) is an enzyme. This enzyme catalyses the following chemical reaction : Hydrolysis of proteins including elastin, collagen types III and IV, fibronectin and immunoglobulin A, generally with bulky hydrophobic group at P1'. Insulin B chain cleavage pattern identical to that of thermolysin, but specificity differs in other respects This enzyme belongs to the peptidase family M4 (thermolysin family).
Procollagen C-endopeptidase (, procollagen C-terminal proteinase, carboxyprocollagen peptidase, procollagen C-terminal peptidase, procollagen C-proteinase, procollagen carboxypeptidase, procollagen carboxy-terminal proteinase, procollagen peptidase) is an enzyme. This enzyme catalyses the following chemical reaction : Cleavage of the C-terminal propeptide at Ala-Asp in type I and II procollagens and at Arg-Asp in type III This endopeptidase belongs to the peptidase family M12 (astacin family).
Peptidoglycan-N-acetylglucosamine deacetylase (, HP310, PgdA, SpPgdA, BC1960, peptidoglycan deacetylase, N-acetylglucosamine deacetylase, peptidoglycan GlcNAc deacetylase, peptidoglycan N-acetylglucosamine deacetylase, PG N-deacetylase) is an enzyme with systematic name peptidoglycan-N- acetylglucosamine amidohydrolase. This enzyme catalyses the following chemical reaction : peptidoglycan-N-acetyl-D-glucosamine + H2O \rightleftharpoons peptidoglycan-D-glucosamine + acetate This enzyme contributes to virulence of Helicobacter pylori, Listeria monocytogenes and Streptococcus suis.
Diadenosine hexaphosphate hydrolase (AMP-forming) (, hAps1, NUDT11 (gene), hAps2, NUDT10 (gene)) is an enzyme with systematic name P1,P6-bis(5'-adenosyl)hexaphosphate nucleotidohydrolase (AMP-forming). This enzyme catalyses the following chemical reaction : (1) P1,P6-bis(5'-adenosyl)hexaphosphate + H2O \rightleftharpoons adenosine 5'-pentaphosphate + AMP : (2) P1,P5-bis(5'-adenosyl)pentaphosphate + H2O \rightleftharpoons adenosine 5'-tetraphosphate + AMP A divalent cation is essential for activity.
Tryptophan is first converted into indoleacetate (indole-3-acetate) and then to skatole by the IAD. Indoleacetate decarboxylase takes part in the tryptophan fermentation, which involves two steps. The first one consists of the degradation of the amino acid into indole-3-acetate. And in the second step, the IAD catalyses the decarboxylation of the indole-3-acetate to form the final product, skatole.
Aminopyrimidine aminohydrolase (, thiaminase, thiaminase II, tenA (gene)) is an enzyme with systematic name 4-amino-5-aminomethyl-2-methylpyrimidine aminohydrolase. This enzyme catalyses the following chemical reaction : (1) 4-amino-5-aminomethyl-2-methylpyrimidine + H2O \rightleftharpoons 4-amino-5-hydroxymethyl-2-methylpyrimidine + ammonia : (2) thiamine + H2O \rightleftharpoons 4-amino-5-hydroxymethyl-2-methylpyrimidine + 5-(2-hydroxyethyl)-4-methylthiazole This enzyme was previously known as thiaminase II.
3,4-dihydroxyphenylalanine oxidative deaminase (, 3,4-dihydroxy-L- phenylalanine: oxidative deaminase, oxidative deaminase, DOPA oxidative deaminase, DOPAODA) is an enzyme with systematic name 3,4-dihydroxy-L- phenylalanine:oxygen oxidoreductase (deaminating). This enzyme catalyses the following chemical reaction : 2 L-dopa + O2 \rightleftharpoons 2 3,4-dihydroxyphenylpyruvate + 2 NH3 This enzyme is one of the three enzymes involved in L-dopa (3,4-dihydroxy-L-phenylalanine) catabolism in the bacterium Rubrivivax benzoatilyticus.
Glycosyltransferase DesVII (, DesVII) is an enzyme with systematic name dTDP-3-dimethylamino-3,4,6-trideoxy-alpha-D-glucopyranose:10-deoxymethynolide 3-dimethylamino-4,6-dideoxy-alpha-D-glucosyltransferase. This enzyme catalyses the following chemical reaction : dTDP-3-dimethylamino-3,4,6-trideoxy-alpha-D- glucopyranose + 10-deoxymethynolide \rightleftharpoons dTDP + 10-deoxymethymycin DesVII is the glycosyltransferase responsible for the attachment of TDP-D-desosamine to macrolactones of varied ring sizes.
4-O-beta-D-mannosyl-D-glucose phosphorylase (, mannosylglucose phosphorylase) is an enzyme with systematic name 4-O-beta-D-mannopyranosyl-D- glucopyranose:phosphate alpha-D-mannosyltransferase. This enzyme catalyses the following chemical reaction : 4-O-beta-D-mannopyranosyl-D-glucopyranose + phosphate \rightleftharpoons D-glucose + alpha-D-mannose 1-phosphate This enzyme forms part of a mannan catabolic pathway in the anaerobic bacterium Bacteroides fragilis NCTC 9343.
Mannosylfructose-phosphate synthase (, mannosylfructose-6-phosphate synthase, MFPS) is an enzyme with systematic name GDP-mannose:D-fructose-6-phosphate 2-alpha-D-mannosyltransferase. This enzyme catalyses the following chemical reaction : GDP-mannose + D-fructose 6-phosphate \rightleftharpoons GDP + beta- D-fructofuranosyl-alpha-D-mannopyranoside 6F-phosphate This enzyme, from the soil proteobacterium and plant pathogen Agrobacterium tumefaciens strain C58, requires Mg2+ or Mn2+ for activity.
Cycloisomaltooligosaccharide glucanotransferase () is an enzyme with systematic name (1->6)-alpha-D-glucan:(1->6)-alpha-D-glucan 6-alpha-D-(1->6alpha-D-glucano)-transferase (cyclizing). This enzyme catalyses the following chemical reaction : cyclizes part of a (1->6)-alpha-D-glucan chain by formation of a (1->6)-alpha-D-glucosidic bond This enzyme is specific for (1->6)-alpha-D-glucans (dextrans).
Glucosyl-3-phosphoglycerate synthase (, GpgS protein, GPG synthase, glucosylphosphoglycerate synthase) is an enzyme with systematic name NDP- glucose:3-phospho-D-glycerate 2-alpha-D-glucosyltransferase. This enzyme catalyses the following chemical reaction : NDP-glucose + 3-phospho-D- glycerate \rightleftharpoons NDP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D- glycerate The enzyme is involved in biosynthesis of 2-O-(alpha-D- glucopyranosyl)-D-glycerate.
TRNA-guanine15 transglycosylase (, tRNA transglycosylase, transfer ribonucleate glycosyltransferase, tRNA guanine15 transglycosidase, TGT, transfer ribonucleic acid guanine15 transglycosylase) is an enzyme with systematic name tRNA-guanine15:7-cyano-7-carbaguanine tRNA-D- ribosyltransferase. This enzyme catalyses the following chemical reaction : guanine15 in tRNA + 7-cyano-7-carbaguanine \rightleftharpoons 7-cyano-7-carbaguanine15 in tRNA + guanine Archaeal tRNAs contain the modified nucleoside archaeosine at position 15.
Pentachlorophenol monooxygenase (, pentachlorophenol dechlorinase, pentachlorophenol dehalogenase, pentachlorophenol 4-monooxygenase, PCP hydroxylase, pentachlorophenol hydroxylase, PcpB, PCB 4-monooxygenase, PCB4MO) is an enzyme with systematic name pentachlorophenol,NADPH:oxygen oxidoreductase (hydroxylating, dechlorinating). This enzyme catalyses the following chemical reaction : (1) pentachlorophenol + 2 NADPH + H+ \+ O2 \rightleftharpoons 2,3,5,6-tetrachlorohydroquinone + 2 NADP+ \+ chloride + H2O : (2) 2,3,5,6-tetrachlorophenol + NADPH + H+ \+ O2 \rightleftharpoons 2,3,5,6-tetrachlorohydroquinone + NADP+ \+ H2O Pentachlorophenol monooxygenase is a flavoprotein (FAD).
Starch synthase (maltosyl-transferring) (, alpha1,4-glucan:maltose-1-P maltosyltransferase, GMPMT) is an enzyme with systematic name alpha-maltose 1-phosphate:(1->4)-alpha-D-glucan 4-alpha-D-maltosyltransferase. This enzyme catalyses the following chemical reaction : alpha-maltose 1-phosphate + [(1->4)-alpha-D-glucosyl]n \rightleftharpoons phosphate + [(1->4)-alpha-D- glucosyl]n+2 The enzyme from the bacterium Mycobacterium smegmatis is specific for maltose.
Signal peptidase II (, premurein-leader peptidase, prolipoprotein signal peptidase, leader peptidase II, premurein leader proteinase) is an enzyme. This enzyme catalyses a chemical reaction. It releases signal peptides from murein prolipoprotein and other bacterial membrane prolipoproteins. It also hydrolyses -Xaa-Yaa-Zaa-(S,diacylglyceryl)Cys-, in which Yaa (Ala or Ser) and Zaa (Gly or Ala) have small neutral sidechains, and Xaa is hydrophobic (preferably Leu).
Atrolysin A (, Crotalus atrox metalloendopeptidase a, hemorrhagic toxin a, Crotalus atrox alpha-proteinase, Crotalus atrox proteinase, bothropasin) is an enzyme. This enzyme catalyses the following chemical reaction : Cleavage of Asn3-Gln, His5-Leu, His10-Leu, Ala14-Leu and Tyr16-Leu in insulin B chain; removes C-terminal Leu from small peptides This endopeptidase is one of six hemorrhagic toxins in the venom of western diamondback rattlesnake.
Premnaspirodiene oxygenase (, HPO, Hyoscymus muticus premnaspirodiene oxygenase) is an enzyme with systematic name (-)-vetispiradiene,NADPH:oxygen 2alpha-oxidoreductase. This enzyme catalyses the following chemical reaction : (-)-vetispiradiene + 2 NADPH + 2 H+ \+ 2 O2 \rightleftharpoons solavetivone + 2 NADP+ \+ 3 H2O (overall reaction) :(1a) (-)-vetispiradiene + NADPH + H+ \+ O2 \rightleftharpoons solavetivol + NADP+ \+ H2O :(1b) solavetivol + NADPH + H+ \+ O2 \rightleftharpoons solavetivone + NADP+ \+ 2 H2O Premnaspirodiene oxygenase heme-thiolate protein (P-450).
1-hydroxy-2-naphthoate hydroxylase (, 1-hydroxy-2-naphthoic acid hydroxylase) is an enzyme with systematic name 1-hydroxy-2-naphthoate,NAD(P)H:oxygen oxidoreductase (2-hydroxylating, decarboxylating). This enzyme catalyses the following chemical reaction : 1-hydroxy-2-naphthoate + NAD(P)H + H+ \+ O2 \rightleftharpoons 1,2-dihydroxynaphthalene + NAD(P)+ + H2O + CO2 1-hydroxy-2-naphthoate hydroxylase is involved in chrysene degradation in some bacteria.
Phenylacetyl-CoA 1,2-epoxidase (, ring 1,2-phenylacetyl-CoA epoxidase, phenylacetyl-CoA monooxygenase, PaaAC, PaaABC(D)E) is an enzyme with systematic name phenylacetyl-CoA:oxygen oxidoreductase (1,2-epoxidizing). This enzyme catalyses the following chemical reaction : phenylacetyl-CoA + NADPH + H+ \+ O2 \rightleftharpoons 2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA + NADP+ \+ H2O Phenylacetyl-CoA 1,2-epoxidase participates in catabolism of phenylacetate in Escherichia coli and Pseudomonas putida.
Delta8-fatty-acid desaturase (, Delta8-sphingolipid desaturase, EFD1, BoDES8, SLD, Delta8 fatty acid desaturase, Delta8-desaturase) is an enzyme with systematic name phytosphinganine,hydrogen donor:oxygen Delta8-oxidoreductase. This enzyme catalyses the following chemical reaction : phytosphinganine + reduced acceptor + O2 \rightleftharpoons Delta8-phytosphingenine + acceptor + 2 H2O This enzyme, which has been found mainly in plants, introduces a double bond at Delta8 of C18 and C20 fatty acids.
Phosphomethylpyrimidine synthase (, thiC (gene)) is an enzyme with systematic name 5-amino-1-(5-phospho-D-ribosyl)imidazole formate-lyase (decarboxylating, 4-amino-2-methyl-5-phosphomethylpyrimidine-forming). This enzyme catalyses the following chemical reaction : 5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine \rightleftharpoons 4-amino-2-methyl-5-phosphomethylpyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO This enzyme binds a 4Fe-4S cluster.
Ent-pimara-9(11),15-diene synthase (, PMD synthase) is an enzyme with systematic name ent-copalyl-diphosphate diphosphate-lyase (ent- pimara-9(11),15-diene-forming). This enzyme catalyses the following chemical reaction : ent-copalyl diphosphate \rightleftharpoons ent- pimara-9(11),15-diene + diphosphate This enzyme is involved in the biosynthesis of the diterpenoid viguiepinol and requires Mg2+, Co2+, Zn2+ or Ni2+ for activity.
Decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose 2-reductase (, decaprenylphospho-beta-D-ribofuranose 2'-epimerase, Rv3791, DprE2) is an enzyme with systematic name trans,octacis-decaprenylphospho-beta-D- arabinofuranose:NAD+ 2-oxidoreductase. This enzyme catalyses the following chemical reaction : trans,octacis-decaprenylphospho-beta-D-arabinofuranose + NAD+ \rightleftharpoons trans,octacis-decaprenylphospho-beta-D-erythro- pentofuranosid-2-ulose + NADH + H+ The reaction is catalysed in the reverse direction.
UDP-N-acetyl-D-mannosamine dehydrogenase (, UDP-ManNAc 6-dehydrogenase, wecC (gene)) is an enzyme with systematic name UDP-N-acetyl-alpha-D- mannosamine:NAD+ 6-oxidoreductase. This enzyme catalyses the following chemical reaction : UDP-N-acetyl-alpha-D-mannosamine + 2 NAD+ \+ H2O \rightleftharpoons UDP-N-acetyl-alpha-D-mannosaminuronate + 2 NADH + 2 H+ This enzyme participates in acetamido sugar biosynthesis in bacteria and archaea.
DTDP-6-deoxy-L-talose 4-dehydrogenase (NAD+) (, tll (gene name)) is an enzyme with systematic name dTDP-6-deoxy-beta-L-talose:NAD+ 4-oxidoreductase. This enzyme catalyses the following chemical reaction : dTDP-6-deoxy-beta-L-talose + NAD+ \rightleftharpoons dTDP-4-dehydro-6-deoxy-beta-L-mannose + NADH + H+ The enzyme from bacterium Aggregatibacter actinomycetemcomitans participates in the biosynthesis of the serotype c-specific polysaccharide antigen.
6-phospho-3-hexuloisomerase (, 3-hexulose-6-phosphate isomerase, phospho-3-hexuloisomerase, PHI, 6-phospho-3-hexulose isomerase, YckF) is an enzyme with systematic name D-arabino-hex-3-ulose-6-phosphate isomerase. This enzyme catalyses the following chemical reaction : D-arabino-hex-3-ulose 6-phosphate \rightleftharpoons D-fructose 6-phosphate This enzyme plays a key role in the ribulose-monophosphate cycle of formaldehyde fixation.
2,3-diketo-5-methylthiopentyl-1-phosphate enolase (, DK-MTP-1-P enolase, MtnW, YkrW, RuBisCO-like protein, RLP) is an enzyme with systematic name 2,3-diketo-5-methylthiopentyl-1-phosphate keto-enol-isomerase. This enzyme catalyses the following chemical reaction : 5-(methylthio)-2,3-dioxopentyl phosphate \rightleftharpoons 2-hydroxy-5-(methylthio)-3-oxopent-1-enyl phosphate The enzyme participates in the methionine salvage pathway in Bacillus subtilis.
2-hydroxymuconate tautomerase (, 4-oxalocrotonate tautomerase, 4-oxalocrotonate isomerase, cnbG (gene), praC (gene), xylH (gene)) is an enzyme with systematic name (2Z,4E)-2-hydroxyhexa-2,4-dienedioate keto-enol isomerase. This enzyme catalyses the following chemical reaction : (2Z,4E)-2-hydroxyhexa-2,4-dienedioate \rightleftharpoons (3E)-2-oxohex-3-enedioate Involved in the meta-cleavage pathway for the degradation of phenols, modified phenols and catechols.
Sulfopropanediol 3-dehydrogenase (, DHPS 3-dehydrogenase (sulfolactate forming), 2,3-dihydroxypropane-1-sulfonate 3-dehydrogenase (sulfolactate forming), dihydroxypropanesulfonate 3-dehydrogenase, hpsN (gene)) is an enzyme with systematic name (R)-2,3-dihydroxypropane-1-sulfonate:NAD+ 3-oxidoreductase. This enzyme catalyses the following chemical reaction : (R)-2,3-dihydroxypropane-1-sulfonate + 2 NAD+ \+ H2O \rightleftharpoons (R)-3-sulfolactate + 2 NADH + 2 H+ The enzyme is involved in degradation of (R)-2,3-dihydroxypropanesulfonate.
Only one cysteine residue is conserved between the sequences of the fungal, plant and bacterial enzymes; it is located in the middle of a conserved hexapeptide. Other enzymes also belong to this family including carboxyvinyl-carboxyphosphonate phosphorylmutase () which catalyses the conversion of 1-carboxyvinyl carboxyphosphonate to 3-(hydrohydroxyphosphoryl) pyruvate carbon dioxide, and phosphoenolpyruvate mutase (), which is involved in the biosynthesis of phosphinothricin tripeptide antiobiotics.
The formation of the hopene skeleton is one of the most complex single step reactions in biochemistry. In a single step, 13 covalent bonds are broken or formed, 9 chiral centers are established, and 5 rings are produced. Squalene–hopene cyclase catalyses the conversion of the acyclic molecule of squalene into the pentacyclic triterpenes of hopene and hopanol. These products appear in the ratio 5:1.
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.
2-hydroxychromene-2-carboxylate isomerase (, HCCA isomerase, 2HC2CA isomerase, 2-hydroxychromene-2-carboxylic acid isomerase) is an enzyme with systematic name 2-hydroxy-2H-chromene-2-carboxylate---(3E)-4-(2-hydroxyphenyl)-2-oxobut-3-enoate isomerase. This enzyme catalyses the following chemical reaction : 2-hydroxy-2H-chromene-2-carboxylate \rightleftharpoons (3E)-4-(2-hydroxyphenyl)-2-oxobut-3-enoate This enzyme is involved in naphthalene degradation.
Trans,polycis-polyprenyl diphosphate synthase ((2Z,6E)-farnesyl diphosphate specific) () is an enzyme with systematic name (2Z,6E)-farnesyl- diphosphate:isopentenyl-diphosphate cistransferase (adding 9--11 isopentenyl units). This enzyme catalyses the following chemical reaction : (2Z,6E)-farnesyl diphosphate + n isopentenyl diphosphate \rightleftharpoons n diphosphate + trans,polycis-polyprenyl diphosphate (n = 9 - 11) This enzyme has the highest activity with (2Z,6E)-farnesyl diphosphate as allylic substrate.
2-deoxy-scyllo-inosamine dehydrogenase (SAM-dependent) (, btrN (gene)) is an enzyme with systematic name 2-deoxy-scyllo-inosamine:S-adenosyl-L-methionine 1-oxidoreductase. This enzyme catalyses the following chemical reaction : 2-deoxy-scyllo-inosamine + S-adenosyl-L-methionine \rightleftharpoons 3-amino-2,3-dideoxy-scyllo-inosose + 5'-deoxyadenosine + L-methionine This enzyme participates in the biosynthetic pathway of the aminoglycoside antibiotics of the butirosin family.
N-acetylhexosamine 1-kinase (, NahK, LnpB, N-acetylgalactosamine/N-acetylglucosamine 1-kinase) is an enzyme with systematic name ATP:N-acetyl-D-hexosamine 1-phosphotransferase. This enzyme catalyses the following chemical reaction : ATP + N-acetyl-D-hexosamine \rightleftharpoons ADP + N-acetyl-alpha-D-hexosamine 1-phosphate This enzyme is involved in the lacto-N-biose I/galacto-N-biose degradation pathway in the probiotic bacterium Bifidobacterium longum.
Phosphonic esters are prepared using the Michaelis–Arbuzov reaction. For example, methyl iodide catalyses the conversion of trimethylphosphite to the phosphonate ester dimethyl methylphosphonate: :P(OMe)3 → MePO(OMe)2 These esters can be hydrolysed to the acid (Me = methyl): :MePO(OMe)2 \+ H2O → MePO(OH)2 \+ 2 MeOH In the Michaelis–Becker reaction, a hydrogen phosphonate diester is first deprotonated and the resulting anion is alkylated.
TRNA (guanine10-N2)-methyltransferase (, (m2G10) methyltransferase, Trm11-Trm112 complex) is an enzyme with systematic name S-adenosyl-L- methionine:tRNA (guanine10-N2)-methyltransferase. This enzyme catalyses the following chemical reaction : S-adenosyl-L-methionine + guanine10 in tRNA \rightleftharpoons S-adenosyl-L-homocysteine + N2-methylguanine10 in tRNA tRNA (guanine10-N2)-methyltransferase from yeast does not catalyse the methylation from N2-methylguanine10 to N2-dimethylguanine10 in tRNA.
23S rRNA (adenine2503-C8)-methyltransferase (, Cfr (gene)) is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (adenine2503-C8)-methyltransferase. This enzyme catalyses the following chemical reaction : 2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA \rightleftharpoons S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA This enzyme is a member of the 'AdoMet radical' (radical SAM) family.
Erythromycin 3-O-methyltransferase (, EryG) is an enzyme with systematic name S-adenosyl-L-methionine:erythromycin C 3-O-methyltransferase. This enzyme catalyses the following chemical reaction : (1) S-adenosyl-L-methionine + erythromycin C \rightleftharpoons S-adenosyl-L-homocysteine + erythromycin A : (2) S-adenosyl-L-methionine + erythromycin D \rightleftharpoons S-adenosyl-L- homocysteine + erythromycin B The enzyme methylates the 3 position of the mycarosyl moiety of erythromycin C.
TRNA (adenine9-N1)-methyltransferase (, Trm10p, tRNA(m1G9/m1A9)-methyltransferase, tRNA(m1G9/m1A9)MTase, TK0422p (gene), tRNA m1A9-methyltransferase, tRNA m1A9 Mtase) is an enzyme with systematic name S-adenosyl-L-methionine:tRNA (adenine9-N1)-methyltransferase. This enzyme catalyses the following chemical reaction : S-adenosyl-L-methionine + adenine9 in tRNA \rightleftharpoons S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA The enzyme from Sulfolobus acidocaldarius specifically methylates adenine9 in tRNA.
D-glycero-alpha-D-manno-heptose 1-phosphate guanylyltransferase (, hddC (gene), gmhD (gene)) is an enzyme with systematic name GTP:D-glycero-alpha-D- manno-heptose 1-phosphate guanylyltransferase. This enzyme catalyses the following chemical reaction : D-glycero-alpha-D-manno-heptose 1-phosphate + GTP \rightleftharpoons GDP-D-glycero-alpha-D-manno-heptose + diphosphate The enzyme is involved in biosynthesis of GDP-D-glycero-alpha-D-manno-heptose.
Pseudaminic acid cytidylyltransferase (, PseF) is an enzyme with systematic name CTP:5,7-diacetamido-3,5,7,9-tetradeoxy-L-glycero-alpha-L-manno- nonulosonic acid cytidylyltransferase. This enzyme catalyses the following chemical reaction : CTP + 5,7-bis(acetylamino)-3,5,7,9-tetradeoxy-L-glycero- alpha-L-manno-2-nonulopyranosonic acid \rightleftharpoons diphosphate + CMP-5,7-bis(acetylamino)-3,5,7,9-tetradeoxy-L-glycero-alpha-L- manno-2-nonulopyranosonic acid Mg2+ is required for activity.
Adenosylcobinamide-GDP ribazoletransferase (, CobS, cobalamin synthase, cobalamin-5'-phosphate synthase, cobalamin (5'-phosphate) synthase) is an enzyme with systematic name adenosylcobinamide-GDP:alpha-ribazole ribazoletransferase. This enzyme catalyses the following chemical reaction : (1) adenosylcobinamide-GDP + alpha-ribazole \rightleftharpoons GMP + adenosylcobalamin : (2) adenosylcobinamide-GDP + alpha-ribazole 5'-phosphate \rightleftharpoons GMP + adenosylcobalamin 5'-phosphate This enzyme is part of the biosynthetic pathway to cobalamin (vitamin B12) in bacteria.
3-O-alpha-D-mannopyranosyl-alpha-D-mannopyranose xylosylphosphotransferase (, XPT1) is an enzyme with systematic name UDP-D-xylose:3-O-alpha-D- mannopyranosyl-alpha-D-mannopyranose xylosylphosphotransferase. This enzyme catalyses the following chemical reaction : UDP-xylose + 3-O-alpha-D- mannopyranosyl-alpha-D-mannopyranose \rightleftharpoons UMP + 3-O-(6-O-alpha- D-xylosylphospho-alpha-D-mannopyranosyl)-alpha-D-mannopyranose Mn2+ required for activity.
GLUD1 catalyses the oxidative deamination of Glu to 2-oxoglutarate and free NH4+ using either NAD+ or NADP+ as a co-factor. The reaction occurs with the transfer of a hydride ion from Glu's Cα to NAD(P)+, thereby forming 2-iminoglutarate, which is hydrolyzed to 2-oxoglutarate and NH4+. The reaction's equilibrium under standard circumstances greatly favors Glu formation over NH4+ (Go' ~ 30 kJ.mol-1) formation.
Thiazole synthase (, thiG (gene)) is an enzyme with systematic name 1-deoxy-D- xylulose 5-phosphate:thiol sulfurtransferase. This enzyme catalyses the following chemical reaction : 1-deoxy-D-xylulose 5-phosphate + 2-iminoacetate + thiocarboxy-adenylate-[sulfur-carrier protein ThiS] \rightleftharpoons 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + [sulfur- carrier protein ThiS] + 2 H2O H2S can provide the sulfur in vitro.
Hexaprenyl-diphosphate synthase ((2E,6E)-farnesyl-diphosphate specific) (, HexPS, hexaprenyl pyrophosphate synthetase, hexaprenyl diphosphate synthase) is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate:isopentenyl- diphosphate farnesyltranstransferase (adding 3 isopentenyl units). This enzyme catalyses the following chemical reaction : (2E,6E)-farnesyl diphosphate + 3 isopentenyl diphosphate \rightleftharpoons 3 diphosphate + all-trans- hexaprenyl diphosphate The enzyme prefers farnesyl diphosphate to geranylgeranyl diphosphate as an allylic substrate.
Trans,polycis-decaprenyl diphosphate synthase (, Rv2361c, (2Z,6Z,10Z,14Z,18Z,22Z,26Z,30Z,34E)-decaprenyl diphosphate synthase) is an enzyme with systematic name (2Z,6E)-farnesyl-diphosphate:isopentenyl- diphosphate farnesylcistransferase (adding 7 isopentenyl units) . This enzyme catalyses the following chemical reaction : (2Z,6E)-farnesyl diphosphate + 7 isopentenyl diphosphate \rightleftharpoons 7 diphosphate + trans,octacis- decaprenyl diphosphate The enzyme is involved in the biosynthesis of decaprenyl phosphate.
Beta-D-glucopyranosyl abscisate beta-glucosidase (, AtBG1, ABA-beta-D- glucosidase, ABA-specific beta-glucosidase, ABA-GE hydrolase, beta-D- glucopyranosyl abscisate hydrolase) is an enzyme with systematic name beta-D- glucopyranosyl abscisate glucohydrolase. This enzyme catalyses the following chemical reaction : D-glucopyranosyl abscisate + H2O \rightleftharpoons D-glucose + abscisate The enzyme hydrolyzes the biologically inactive beta-D- glucopyranosyl ester of abscisic acid to produce active abscisate.
Glycoprotein endo-alpha-1,2-mannosidase (, glucosylmannosidase, endo-alpha-D- mannosidase, endo-alpha-mannosidase, endomannosidase, glucosyl mannosidase) is an enzyme with systematic name glycoprotein glucosylmannohydrolase. This enzyme catalyses the following chemical reaction : Hydrolysis of the terminal alpha-D-glucosyl-(1,3)-D-mannosyl unit from the GlcMan9(GlcNAc)2 oligosaccharide component of the glycoprotein produced in the Golgi membrane This protein is involved in the synthesis of glycoproteins.
Mannosylglycerate hydrolase (, 2-O-(6-phospho-mannosyl)-D-glycerate hydrolase, alpha-mannosidase, mngB (gene)) is an enzyme with systematic name 2-O-(6-phospho-alpha-D-mannosyl)-D-glycerate acylhydrolase. This enzyme catalyses the following chemical reaction : 2-O-(6-phospho-alpha-D- mannosyl)-D-glycerate + H2O \rightleftharpoons D-mannose 6-phosphate + D-glycerate The enzyme participates in the mannosylglycerate degradation pathway of some bacteria.
Oligosaccharide reducing-end xylanase (, Rex, reducing end xylose-releasing exo-oligoxylanase) is an enzyme with systematic name beta-D- xylopyranosyl-(1->4)-beta-D-xylopyranose reducing-end xylanase. This enzyme catalyses the following chemical reaction : Hydrolysis of (1->4)-beta-D-xylose residues from the reducing end of oligosaccharides The enzyme acts rapidly on the beta-anomer of beta-D-xylopyranosyl-(1->4)-beta-D-xylopyranose.
Glucan 1,3-alpha-glucosidase (, exo-1,3-alpha-glucanase, glucosidase II, 1,3-alpha-D-glucan 3-glucohydrolase) is an enzyme with systematic name 3-alpha-D-glucan 3-glucohydrolase. This enzyme catalyses the following chemical reaction : Hydrolysis of terminal (1->3)-alpha-D-glucosidic links in (1->3)-alpha-D-glucans This enzyme does not act on nigeran although it has some activity against nigerose.
Keratan-sulfate endo-1,4-beta-galactosidase (, endo-beta-galactosidase, keratan sulfate endogalactosidase, keratanase, keratan-sulfate 1,4-beta-D- galactanohydrolase) is an enzyme with systematic name keratan-sulfate 4-beta- D-galactanohydrolase. This enzyme catalyses the following chemical reaction : Endohydrolysis of (1->4)-beta-D-galactosidic linkages in keratan sulfate Hydrolyses the 1,4-beta-D-galactosyl linkages adjacent to 1,3-N-acetyl-alpha- D-glucosaminyl residues.
Glycosylphosphatidylinositol phospholipase D (, GPI-PLD, glycoprotein phospholipase D, phosphatidylinositol phospholipase D, phosphatidylinositol- specific phospholipase D) is an enzyme with systematic name glycoprotein- phosphatidylinositol phosphatidohydrolase. This enzyme catalyses the following chemical reaction : 6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H2O \rightleftharpoons 6-(alpha-D-glucosaminyl)-1D-myo-inositol + 3-sn- phosphatidate This enzyme cleaves proteins from the lipid part of the glycosylphosphatidylinositol (GPI) anchors.
Cytochrome b mutations can frequently cause isolated exercise intolerance and myopathy and in some cases multisystem disorders. The mitochondrial respiratory chain complex III catalyses electron transfer to cytochrome c. Complex III is embedded in the inner membrane of the mitochondria and consists of 11 subunits. Cytochrome b is encoded by the mitochondrial DNA which differs from all other subunits which are encoded in the nucleus.
Ginni is a mysterious girl with premonition skills, who predicted various mishaps and deaths of few people including her mother's death and Ija's first son (excluding Kabir), Abhinav's death too. All the predictions come true. This makes Ija really angry and catalyses the bloody game of betrayal. Enter Maai, Ija's mother, who is an expert black magician, who also comes to know about Ginni's premonition skills.
Xaa-Pro dipeptidyl-peptidase (, X-prolyl dipeptidyl aminopeptidase, PepX, X-prolyl dipeptidyl peptidase is an enzyme. It catalyses the following chemical reaction : Hydrolyses Xaa-Pro bonds to release unblocked, N-terminal dipeptides from substrates including Ala-Pro-p-nitroanilide and (sequentially) Tyr-Pro--Phe-Pro--Gly-Pro--Ile The intracellular enzyme from Lactococcus lactis (190-kDa) is the type example of peptidase family S15.

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