1000 Sentences With "biosynthesis" | Random Sentence Generator

They take in sugar and output whatever molecule their biosynthesis pathway has been modified to produce — within reason, of course.

Among them were "Protein Biosynthesis and Problems of Heredity, Development and Aging" (1963) and "Molecular-Genetic Mechanisms of Development" (1968).

In the meantime, Librede is racing to develop cheaper biosynthesis of other cannabinoids that can compare with the cost of growing marijuana.

Valine (abbreviated as Val or V) encoded by the codons GUU, GUC, GUA, and GUG is an -amino acid that is used in the biosynthesis of proteins.

Many people already do basic home biosynthesis, says University of Ottawa biologist Andrew Pelling, although perhaps the best-known examples—home meth or THC labs—are morally charged.

Developed by researchers from the University of Florida, the Mexican lime you're looking at has been modified so that its contains a protein that induces a process known as anthocyanin biosynthesis.

By then, he had published more than 100 scientific papers on the biosynthesis of proteins, heredity and the aging process, and had become a prolific contributor to the underground literature of protest.

It's completely self-sufficient producing, but basically they turbocharged its heme biosynthesis and introduced a gene for a plant protein that kind of holds the heme and delivers it when you cook the meat.

Phyto Partners Managing Partner Larry Schnurmacher told Business Insider that in 2020, Phyto is focusing on international opportunities for CBD and hemp, synthetic cannabinoids produced using biosynthesis, and opportunities in advertising and marketing tech, among other things.

This enzyme participates in 4 metabolic pathways: keratan sulfate biosynthesis, glycosphingolipid biosynthesis - lactoseries, glycan structures - biosynthesis 1, and glycan structures - biosynthesis 2.

This enzyme participates in 4 metabolic pathways: glycosphingolipid biosynthesis - lactoseries, glycosphingolipid biosynthesis - neo-lactoseries, glycosphingolipid biosynthesis - globoseries, and glycan structures - biosynthesis 2.

This enzyme participates in 4 metabolic pathways: keratan sulfate biosynthesis, glycosphingolipid biosynthesis - neo-lactoseries, glycan structures - biosynthesis 1, and glycan structures - biosynthesis 2.

This enzyme participates in 3 metabolic pathways: n-glycan biosynthesis, keratan sulfate biosynthesis, and glycan structures - biosynthesis 1.

This enzyme participates in 3 metabolic pathways: glycosphingolipid biosynthesis - lactoseries, glycosphingolipid biosynthesis - neo-lactoseries, and glycan structures - biosynthesis 2.

This enzyme participates in lipopolysaccharide biosynthesis and glycan structures - biosynthesis 2.

This enzyme participates in chondroitin sulfate biosynthesis and glycan structures - biosynthesis 1.

This enzyme participates in heparan sulfate biosynthesis and glycogen structures - biosynthesis 1.

This enzyme participates in heparan sulfate biosynthesis and glycan structures - biosynthesis 1.

This enzyme participates in phenylalanine, tyrosine and tryptophan biosynthesis and novobiocin biosynthesis.

This enzyme participates in glycosphingolipid biosynthesis - globoseries and glycan structures - biosynthesis 2.

This enzyme participates in n-glycan biosynthesis and glycan structures - biosynthesis 1.

This enzyme participates in glycosphingolipid biosynthesis - ganglioseries and glycan structures - biosynthesis 2.

This enzyme participates in fatty acid biosynthesis and polyunsaturated fatty acid biosynthesis.

This enzyme participates in glycosphingolipid biosynthesis - ganglioseries and glycan structures - biosynthesis 2.

This enzyme participates in glycosphingolipid biosynthesis - globoseries and glycan structures - biosynthesis 2.

This enzyme participates in o-glycan biosynthesis and glycan structures - biosynthesis 1.

This enzyme participates in n-glycan biosynthesis and glycan structures - biosynthesis 1.

This enzyme participates in valine, leucine and isoleucine biosynthesis and aminoacyl-trna biosynthesis.

This enzyme participates in glycosphingolipid biosynthesis - neo-lactoseries and glycan structures - biosynthesis 2.

It plays a key role in chain elongation in fatty acid biosynthesis and polyketide biosynthesis.

This enzyme participates in 6 metabolic pathways: methionine metabolism, tyrosine metabolism, phenylalanine metabolism, phenylalanine, tyrosine and tryptophan biosynthesis, novobiocin biosynthesis, and alkaloid biosynthesis i. It employs one cofactor, pyridoxal phosphate.

This enzyme participates in 3 metabolic pathways: nucleotide sugars metabolism, streptomycin biosynthesis, and polyketide sugar unit biosynthesis.

This enzyme participates in chondroitin sulfate biosynthesis and glycan structures - biosynthesis 1. It employs one cofactor, manganese.

This enzyme participates in 3 metabolic pathways: chondroitin sulfate biosynthesis, sulfur metabolism, and the biosynthesis of glycan structures.

PAL is involved in 5 metabolic pathways: tyrosine metabolism, phenylalanine metabolism, nitrogen metabolism, phenylpropanoid biosynthesis, and alkaloid biosynthesis.

The polymerization step of aromatic monomers has been shown to involve a peroxidase reaction. The biosynthesis of the aliphatic monomers shares the same upstream reactions with cutin biosynthesis, and the biosynthesis of aromatics shares the same upstream reactions with lignin biosynthesis. Phlobaphen also occurs in the polyaromatic part of the suberin mixture.

This enzyme participates in biosynthesis of steroids and terpenoid biosynthesis. This protein may use the morpheein model of allosteric regulation.

The enzyme has demonstrated value in biosynthesis of semi-opiate drugs in microorganisms, expanding the chemical diversity of BIA biosynthesis.

Rhodelphis also contains mitochondria with tubular cristae that possess an iron-sulfur cluster biosynthesis pathway and play a part in heme biosynthesis.

This enzyme participates in 3 metabolic pathways: the lactoseries and neolactoseries of glycosphingolipid biosynthesis, as well as the biosynthesis of glycan structures.

Hence TrpR provides a negative feedback mechanism that regulates the biosynthesis of tryptophan. In short tryptophan acts as a corepressor for its own biosynthesis.

Other names in common use include ATC oxygenase, and anhydrotetracycline oxygenase. This enzyme participates in tetracycline biosynthesis and biosynthesis of type ii polyketide products.

Kutchan, Toni M. "Molecular genetics of plant alkaloid biosynthesis." The alkaloids 50 (1998): 257-316. Salutaridinol's unique position adjacent to two of the four enzymes in the morphine biosynthesis pathway gives it an important role in enzymatic, genetic, and synthetic biology studies of morphine biosynthesis.

The structural variants of the swinholide biosynthesis gene clusters origins were elucidate through phylogenic studies. A phylogenetic tree of trans-encoded AT proteins showed that all six biosynthesis gene clusters were similar and assembled their own group. Scytophycin, luminaolide, and tolytoxin biosynthesis gene clusters were arranged together based on ketosynthase domains, and the misakinolide and swinholide biosynthesis gene clusters constituted their own category (Figure 5). Figure 5.

This enzyme participates in 5 metabolic pathways: histidine metabolism, tyrosine metabolism, phenylalanine metabolism, phenylalanine, tyrosine and tryptophan biosynthesis, and novobiocin biosynthesis. It employs one cofactor, pyridoxal phosphate.

This enzyme participates in 3 metabolic pathways: valine, leucine and isoleucine degradation, valine, leucine and isoleucine biosynthesis, and pantothenate and coa biosynthesis. It employs one cofactor, pyridoxal phosphate.

The third enzyme of L-carnitine biosynthesis is 4-N-trimethylaminobutyraldehyde dehydrogenase.Hulse, J. D.; Henderson, L. M. Carnitine biosynthesis. Purification of 4-N’-trimethylaminobutyraldehyde dehydrogenase from beef liver.

Figure 3. Swinholide Biosynthesis. The swinholide biosynthesis gene cluster codes for a trans-AT PKS and does not integrate AT domains similar to the phormidolide (phm), miskinolide (mis), tolytoxin (tto), luminaolide (lum), and nosperin (nsp) gene clusters. The swinholide biosynthesis gene cluster is also similar to the tto and lum gene clusters.

The PyrR binding site is an RNA element that is found upstream of a variety of genes involved in pyrimidine biosynthesis and transport. The RNA structure permits binding of PyrR protein which regulates pyrimidine biosynthesis in Bacillus subtilis. When the protein binds, a downstream terminator hairpin forms, repressing transcription of biosynthesis genes.

Vitamin C biosynthesis in plants There are many different biosynthesis pathways for ascorbic acid in plants. Most of these pathways are derived from products found in glycolysis and other pathways. For example, one pathway goes through the plant cell wall polymers. The plant ascorbic acid biosynthesis pathway most principal seems to be -galactose.

Figure 1. Proposed Mechanistic Biosynthesis of α-santonin The full biosynthesis of α-santonin has not been elucidated but α-santonin bears much similarity to parthenolide. The proposed biosynthesis begins with the cyclization of farnesyl diphosphate (FPP) to (+)-germacrene A by a sesquiterpene synthase. (+)-germacrene A hydroxylase then hydroxylates the isopropenyl side chain.

The biosynthesis of echinomycin starts with molecule QC. L-tryptophan is the precursor for QC and its biosynthesis parallels the first stage of nikkomycin biosynthesis. After QC is biosynthesized, the adenylation domain-containing Ecm1 activates and transfers QC to FabC using the fatty acid biosynthesis acyl carrier protein (ACP). The first module, Ecm6 accepts the QC-SFabC as the starter unit. Emc7 contains a terminal thioesterase domain which allows the peptide to dimerize and then release.

Vomilenine is an intermediate chemical in the biosynthesis of ajmaline.

It is an intermediary compound in the biosynthesis of scytonemin.

This enzyme participates in terpene indole and ipecac alkaloid biosynthesis.

This enzyme participates in the biosynthesis of siderophore group (nonribosomal).

Lobelanine is a chemical precursor in the biosynthesis of lobeline.

In enzymology, a beta-galactoside alpha-2,3-sialyltransferase () is an enzyme that catalyzes the chemical reaction :CMP-N-acetylneuraminate + beta-D- galactosyl-1,3-N-acetyl-alpha-D-galactosaminyl-R \rightleftharpoons CMP + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,3-N-acetyl-alpha-D- galactosaminyl-R Thus, the two substrates of this enzyme are CMP-N- acetylneuraminate and beta-D-galactosyl-1,3-N-acetyl-alpha-D-galactosaminyl-R, whereas its 3 products are CMP, alpha-N-acetylneuraminyl-2,3-beta-D- galactosyl-1,3-N-acetyl-alpha-D-, and galactosaminyl-R. This enzyme belongs to the family of transferases, specifically those glycosyltransferases that do not transfer hexosyl or pentosyl groups. The systematic name of this enzyme class is CMP-N-acetylneuraminate:beta-D-galactoside alpha-2,3-N-acetylneuraminyl-transferase. This enzyme participates in 7 metabolic pathways: o-glycan biosynthesis, keratan sulfate biosynthesis, glycosphingolipid biosynthesis - lactoseries, glycosphingolipid biosynthesis - globoseries, glycosphingolipid biosynthesis - ganglioseries, glycan structures - biosynthesis 1, and glycan structures - biosynthesis 2.

The phosphatidic acid is also a precursor for triglyceride biosynthesis. Phosphatidic acid phosphotase catalyzes the conversion of phosphatidic acid to diacylglyceride, which will be converted to triacylglyceride by acyltransferase. Tryglyceride biosynthesis occurs in the cytosol.

Biochemistry 1967, 6, 1262–1270.Vaz, F. M.; Wanders, R. J. A. Carnitine biosynthesis in mammals. Biochem. J. 2002, 361, 417–429.Strijbis, K.; Vaz, F, M.; Distel, B. Enzymology of the carnitine biosynthesis pathway.

This enzyme participates in coenzyme A (CoA) biosynthesis from pantothenic acid.

Other amine and neuropeptide neurotransmitters may also inhibit juvenile hormone biosynthesis.

Pyrimidine biosynthesis occurs both in the body and through organic synthesis.

This enzyme participates in monoterpenoid biosynthesis and limonene and pinene degradation.

This enzyme participates in monoterpenoid biosynthesis. It employs one cofactor, heme.

This enzyme participates in bile acid biosynthesis and ppar signaling pathway.

Granadaene is an organic compound produced by S.agalactiae. It is the product of a metabolic pathway similar to that of biosynthesis of fatty acids. The enzymes necessary for the biosynthesis of granadaene in GBS are coded by a gene cluster of 12 genes, the cyl operon, and a pathway for the pigment biosynthesis requiring all the genes of the cyl operon has been proposed. Like the biosynthesis of the pigment, the hemolytic activity requires also in GBS the 12 genes of the cyl operon.

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).

The swinholide biosynthesis gene cluster (swi) was located on a single scaffold by BLASTp searches against misakinolide biosynthesis cluster genes. This was chosen because of the close structural resemblance of these compounds. The swinholide biosynthesis gene cluster (85-kb) encodes for five PKS proteins, including SwiC to SwiG. This includes an AT enzyme, SwiG, which is an characteristic of trans-PKSs (Figure 3).

SdCPS2 catalyzes the first committed reaction in the biosynthesis of salvinorin A by producing its characteristic clerodane scaffold. A series of oxygenation, acylation and methylation reactions is then required to complete the biosynthesis of salvinorin A. Biosynthesis of Salvinorin A Similar to many plant-derived psychoactive compounds, salvinorin A is excreted via peltate glandular trichomes, which reside external to the epidermis.

Salicylate Biosynthesis I Pathway Isochorismate lyase is the second enzyme in the pathway salicylate biosynthesis I, a pathway occurring immediately following chorismate biosynthesis I. Using the chorismate produced from that metabolic process, first the enzyme PchA will catalyze the reaction of chorismate into isochorismate, which in turn is used by IPL to cleave off a pyruvate, leaving the product salicylate.

The biosynthesis of JH is similar to that of cholesterol in animals. There are considerable differences between the biosynthesis of the homo-isoprenoid JHs found almost exclusively in Lepidoptera, as opposed to the isoprenoids JH III, JH III bisepoxide, and methyl farnesoate found in other insects. Cholesterol biosynthesis has been exhaustively studied in animals. All steps occur in the cytosol.

Folate derivatives participate in the biosynthesis of both purines and pyrimidines. Formyl folate is required for two of the steps in the biosynthesis of inosine monophosphate, the precursor to GMP and AMP. Methylenetetrahydrofolate donates the C1 center required for the biosynthesis of dTMP (2′-deoxythymidine-5′-phosphate) from dUMP (2′-deoxyuridine-5′-phosphate). The conversion is catalyzed by thymidylate synthase.

This locus represents a mitochondrial ubiquinone biosynthesis gene. The encoded protein is likely necessary for biosynthesis of coenzyme Q10, as mutations at this locus have been associated with autosomal-recessive neonatal-onset primary coenzyme Q10 deficiency.

Disruption of this biosynthesis step results in albinism and stunted plant growth.

This enzyme participates in alanine and aspartate metabolism and aminoacyl-trna biosynthesis.

This enzyme participates in beta-alanine metabolism and pantothenate and CoA biosynthesis.

Erysodienone is a precursor in the biosynthesis of many of these alkaloids.

Folates are also essential for the biosynthesis of purines and one pyrimidine.

In 1975, he published a classic paper on the biosynthesis of prothrombin.

This enzyme participates in biosynthesis of 12-, 14- and 16-membered macrolides.

This enzyme participates in biosynthesis of steroids. It employs one cofactor, glutathione.

This enzyme participates in lysine biosynthesis. It employs one cofactor, pyridoxal phosphate.

This enzyme participates in alkaloid biosynthesis i. It employs one cofactor, iron.

Homoserine is an intermediate in the biosynthesis of threonine, isoleucine, and methionine.

This enzyme participates in the biosynthesis of N-glycan and glycan structures.

This enzyme participates in the biosynthesis of chondroitin sulfate and glycan structures.

Asimilobine is an inhibitor of dopamine biosynthesis, and a serotonergic receptor antagonist.

1 Tryptamine biosynthesis pathway 2 Secologanin biosynthesis pathway Tryptamine and strictosidine to camptothecin Like all other monoterpenoid indole-alkaloids, biosynthesis of camptothecin requires production of the strictosidine. Strictosidine is synthesized through condensation reaction between trypamine from shikimate pathway and secologanin from either mevalonate (MVA) pathway or non-mevalonate pathway (MEP). Strictosidine then undergoes intermolecular cyclization to produce strictosamide, which is converted to camptothecin through a series of oxidation reactions by enzymes that still needs to be resolved. The shikimate pathway leading to biosynthesis of tryptamine is mostly understood.

Advances in the field of evolutionary genetics have also led to the proposal of trichothecene classification systems based on the pathway of their biosynthesis. Genes responsible for the biosynthesis of a mycotoxin are typically located in clusters; in Fusariumi these are known as TRI genes. TRI genes are each responsible for producing an enzyme that carries out a specific step in the biosynthesis of trichothecenes. Mutations in these genes can lead to the production of variant trichothecenes and therefore these moleules could be grouped on the basis of shared biosynthesis steps.

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.

Hardeman, H. van den Bosch, Topography of ether phospholipid biosynthesis, Biochim. Biophys. Acta 1006 (1989) 1–8. The first step of the biosynthesis is catalyzed by GNPAT. This enzyme acylates dihydroxyacetone phosphate (DHAP) at the sn-1 position.

Salutaridinol was first identified as an intermediate in the morphine biosynthesis pathway in the mid 1960s.Barton, D. H. R., et al. "444. Investigations on the biosynthesis of morphine alkaloids." Journal of the Chemical Society (Resumed) (1965): 2423-2438.

SREB proteins are indirectly required for cholesterol biosynthesis and for uptake and fatty acid biosynthesis. These proteins work with asymmetric sterol regulatory element (StRE). SREBPs have a structure similar to E-box-binding helix-loop-helix (HLH) proteins. However, in contrast to E-box-binding HLH proteins, an arginine residue is replaced with tyrosine making them capable of recognizing StREs and thereby regulating membrane biosynthesis.

In mammals and humans, αKG-dependent dioxygenase have functional roles in biosyntheses (e.g. collagen biosynthesis and L-carnitine biosynthesis), post-translational modifications (e.g. protein hydroxylation), epigenetic regulations (e.g. histone and DNA demethylation), as well as sensors of energy metabolism.

The biosynthesis of the tropane alkaloids have attracted intense interest because of their high physiological activity as well as the presence of the bicyclic tropane core. Final stages in the pathway for the biosynthesis of the tropane alkaloid cocaine.

See also: Vancomycin#Biosynthesis Chloroeremomycin was found to be synthesized by Amycolatopsis orientalis.

This enzyme participates in glycine, serine and threonine metabolism and aminoacyl-trna biosynthesis.

This enzyme participates in d-glutamine and d-glutamate metabolism and peptidoglycan biosynthesis.

This enzyme participates in glycine, serine and threonine metabolism and aminoacyl-trna biosynthesis.

Alternatively, β-alanine can be diverted into pantothenic acid and coenzyme A biosynthesis.

ALOXE3 is also a protein coding gene, more focusing on Prostaglandin 2 biosynthesis.

Geranylfarnesyl pyrophosphate is an intermediate used by organisms in the biosynthesis of sesterterpenoids.

E1210 is an isoxazole-based broad-spectrum antifungal. E1210 targets GPI- protein biosynthesis.

Marmesin (nodakenetin) is a chemical compound precursor in psoralen and linear furanocoumarins biosynthesis.

Schiff base formation confirms the biosynthesis of the N-methyl-Δ1-pyrrolinium cation.

In plant physiology, lovastatin has occasionally been used as inhibitor of cytokinin biosynthesis.

This enzyme participates in arginine and proline biosynthesis. It employs one cofactor, NAD+.

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

However, it is a key intermediate in the biosynthesis of the other phosphoglycerides.

In chlorophyll biosynthesis, the enzyme magnesium chelatase converts it into Mg-protoporphyrin IX.

1.95), serC (EC 2.6.1.52), and serB (EC 3.1.3.3).Uniprot: serB Serine biosynthesis Glycine biosynthesis: Serine hydroxymethyltransferase (SHMT = serine transhydroxymethylase) also catalyzes the reversible conversions of L-serine to glycine (retro-aldol cleavage) and 5,6,7,8-tetrahydrofolate to 5,10-methylenetetrahydrofolate (mTHF) (hydrolysis).

Examples of these biosynthetic pathways include the production of lipid membrane components and nucleotides. Biosynthesis is usually synonymous with anabolism. The prerequisite elements for biosynthesis include: precursor compounds, chemical energy (e.g. ATP), and catalytic enzymes which may require coenzymes (e.g.

Originally isolated from the plant Rauvolfia serpentina, a medicinal plant widely used in Indian folk medicine, this enzyme participates in terpenoid biosynthesis and indole and ipecac alkaloid biosynthesis, both of which produce many compounds with significant physiological and medicinal properties.

Goss completed her undergraduate studies in Chemistry at the University of Durham in 1997. Under the supervision of Prof. David O'Hagan, Goss completed her Ph.D. studying the biosynthesis of various natural products including the stereochemistry of enzymatic fluorination in fluoroacetate biosynthesis.

Wolf, G.; Berger, C. R. A. Studies on the biosynthesis and turnover of carnitine. Arch. Biochem. Biophys. 1961, 92, 360–365.Paik, W. K.; Nochumson, S.; Kim, S. Carnitine biosynthesis via protein methylation. Trends Biochem. Sci. 1977, 2, 159–161.

The biosynthesis of nargenicin is believed to be closely related to fatty acid biosynthesis to produce a polyketide chain. David E. Cane and colleagues have used feeding experiments to determine that nargenicin is derived from common precursors acetate and propionate. Proposed Biosynthesis of Nargenicin. The polyketide chain produced then undergoes a ring closure to form the large lactone ring and a Diels–Alder reaction to form the fused cyclohexane/cyclohexene rings.

The seminal proposal for the biosynthesis of leinamycin was published in Chemistry & Biochemistry in 2004. This biosynthesis consists of a discrete and modular NRPS, AT-less PKSs, and PKS modules. NRPS-PKS assembly line dictates the loading of D-Ala to initiate biosynthesis, followed by the loading of L-Cys to the peptidyl carrier protein (PCP). The dipeptide is then cyclized and oxidized to form the thiazonyl-S-PCP intermediate.

In collaboration with Samuel Gurin at the University of Pennsylvania, Brady discovered the enzyme system for the biosynthesis of long chain fatty acids,Brady RO, Gurin S. The biosynthesis of fatty acids by cell-free or water-soluble enzyme systems. J Biol Chem 1952; 199: 421–431 and later discovered the role of malonate coenzyme A in this process.Brady RO. Biosynthesis of fatty acids. II. Studies with enzymes from rat brain.

COX15 multimerization is important for heme A biosynthesis and/or transfer to maturing COX.

It plays dominant roles in L-selectin ligand biosynthesis, lymphocyte homing and lymphocyte trafficking.

This enzyme participates in fatty acid elongation in mitochondria and polyunsaturated fatty acid biosynthesis.

This enzyme participates in biosynthesis of steroids. It has 2 cofactors: FAD, and FMN.

CTP synthase is an enzyme involved in pyrimidine biosynthesis that interconverts UTP and CTP.

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

This enzyme participates in valine, leucine and isoleucine biosynthesis. It employs one cofactor, ascorbate.

This enzyme participates in porphyrin and chlorophyll biosynthesis. It employs one cofactor, pyridoxal phosphate.

This enzyme participates in the MEP pathway (non-mevalonate pathway) of isoprenoid precursor biosynthesis.

Blocking pyrimidine salvage can prevent DNA and RNA biosynthesis, resulting in reduced cell proliferation.

Vindoline is a chemical precursor to vinblastine. Vindoline is formed through biosynthesis from Tabersonine.

Isotope labeling may also be used to identify the pathways used in phycotoxin biosynthesis.

Biosynthesis of the compound is hypothesized to proceed via a NIH shift of anethole.

Experiments to clarify the function of these enzymes in gephyronic acid biosynthesis are underway.

The stereochemistry reported by Kato et al. in 1973 is different than that shown in the biosynthesis references. The stereochemistry of momilactone B shown here is based on the biosynthesis references. There are no known papers correcting the stereochemistry from the isolation paper.

By inactivating salC the researchers have demonstrated that salinomycin biosynthesis proceeds via a diene intermediate.

This enzyme participates in tyrosine metabolism and alkaloid biosynthesis. It employs one cofactor, pyridoxal phosphate.

Reaction sequence accounting for precursor of the tetraene structure required for biosynthesis of endiandric acids.

This enzyme participates in 3 metabolic pathways: glycosylphosphatidylinositol(gpi)-anchor, and glycan structures - biosynthesis 2.

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

This enzyme participates in alkaloid biosynthesis i. It employs one cofactor, heme- thiolate(P-450).

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

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

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

This enzyme participates in lysine biosynthesis and lysine degradation. It employs one cofactor, pyridoxal phosphate.

Three scytonemin biosynthetic enzymes are necessary, denoted as ScyA-C. Scytonemin biosynthesis in Lyngbya aestuarii.

6-pyruvoyltetrahydropterin synthase, also known as PTS, is a human gene which facilitates folate biosynthesis.

The biosynthesis of terphenylquinones is carried out by dimerization of substituted oxophenylpropanoic acids (phenylpyruvic acids).

Galanie, Stephanie, et al. "Complete biosynthesis of opioids in yeast." Science 349.6252 (2015): 1095-1100.

The following is the proposed biosynthesis of viomycin using NRPS-catalyzed peptide synthesis. There are five modules for cyclic pentapeptide biosynthesis, including one that lacks an adenylation domain (A). It is therefore proposed that one of the other A domains functions twice. Additionally, the NRPS subunits are not suspected to function in the order in which their genes are arranged, a characteristic of viomycin biosynthesis that is unlike typical NRPS-catalyzed peptide synthesis.

There are two major factors that lead to deficiency of CoQ10 in humans: reduced biosynthesis, and increased use by the body. Biosynthesis is the major source of CoQ10. Biosynthesis requires at least 12 genes, and mutations in many of them cause CoQ deficiency. CoQ10 levels also may be affected by other genetic defects (such as mutations of mitochondrial DNA, ETFDH, APTX, FXN, and BRAF, genes that are not directly related to the CoQ10 biosynthetic process).

This domain contains both N-acetyl- glutamine semialdehyde dehydrogenase (AgrC), which is involved in arginine biosynthesis, and aspartate-semialdehyde dehydrogenase, an enzyme involved in the biosynthesis of various amino acids from aspartate. It also contains the yeast and fungal Arg5,6 protein, which is cleaved into the enzymes N-acetyl- gamma-glutamyl-phosphate reductase and acetylglutamate kinase. These are also involved in arginine biosynthesis. All proteins in this entry contain a dimerisation domain of semialdehyde dehydrogenase.

Riboswitch sequences (in the mRNA leader transcript) bind molecules such as amino acids, nucleotides, sugars, vitamins, metal ions and other small ligands which cause a conformational change in the mRNA. Most of these attenuators are inhibitory and are employed by genes for biosynthetic enzymes or transporters whose expression is inversely related to the concentration of their corresponding metabolites. Example- Cobalamine biosynthesis, Cyclic AMP-GMP switch, lysin biosynthesis, glycine biosynthesis, fluroide switch etc.

However, no xylan synthase complexes have been isolated from Arabidopsis tissues (dicot). The first gene involved in the biosynthesis of xylan was revealed on xylem mutants (irx) in Arabidopsis thaliana because of some mutation affecting xylan biosynthesis genes. As a result, abnormal plant growth due to thinning and weakening of secondary xylem cell walls was seen. Arabidopsis mutant irx9 (At2g37090), irx14 (At4g36890), irx10/gut2 (At1g27440), irx10-L/gut1 (At5g61840) showed defect in xylan backbone biosynthesis.

Glutamate-5-semialdehyde is a non-proteinogenic amino acid involved in the biosynthesis of proline and arginine (via ornithine), as well as in the biosynthesis of antibiotics, such as carbapenems. It is synthesized by the reduction of glutamyl-5-phosphate by glutamate-5-semialdehyde dehydrogenase.

The enzyme from the pathogenic fungus Aspergillus fumigatus catalyzes a step in the biosynthesis of the siderophores triacetylfusarinine and desferriferricrocin, while the enzyme from the bacterium Kutzneria 744 is involved in the biosynthesis of piperazate, a building block of the kutzneride family of antifungal antibiotics.

Another major role of SAM-e is in polyamine biosynthesis. Here, SAM-e is decarboxylated by adenosylmethionine decarboxylase (EC 4.1.1.50) to form S-adenosylmethioninamine. This compound then donates its n-propylamine group in the biosynthesis of polyamines such as spermidine and spermine from putrescine.

Phosphoglucosamine mutase (PNGM) participates in the biosynthesis of UDP-N-Acetylglucosamine (UDP-GlcNAc). This bacterial enzyme has been conserved throughout evolution and is involved in the cytoplasmic steps of peptidoglycan biosynthesis, which is essential for bacterial survival and is also not present in humans.

Dolichyl monophosphate is an essential glycosyl carrier lipid for C- and O-mannosylation and N-glycosylation of proteins and for biosynthesis of glycosylphosphatidylinositol anchors in endoplasmic reticulum (ER). Dolichol kinase catalyzes CTP-mediated phosphorylation of dolichol, the terminal step in de novo dolichyl monophosphate biosynthesis.

This enzyme participates in terpenoid biosynthesis. This protein may use the morpheein model of allosteric regulation.

This enzyme participates in monoterpenoid biosynthesis and is localized to Leucoplasts of oil gland secretory cells.

Multiple translation factor family GTPases play important roles in initiation, elongation and termination of protein biosynthesis.

Third Edition ed.; Wiley&Sons;: West Sussex, England, 2009; p 230-232. Biosynthesis mechanism of Bilobalide.

The YgbB protein domain has a main function of being involved in terpenoid and isoprenoid biosynthesis.

This enzyme participates in 3 metabolic pathways: methionine metabolism, selenoamino acid metabolism, and aminoacyl-trna biosynthesis.

The biosynthesis of tyrocidine involves three enzymes. Parts of its sequence are identical to gramicidin S.

Metabolic gene clusters are also involved in nutrient acquisition, toxin degradation, antimicrobial resistance, and vitamin biosynthesis.

2.2), AIR synthetase (FGAM cyclase) (EC 6.3.3.1) activity which is required for de novo purine biosynthesis.

This enzyme participates in monoterpenoid biosynthesis and limonene and pinene degradation. It employs one cofactor, heme.

Natural biosynthesis of vitamin C occurs in many plants, and animals, by a variety of processes.

The core biosynthetic enzymes are thought to include 3 proteins for the biosynthesis of the α-ketopyrrole moiety, 5 for modular type I polyketide synthases for the spiroketal ring, 4 for the biosynthesis of 3-hydroxyanthranilic acid, an N-methyltransferase tailoring enzyme, and a type II thioesterase.

The pathway used is called the ubiquinone biosynthesis pathway, it catalyzes the first step in the biosynthesis of ubiquinone in E. coli. Ubiquinone is a lipid-soluble electron- transporting coenzyme. They are essential electron carriers in prokaryotes and are essential in aerobic organisms to achieve ATP.

The biosynthesis of cycloartenol starts from the triterpenoid squalene. It is the first precursor in the biosynthesis of other stanols and sterols, referred to as phytostanols and phytosterols in photosynthetic organisms and plants. The identities and distribution of phytostanols and phytosterols is characteristic of a plant species.

Pathway for the biosynthesis of trans-cinnamaldehyde. The biosynthesis of cinnamaldehyde begins with deamination of L-phenylalanine into cinnamic acid by the action of phenylalanine ammonia lyase (PAL). PAL catalyzes this reaction by a non-oxidative deamination. This deamination relies on the MIO prosthetic group of PAL.

Lipid biosynthesis is biochemically complex, involving multiple enzyme-dependent steps that can lead to isotope fractionations. There are three major pathways of lipid biosynthesis, known as the mevalonate pathway, the acetogenic pathway, and the 1-deoxyD-xylulose-5-phosphate/2-methylerythroyl-4-phosphate pathway. The acetogenic pathway is responsible for the production of n-alkyl lipids like leaf waxes, and is associated with a smaller δD depletion relative to source water than the other two lipid biosynthesis pathways.

Ginkgotoxin is the 4'-O-methyl derivative of vitamin B6 (pyridoxine), but the presence of the vitamin is not required for the biosynthesis of ginkgotoxin. It indicates that the pyridoxine system can be synthesized de novo in the cells of Ginkgo biloba. Biosynthesis of ginkgotoxin The first step of the biosynthesis involves ribulose 5-phosphate and dihydroxyacetone phosphate. They react in the presence of a synthase complex consisting of Pdx1 and Pdx2, and form pyridoxal phosphate.

Fenpropimorph is a morpholine-derived fungicide used in agriculture, primarily on cereal crops such as wheat. It has been reported to disrupt eukaryotic sterol biosynthesis pathways, notably by inhibiting fungal Δ14 reductases. It has also been reported to inhibit mammalian sterol biosynthesis by affecting lanosterol demethylation. Although used in agriculture for pest management purposes, it has been reported to have a strong adverse effect on sterol biosynthesis in higher-plants by inhibiting the cycloeucalenol-obtusifoliol isomerase.

Although there may not be a precise elucidation of Pancratistatin biological synthesis, there have been speculations on biosynthesis of Narciclasine and Lycoricidine that are very similar to Pancratistatin in terms of structure. The biosynthesis is accomplished via synthesis from O-methylnorbelladine 4 by para-para phenol coupling to obtain vittatine 5 as an intermediate. Subsequent elimination of two carbon atoms and hydroxylations of compound 5 (vittatine) then leads to narciclasine.Fuganti, C; Staunton, J; Battersby, AR. The biosynthesis of narciclasine.

This enzyme participates in 3 metabolic pathways: glutamate metabolism, porphyrin and chlorophyll metabolism, and aminoacyl-trna biosynthesis.

The same C-7/C-12 attack occurs in the biosynthesis of DXR, in a similar fashion.

797 PABA (center) is the basis for the inhibitory activity of sulfa drugs on tetrahydrofolate (right) biosynthesis.

A diarylheptanoid is an intermediate in the biosynthesis of phenylphenalenones in Anigozanthos preissii or Wachendorfia thyrsiflora (Haemodoraceae).

This enzyme participates in 3 metabolic pathways: pyrimidine metabolism, beta-alanine metabolism, and pantothenate and coa biosynthesis.

4,5-Dihydroorotic acid is a derivative of orotic acid which serves as an intermediate in pyrimidine biosynthesis.

Carbamoyl aspartic acid (or ureidosuccinic acid) is a carbamate derivative, serving as an intermediate in pyrimidine biosynthesis.

This enzyme participates in alanine and aspartate metabolism and tetracycline biosynthesis. It employs one cofactor, pyridoxal phosphate.

ORMDL sphingolipid biosynthesis regulator 1 is a protein that in humans is encoded by the ORMDL1 gene.

This enzyme participates in N-glycan biosynthesis. In humans dolichol kinase is encoded by the DOLK gene.

Desmosine has pathways for form multiple conformations of itself, both through biosynthesis and through man- made systems.

By contrast, the term "assimilatory" would be used in relation to the biosynthesis of organo-sulfur compounds.

The biosynthesis of apparicine requires alteration of the usual tryptamine side chain with loss of C-1.

At least three biological pathways support trehalose biosynthesis. An industrial process can derive trehalose from corn starch.

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.

Further oxidation at C3 forms the β-ketohydroxyl which upon elimination of H2O completes the proposed biosynthetic pathway of α-santonin.Barton, D.H.R.; Moss, G.P.; Whittle, J.A.; “Investigations on the Biosynthesis of Steroids and Terpenoids. Part I. A Preliminary Study of the Biosynthesis of Santonin”. (1968). J. Chem. Soc.

Arabidopsis mutants irx7, irx8, and parvus are thought to be related to the reducing end oligosaccharide biosynthesis. Thus, many genes have been associated with xylan biosynthesis but their biochemical mechanism is still unknown. Zeng et al. (2010) immuno- purified xylan synthase activity from etiolated wheat (Triticum aestivum) microsomes.

This enzyme is also called 5-O-(1-carboxyvinyl)-3-phosphoshikimate phosphate-lyase. This enzyme participates in phenylalanine, tyrosine and tryptophan biosynthesis. Chorismate synthase catalyzes the last of the seven steps in the shikimate pathway which is used in prokaryotes, fungi and plants for the biosynthesis of aromatic amino acids. It catalyzes the 1,4-trans elimination of the phosphate group from 5-enolpyruvylshikimate-3-phosphate (EPSP) to form chorismate which can then be used in phenylalanine, tyrosine or tryptophan biosynthesis.

This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is dTDP-glucose 4,6-hydro-lyase (dTDP-4-dehydro-6-deoxy-D-glucose-forming). Other names in common use include thymidine diphosphoglucose oxidoreductase, TDP-glucose oxidoreductase, RmlB, DESIV, and dTDP-glucose 4,6-hydro-lyase. This enzyme participates in 4 metabolic pathways: nucleotide sugars metabolism, streptomycin biosynthesis, polyketide sugar unit biosynthesis, and biosynthesis of vancomycin group antibiotics.

Prof Alan Battersby lecturing on porphyrin biosynthesis. Alan Battersby is, above all, known for his research on the biosynthesis of the "pigments of life" that are built on closely related tetrapyrrolic structural frameworks. His research group elucidated, in particular, the essential role played by two enzymes, deaminase and cosynthetase, in the steps from aminolevulinic acid via porphobilinogen and hydroxymethylbilane to uroporphyrinogen III. The latter is the first macrocyclic intermediate in the biosynthesis of haem, chlorophyll, vitamin B12 (cobalamin), sirohaem and cofactor F430.

A number of factors affect sponge metabolite production, with metabolite concentration varying greatly between neighbouring explants. Localised differences in light intensity and bio-fouling are physical and biological factors that have been found to significantly affect metabolite biosynthesis in sponges. Changes in environmental factors may alter microbial populations and subsequently affect metabolite biosynthesis. Understanding the environmental factors that affect metabolite biosynthesis or the ecological role of the metabolite, can be used as a competitive advantage to maximise metabolite production and total yield.

Dolichol phosphate-mannose biosynthesis regulatory protein is a protein that in humans is encoded by the DPM2 gene.

Ubiquinone biosynthesis protein COQ4 homolog, mitochondrial is a protein that in humans is encoded by the COQ4 gene.

Phosphatidylinositol-glycan biosynthesis class F protein is a protein that in humans is encoded by the PIGF gene.

This enzyme participates in 3 metabolic pathways: carbazole degradation, benzoate degradation via coa ligation, and acridone alkaloid biosynthesis.

This protein domain provides the precursors necessary for DNA synthesis. It catalyses the biosynthesis of DNA from RNA.

This enzyme participates in pantothenate and coa biosynthesis. It has 5 cofactors: ammonia, manganese, cobalt, potassium, and NH4+.

Phosphatidylinositol glycan anchor biosynthesis class W is a protein that in humans is encoded by the PIGW gene.

J. Chem. Soc. D: Chem. Commun. 1971, 19, 1154–1155. Pancratistatin-like biosynthesis using Narciclasine as a model.

Although the biosynthesis of saxitoxin seems complex, organisms from two different kingdoms, indeed two different domains, species of marine dinoflagellates and freshwater cyanobacteria, are capable of producing these toxins. While the prevailing theory of production in dinoflagellates was through symbiotic mutualism with cyanobacteria, evidence has emerged suggesting that dinoflagellates, themselves, also possess the genes required for saxitoxin synthesis. Saxitoxin biosynthesis is the first non-terpene alkaloid pathway described for bacteria, though the exact mechanism of saxitoxin biosynthesis is still essentially a theoretical model. The precise mechanism of how substrates bind to enzymes is still unknown, and genes involved in the biosynthesis of saxitoxin are either putative or have only recently been identified.

Pinoresinol biosynthesis involved a protein called a dirigent protein. The first dirigent protein was discovered in Forsythia intermedia. This protein has been found to direct the stereoselective biosynthesis of (+)-pinoresinol from coniferyl alcohol monomers. Recently, a second, enantiocomplementary dirigent protein was identified in Arabidopsis thaliana, which directs enantioselective synthesis of (−)-pinoresinol.

In enzymology, a phosphoribosylanthranilate isomerase [ PRAI ] () is an enzyme that catalyzes the third step of the synthesis of the amino acid tryptophan. This enzyme participates in the phenylalanine, tyrosine and tryptophan biosynthesis pathway, also known as the aromatic amino acid biosynthesis pathway In yeast it is encoded by the TRP1 gene.

This enzyme participates in phenylalanine, tyrosine and tryptophan biosynthesis and two-component system - general. It employs one cofactor, pyruvate.

This is expected to be able to give all characteristic sesquiterpenes in Illicium plants a reasonable explanation of biosynthesis.

The biosynthesis of prunasin occurs in the tegument, then transported to other tissues for conversion to amygdalin or degraded.

This enzyme participates in 3 metabolic pathways: bile acid biosynthesis, c21-steroid hormone metabolism, and androgen and estrogen metabolism.

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

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

It exerts its bacteriocidal effect by inhibiting cell wall biosynthesis, acting by inhibiting the transglycosylation step of peptidoglycan synthesis.

The swi and mis clusters both include four large genes encoding PKS enzymes and a gene encoding for the AT protein, but the order of the genes differs (Figure 4). In the swi biosynthesis gene cluster, first gene, SwiC, is on the reverse strand and the other four genes are facing the forward direction. In the mis biosynthesis gene cluster, all genes are oriented in the same direction. Although this is different, both swi and mis biosynthesis gene clusters are composed of similar catalytic domains.

Arabidopsis mutant (FLU), unable to control biosynthesis of protochlorophyllide, glows red in the blue light. Protochlorophyllide,KEGG compound database entry or monovinyl protochlorophyllide, is an intermediate in the biosynthesis of chlorophyll a. It lacks the phytol side-chain of chlorophyll and the reduced pyrrole in ring D. Protochlorophyllide is highly fluorescent; mutants that accumulate it glow red if irradiated with blue light.Meskauskiene R, Nater M, Goslings D, Kessler F, op den Camp R, Apel K. FLU: a negative regulator of chlorophyll biosynthesis in Arabidopsis thaliana.

The CHKB gene encodes for a key protein in phospholipid biosynthesis. The choline kinase (CK) and ethanolamine kinase (EK) proteins, which are coded by the CHKB gene, catalyze the phosphorylation of choline/ethanolamine in vitro to phosphocholine/phosphoethanolamine. The catalysis is controlled by ATP in the presence of magnesium and ADP, and commits choline to the enzymatic pathway for biosynthesis of phosphatidylcholine. This is the first step in the biosynthesis of phosphocholine/phosphoethanolamine in all animal cells, and is done by the Kennedy pathway.

Biosynthesis of N-methyl-pyrrolinium cation Biosynthesis of cocaine Robinson biosynthesis of tropane Reduction of tropinone The first synthesis and elucidation of the cocaine molecule was by Richard Willstätter in 1898. Willstätter's synthesis derived cocaine from tropinone. Since then, Robert Robinson and Edward Leete have made significant contributions to the mechanism of the synthesis. (-NO3) The additional carbon atoms required for the synthesis of cocaine are derived from acetyl-CoA, by addition of two acetyl-CoA units to the N-methyl-Δ1-pyrrolinium cation.

Flavonoid biosynthesis gene regulation occurs through the interaction of different transcription factors. Depending on the combination of transcription factor interactions, the structural genes involved in flavonoid biosynthesis are expressed in specific locations of the plant and at specific times. Many myeloblastosis (MYB) transcription factors have been identified in a variety of fruits and plants, including strawberries, maize, and arabidopsis, as being important in the regulation of flavonoid biosynthesis and accumulation. These transcription factors continue to be studied in plant model organisms such as maize and Arabidopsis.

In humans, phenylalanine hydroxylase deficiency can cause phenylketonuria, the most common inborn error of amino acid metabolism. Phenylalanine hydroxylase catalyzes the conversion of to . Tyrosine hydroxylase catalyzes the rate-limiting step in catecholamine biosynthesis: the conversion of to . Similarly, tryptophan hydroxylase catalyzes the rate-limiting step in serotonin biosynthesis: the conversion of to .

Biosynthesis of (+)-pisatin The biosynthesis of pisatin begins with the amino acid L-phenylalanine. A deamination reaction then produces trans-cinnamate, which undergoes hydroxylation to form 4-coumarate. Acetyl-CoA is then added to form 4-coumaryl-CoA. Three malonyl-CoA moities are then added and cyclized to introduce a phenol ring.

The complete biosynthesis of thapsigargin has yet to be elucidated. A proposed biosynthesis starts with the farnesyl pyrophosphate. The first step is controlled by the enzyme germacrene B synthase. In the second step, the C(8) position is easily activated for an allylic oxidation due to the position of the double bond.

The biosynthesis of cucurbitacin C has been described. Zhang et al. (2014) identified nine cucumber genes in the pathway for biosynthesis of cucurbitacin C and elucidated four catalytic steps. These authors also discovered the transcription factors Bl (Bitter leaf) and Bt (Bitter fruit) that regulate this pathway in leaves and fruits, respectively.

Biosynthetic mechanism for the moenocinol lipid tail of moenomycin A. From farnesyl derivative and geranyl pyrophosphate: 1. Cyclization and pyrophosphate elimination 2. Ring expansion 3. Base catalyzed ring opening Extensive exploration into the biosynthesis of the moenomycin family has been conducted to better inform the genetic engineering and biosynthesis of novel moenomycin analogues.

This is because estradiol lowers the GnRH pulse frequency and amplitude required to stimulate the biosynthesis and secretion of LH.

It has also been identified as the enzyme which inserts nickel into sirohydrochlorin in the biosynthesis of cofactor F430, reaction .

Subsequently the prostoglandins are moved to the cerata. The biosynthesis of prostgandins has been studied by Marzo et al. (1991).

Neurosporene is a carotenoid pigment. It is an intermediate in the biosynthesis of lycopene and a variety of bacterial carotenoids.

TarB inhibits the expression of Toxin coregulated pilus biosynthesis protein F (TcpF). It does not act in conjunction with Hfq.

Corticosteroid biosynthetic pathway in rat A steroid hydroxylase is a class of hydroxylase enzymes involved in the biosynthesis of steroids.

Other names in common use include isoflavone 2'-monooxygenase, CYP81E1, and CYP Ge-3. This enzyme participates in isoflavonoid biosynthesis.

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

As steroid biosynthesis requires molecular oxygen, fossil steranes have been used to draw inferences about aerobiosis in the early Precambrian.

In the general porphyrin biosynthesis pathway, uroporphyrinogen III is derived from the linear tetrapyrrole preuroporphyrinogen (a substituted hydroxymethylbilane) by the action of the enzyme uroporphyrinogen-III cosynthase. alt=Biosynthesis of Uroporphyrinogen-III from pre-uroporphyrinogen The conversion entails a reversal of the last pyrrole unit (thus swapping the acetic and propionic acid groups) and a condensation reaction that closes the macrocycle by eliminating the final hydroxyl with a hydrogen atom of the first ring. In the biosynthesis of hemes and chlorophylls, uroporphyrinogen III is converted into coproporphyrinogen III by the enzyme uroporphyrinogen III decarboxylase. In the biosynthesis of sirohemes, uroporphyrinogen III is converted by two methyl transferases to dihydrosirohydrochlorin, which is subsequently oxidized sirohydrochlorin, a precursor to the siroheme prosthetic group.

Gluconacetobacter hansenii is a species of acetic acid bacteria, notable as the model organism for the biosynthesis of bacterial celluloseRoss, P., Mayer, R., & Benziman, M. (1991) "Cellulose biosynthesis and function in bacteria", Microbiological Reviews, 55(1), 35-58.Römling, U. (2002) "Molecular biology of cellulose production in bacteria", Research in microbiology, 153(4), 205-212.

They are required for the utilization of free lipoic acid. Octanoyl-(acyl carrier protein):protein N-octanoyltransferases, or octanoyltransferases, are required for lipoic acid biosynthesis. They transfer octanoate from the acyl carrier protein (ACP), part of fatty acid biosynthesis, to the specific lysine residue of lipoyl domains. Two octanoyltransferase isozymes exist in this superfamily.

Molybdenum cofactor biosynthesis protein 1 is a protein that in humans and other animals, fungi, and cellular slime molds, is encoded by the MOCS1 gene. Both copies of this gene are defective in patients with molybdenum cofactor deficiency, type A. Molybdenum cofactor biosynthesis is a conserved pathway leading to the biological activation of molybdenum. The protein encoded by this gene is involved in molybdopterin biosynthesis. (This gene was originally thought to produce a bicistronic mRNA with the potential to produce two proteins (MOCS1A and MOCS1B) from adjacent open reading frames.

The pheromone biosynthesis activation neuropeptide (PBAN) is a neurohormone (member of the PBAN/pyrokinin neuropeptide family) that activates the biosynthesis of pheromones in moths. Female moths release PBAN into their hemolymph during the scotophase to stimulate the biosynthesis of the unique pheromone that will attract the conspecific males. PBAN release is drastically reduced after mating, contributing to the loss in female receptivity. In Agrotis ipsilon (black cutworm), it has been shown that the Juvenile Hormone helps induce release of PBAN which goes on to influence pheromone production and responsiveness in females and males, respectively.

He also uses the enzyme dihydrofolate reductase and the pathway for de novo purine biosynthesis to gain insights into enzymatic catalysis.

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

Geraniol is important in biosynthesis of other terpenes. For example, myrcene and ocimene are formed by dehydration and isomerization of geraniol.

COQ3, also known as ubiquinone biosynthesis O-methyltransferase, mitochondrial is an enzyme that in humans is encoded by the COQ3 gene.

While the biosynthesis has not been conclusively elucidated, brevianamide A and B are constructed from tryptophan, proline, and an isoprene unit.

If the RNA polymerase reaches the terminator (at the end of the DNA strand), the enzymes for tryptophan biosynthesis are expressed.

Other names in common use include tabersonine-11-hydroxylase, and T11H. This enzyme participates in terpene indole and ipecac alkaloid biosynthesis.

Biosynthesis of heme which involves many enzymatic steps which begin in the mitochondrion and ends in the cytoplasm of the cell.

Tyrosine ammonia lyase (TAL) is an enzyme in the natural phenols biosynthesis pathway. It transforms L-tyrosine into p-coumaric acid.

Etifoxine stimulates the biosynthesis of endogenous neurosteroids, for example: allopregnanolone (3-alpha,5-alpha THP), a nanomolar potentiator of GABA activity.

Several studies of thiopeptide biosynthesis have been contemporarily published in 2009 and two of them (Liao et al. and Kelly et al.) included the similar biosynthesis of thiostrepton: it's ribosomally synthesized from thiostrepton biosynthetic genes (tsr genes) and posttranslational modification is needed. A total synthesis of thiostrepton was completed by K.C. Nicolaou, et al. in 2004.

Isopentenyl pyrophosphate (IPP, isopentenyl diphosphate, or IDP) is an isoprenoid precursor. IPP is an intermediate in the classical, HMG-CoA reductase pathway (commonly called the mevalonate pathway) and in the non- mevalonate MEP pathway of isoprenoid precursor biosynthesis. Isoprenoid precursors such as IPP, and its isomer DMAPP, are used by organisms in the biosynthesis of terpenes and terpenoids.

Historically, it has been assumed that astaxanthin biosynthesis proceeds along both routes. However, recent work has suggested that efficient biosynthesis may, in fact, proceed from beta-carotene to astaxanthin via zeaxanthin. The production of astaxanthin by metabolic engineering, in isolation, will not provide a suitable alternative to current industrial methods. Rather, a bioprocess approach should be adopted.

All the bergamotenes are biosynthesized from farnesyl pyrophosphate via a variety of enzymes including exo-alpha-bergamotene synthase, (+)-endo-beta-bergamotene synthase, (-)-endo-alpha-bergamotene synthase, and others. Bergamotenes, in turn, are intermediates in the biosynthesis of more complex chemical compounds. For example, β-trans-bergamotene is a precursor in the biosynthesis of fumagillin, ovalicin, and related antibiotics.

Although the exact biosynthesis of bipinnatin J has not been formally studied, the biosynthesis the core cembrane skeleton, neo-cembrene, has been extensively studied. Starting from geranylgeranyl pyrophosphate, the pyrophosphate leaves, creating the allyl carbocation. A type A cyclization then yields the 14-membered cembrane ring with the isopropyl cation outside the ring. Proton elimination then yields neo-cembrene.

The addition of 3 malonyl-CoA monomers, cyclization, and release by the thioesterase PltG gives pyoluteorin. Pyoluteorin biosynthesis. Asterisk denotes inactive domain.

Asp is pervasive in biosynthesis. Because aspartate can be synthesized by the body it is classified as a non-essential amino acid.

Lipocortins control the biosynthesis of inflammation mediators, like prostaglandins and leukotrienes. Lipocortins can inhibit the common precursor of inflammation mediators, arachidonic acid.

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

S-Adenosylmethioninamine (decarboxylated S-adenosyl methionine) is a substrate that is involved in the biosynthesis of polyamines including spermidine, spermine, and thermospermine.

Pathway for biosynthesis of jasmonic acid via allene oxide intermediate. Highlighted is the pentadiene core that is the site of the reactions.

Six enzymes are required for its biosynthesis from TDP-glucose in Streptomyces venezuelae. Desosamine serves as the sugar donor in this formation.

PGC-1α has also been shown to drive NAD biosynthesis to play a large role in renal protection in Acute Kidney Injury.

Pathway for biosynthesis of jasmonic acid via allene oxide intermediate. Highlighted is the pentadiene core that is the site of the reactions.

The semicarbazone of the hydrochloride is another bench- stable precursor.upon Aminoacetone is a metabolite that is implicated in the biosynthesis of methylglyoxal.

Dumetorine is an alkaloid that can be isolated from Dioscorea dumetorum. Biosynthesis of dioscorine (highlighted) and dumetorine from trigonelline in Dioscorea hispida.

H., Walsh, C. T., Drennan, C. L., "Crystal structure of the non-haem iron halogenase SyrB2 in syringomycin biosynthesis", Nature 2006, 440, 368.

In addition, genetic infrastructure for sterol biosynthesis is observed in poribacterial genomes, otherwise found almost exclusively in eukaryotes and the planctomycete Gemmata obscuriglobus.

Dopachrome is a cyclization product of L-DOPA and is an intermediate in the biosynthesis of melanin. It may tautomerise to form DHICA.

Thomas J. R. et al. (1990) Structure, biosynthesis, and function of glycosylphosphatidylinositols. Biochemistry. 29, 5413-22.Ikezawa H. (2002) Glycosylphosphatidylinositol (GPI)-anchored proteins.

This enzyme participates in 3 metabolic pathways: fatty acid metabolism, polyunsaturated fatty acid biosynthesis, and ppar signaling pathway. It employs one cofactor, FAD.

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

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

In terms of its biosynthesis, benzoate is produced in plants from cinnamic acid. A pathway has been identified from phenol via 4-hydroxybenzoate.

All of the genes necessary for the biosynthesis of annimycin are contained within a single 35 kb cluster. The biosynthetic structural genes, summarized in figure 2. consist of five open reading frames encoding the biosynthesis of the C5N group (ann1, ann2 and ann3 genes) and the polyenoic acid (genes ann4 and ann5). The genes ann4 and ann5 encode two polypeptides that correspond to a type 1 polyketide synthase PKS. The biosynthesis of the C5N ring was recently reconstructed. The ann2 gene encode for a 5-aminolevulinate synthase which condenses glycine and succinyl- CoA in a Claisen-like reaction to form 5-aminolevulinate.

The biosynthesis of pterins begins with guanosine triphosphate (GTP), which is the substrate for GTP cyclohydrolase I. The enzyme is found in both prokaryotes and eukaryotes. step in biosynthesis of dihydroneopterin from GTP. Molybdopterin biosynthesis occurs in four steps: (i) the radical-mediated cyclization of nucleotide, guanosine 5'-triphosphate (GTP), to (8S)‑3 ́,8‐cyclo‑7,8‑dihydroguanosine 5 ́‑triphosphate (3 ́,8‑cH2GTP), (ii) the formation of cyclic pyranopterin monophosphate (cPMP) from the 3 ́,8‑cH2GTP, (iii) the conversion of cPMP into molybdopterin (MPT), (iv) the insertion of molybdate into MPT to form Moco. The human enzymes are indicated in parenthesis.

Summary of heme B biosynthesis—note that some reactions occur in the cytoplasm and some in the mitochondrion (yellow) Ferrochelatase catalyzes the insertion of ferrous iron into protoporphyrin IX in the heme biosynthesis pathway to form heme B. The enzyme is localized to the matrix-facing side of the inner mitochondrial membrane. Ferrochelatase is the best known member of a family of enzymes that add divalent metal cations to tetrapyrrole structures. For example, magnesium chelatase adds magnesium to protoporphyrin IX in the first step of bacteriochlorophyll biosynthesis. Heme B is an essential cofactor in many proteins and enzymes.

Dewick, pp. 369–370 center Biosynthesis of monoterpenoid indole alkaloids begins with the Mannich reaction of tryptamine and secologanin; it yields strictosidine which is converted to 4,21-dehydrogeissoschizine. Then, the biosynthesis of most alkaloids containing the unperturbed monoterpenoid part (Corynanthe type) proceeds through cyclization with the formation of cathenamine and subsequent reduction to ajmalicine in the presence of nicotinamide adenine dinucleotide phosphate (NADPH). In the biosynthesis of other alkaloids, 4,21-dehydrogeissoschizine first converts into preakuammicine (an alkaloid of subtype strychnos, type Corynanthe) which gives rise to other alkaloids of subtype strychnos and of the types Iboga and Aspidosperma.

In enzymology, a dihydroxy-acid dehydratase () is an enzyme that catalyzes the chemical reaction :2,3-dihydroxy-3-methylbutanoate \rightleftharpoons 3-methyl-2-oxobutanoate + H2O Hence, this enzyme has one substrate, 2,3-dihydroxy-3-methylbutanoate, and two products, 3-methyl-2-oxobutanoate (α-ketoisovaleric acid) and H2O. This enzyme participates in valine, leucine and isoleucine biosynthesis and pantothenate and coenzyme A (CoA) biosynthesis.

Lysine biosynthesis pathways. Two pathways are responsible for the de novo biosynthesis of L-lysine, namely the (A) diaminopimelate pathway and (B) α‑aminoadipate pathway. Two pathways have been identified in nature for the synthesis of lysine. The diaminopimelate (DAP) pathway belongs to the aspartate derived biosynthetic family, which is also involved in the synthesis of threonine, methionine and isoleucine.

The addition of another methyl group transforms this compound into reticuline. Notably, biosynthesis of sanguinarine up to this point is virtually identical to that of morphine. However, instead of being converted to codeinone (as in the biosynthesis of morphine), reticuline is converted to scoulerine via berberine bridge enzyme (BBE). As such, this is the commitment step in the sanguinarine pathway.

Anne Elisabeth Osbourn is a professor of biology and director of the Norwich Research Park industrial biotechnology alliance at the John Innes Centre, where she investigates plant natural product biosynthesis. She recognised that in the plant genome, the genes involved with biosynthesis organise in clusters. She is also a popular science communicator, and founder of the Science, Art and Writing (SAW) Initiative.

Osbourn studies natural product biosynthesis. In particular, she has worked on the biosynthesis of triterpene. She identified that metabolic pathways organise in operon-like clusters, which allowed her to develop a novel opportunity to discover natural product pathways through genome mining. The natural products include terpenes, which can be used in the pharmaceutical industry as well as food and manufacturing.

ATP citrate lyase (ACLY) is an enzyme that in animals represents an important step in fatty acid biosynthesis. By converting citrate to acetyl-CoA, the enzyme links carbohydrate metabolism, which yields citrate as an intermediate, with fatty acid biosynthesis, which consumes acetyl-CoA. In plants, ATP citrate lyase generates cytosolic acetyl-CoA precursors of thousands of specialized metabolites, including waxes, sterols, and polyketides.

550, pp. 1647-1652). Trans Tech Publications Ltd. . De novo biosynthesis of liquiritin in Saccharomyces cerevisiae using endogenous yeast metabolites as precursors and cofactors, provides a possibility for the economical and sustainable production and application of licorice flavonoids through synthetic biologyYin, Y., Li, Y., Jiang, D., Zhang, X., Gao, W., & Liu, C. (2019). De novo biosynthesis of liquiritin in Saccharomyces cerevisiae.

The specific mechanism of how this enzyme works is still under investigation; however, it is known that this enzyme has the ability to couple together glyceraldehyde-3-phosphate with L-arginine in the presence of thiamine diphosphate (TDP or thiamine pyrophosphate), which is the first step of the clavulanic acid biosynthesis. Proposed mechanism of CEA synthetase in the biosynthesis of clavulanic acid.

Higher eukaryotes employ a similar reaction mechanism in ten reaction steps. Purine bases are synthesized by converting phosphoribosyl pyrophosphate (PRPP) to inosine monophosphate (IMP), which is the first key intermediate in purine base biosynthesis. Further enzymatic modification of IMP produces the adenosine and guanosine bases of nucleotides. # The first step in purine biosynthesis is a condensation reaction, performed by glutamine-PRPP amidotransferase.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is prephenate:NAD+ oxidoreductase (decarboxylating). Other names in common use include hydroxyphenylpyruvate synthase, and chorismate mutase---prephenate dehydrogenase. This enzyme participates in phenylalanine, tyrosine and tryptophan biosynthesis and novobiocin biosynthesis.

The environment of the plant has also been shown to affect the flavonoid biosynthesis pathway. Shorter wavelengths of light, ranging from blue to UV light, allow for higher production and accumulation of flavonoids in fruits. These wavelengths activate enzymes that are involved in the phenylpropanoid and flavonoid biosynthesis pathways, stimulating the production of flavonoids. The level of stimulation can vary between individual fruits.

In rice (Oryza sativa), for example, evidence suggests that the CCR1 homolog is an effector of Rac1, a small GTPase important for plant defense response. In this case, the Rac1 protein is proposed to activate CCR upon binding, leading to enhanced monolignol biosynthesis. Because Rac1 also activates NADPH oxidase, which produces peroxides critical for monolignol polymerization, overall lignin biosynthesis is enhanced as well.

It catalyzes the following reaction, the second step of the biosynthesis of porphyrin: :2 δ-aminolevulinic acid \rightleftharpoons porphobilinogen + 2 H2O It therefore catalyzes the condensation of 2 molecules of delta-aminolevulinate to form porphobilinogen (a precursor of heme, cytochromes and other hemoproteins). This reaction is the first common step in the biosynthesis of all biological tetrapyrroles. Zinc is essential for enzymatic activity.

In plants and microorganisms, isoleucine is biosynthesized from pyruvic acid and alpha-ketoglutarate. Enzymes involved in this biosynthesis include acetolactate synthase (also known as acetohydroxy acid synthase), acetohydroxy acid isomeroreductase, dihydroxyacid dehydratase, and Valine aminotransferase. In terms of regulation, the enzymes threonine deaminase, dihydroxy acid dehydrase, and transaminase are controlled by end-product regulation. i.e. the presence of isoleucine will downregulate threonine biosynthesis.

In enzymology, a lipopolysaccharide N-acetylglucosaminyltransferase () is an enzyme that catalyzes the chemical reaction :UDP-N-acetyl-D-glucosamine + lipopolysaccharide \rightleftharpoons UDP + N-acetyl-D- glucosaminyllipopolysaccharide Thus, the two substrates of this enzyme are UDP-N-acetyl-D-glucosamine and lipopolysaccharide, whereas its two products are UDP and N-acetyl-D-glucosaminyllipopolysaccharide. This enzyme participates in lipopolysaccharide biosynthesis and glycan structures - biosynthesis 2.

Michel Rohmer is working on isoprenoids, a class of natural substances familiar to all in the form of cholesterol in our cells. He studied hopanoids in particular, which are found in sedimentary rock materials. He then discovered biohopanoids, a family of pentacyclic triterpenoids. His work on the biosynthesis of these bacterial hopanoids is revolutionizing the understanding of the early stages of isoprenoid biosynthesis.

It is also the precursor to numerous other metabolites, including sphingolipids and folate, which is the principal donor of one-carbon fragments in biosynthesis.

This enzyme participates in 5 metabolic pathways: purine metabolism, starch and sucrose metabolism, riboflavin metabolism, nicotinate and nicotinamide metabolism, and pantothenate and coa biosynthesis.

The protein MAX1 has been proposed to catalyze the last step of the biosynthesis of strigolactones due its role in oxidative metabolism in plants.

Atromentin and leucomelone possess antibacterial activity, inhibiting the enzyme enoyl-acyl carrier protein reductase, (essential for the biosynthesis of fatty acids) in S. pneumoniae.

The biosynthesis of PBP was first shown through isotope feeding studies, and then biochemically when genomic data of PBP-producing strains became readily available.

Nucleoside antibiotics are a class of antibiotics that inhibit the Mray enzyme in peptidoglycan biosynthesis pathway of mycobacteria, gram positive and gram negative strains.

However, there are a few typical reactions involved in the biosynthesis of various classes of alkaloids, including synthesis of Schiff bases and Mannich reaction.

Isochorismate synthase (EC number 5.4.4.2) is an isomerase enzyme that catalyzes the first step in the biosynthesis of vitamin K2 (menaquinone) in Escherichia coli.

It is speculated that the presence of the light independent genes for chlorophyll biosynthesis is what allows A.lagunensis to persist in low light intensities.

Ubiquinone biosynthesis protein COQ9, mitochondrial, also known as coenzyme Q9 homolog (COQ9), is a protein that in humans is encoded by the COQ9 gene.

It exerts a bactericidal action against penicillin-sensitive microorganisms during the stage of active multiplication. It acts by inhibiting the biosynthesis of cell-wall peptidoglycan.

Glyceraldehyde 3-phosphate occurs as a byproduct in the biosynthesis pathway of tryptophan, an essential amino acid that cannot be produced by the human body.

Barofsky, Alexandra, and Georg Pohnert. "Biosynthesis of Polyunsaturated Short Chain Aldehydes in the Diatom Thalassiosira Rotula." Org. Lett. Organic Letters 9.6 (2007): 1017-020. Web.

Alan Richard Brash (born 1949) is a professor of pharmacology at Vanderbilt University. He is a leading authority on the biosynthesis of prostoglandins and eicosanoids.

In enzymology, a lysine-tRNA ligase () is an enzyme that catalyzes the chemical reaction :ATP + L-lysine + tRNALys \rightleftharpoons AMP + diphosphate + L-lysyl-tRNALys The 3 substrates of this enzyme are ATP, L-lysine, and tRNA(Lys), whereas its 3 products are AMP, diphosphate, and L-lysyl-tRNA(Lys). This enzyme participates in 3 metabolic pathways: lysine biosynthesis, aminoacyl-trna biosynthesis, and amyotrophic lateral sclerosis (als).

Plant Mol. Bio. 50, 473-503. Biosynthesis of 2-succinylbenzoic acid via the shikimate pathway After 2-succinylbenzoic acid has been produced, a cyclization, a prenylation, a methylation, and an oxidation occur which yields a naphthoquinone.Heide, L., Leistner, E. (1981) 2-Methoxycarbonyl-3-prenyl-1,4-naphthoquinone, a Metabolite related to the Biosynthesis of Mollugin and Anthraquinones in Galium mollugo L. J.C.S. Chem. Comm. 334-336.

Choline kinase beta (CK), also known as Ethanolamine kinase (EK), Choline kinase-like protein , choline/ethanolamine kinase beta (CKEKB), or Choline/ethanolamine kinase is a protein encoded by the CHKB gene. This gene is found on chromosome 22 in humans. The encoded protein plays a key role in phospholipid biosynthesis. Choline kinase (CK) and ethanolamine kinase (EK) catalyzes the first step in phosphatidylethanolamine biosynthesis.

In contrast, targeted mutation of sidA, the first gene in the siderophore biosynthesis pathway, proved siderophore-mediated iron uptake to be essential for virulence. Mutation of the downstream siderophore biosynthesis genes sidC, sidD, sidF and sidG resulted in strains of A. fumigatus with similar decreases in virulence. These mechanisms of iron uptake appear to work in parallel and both are upregulated in response to iron starvation.

3-Deoxy--arabino-heptulosonic acid 7-phosphate (DAHP) is a 7-carbon ulonic acid. This compound is found in the shikimic acid biosynthesis pathway and is an intermediate in the production of aromatic amino acids. Phosphoenolpyruvate and erythrose-4-phosphate react to form 3-deoxy-- arabinoheptulosonate-7-phosphate (DAHP), in a reaction catalyzed by the enzyme DAHP synthase. :Biosynthesis of DAHP from phosphoenolpyruvate and erythrose-4-phosphate.

Ergotamine is a secondary metabolite (natural product) and the principal alkaloid produced by the ergot fungus, Claviceps purpurea, and related fungi in the family Clavicipitaceae. Its biosynthesis in these fungi requires the amino acid L-tryptophan and dimethylallyl diphosphate. These precursor compounds are the substrates for the enzyme, tryptophan dimethylallyltransferase, catalyzing the first step in ergot alkaloid biosynthesis, i.e., the prenylation of L-tryptophan.

Biosynthesis is a multi-step, enzyme-catalyzed process where substrates are converted into more complex products in living organisms. In biosynthesis, simple compounds are modified, converted into other compounds, or joined together to form macromolecules. This process often consists of metabolic pathways. Some of these biosynthetic pathways are located within a single cellular organelle, while others involve enzymes that are located within multiple cellular organelles.

The serine family of amino acid includes: serine, cysteine, and glycine. Most microorganisms and plants obtain the sulfur for synthesizing methionine from the amino acid cysteine. Furthermore, the conversion of serine to glycine provides the carbons needed for the biosynthesis of the methionine and histidine. During serine biosynthesis, the enzyme phosphoglycerate dehydrogenase catalyzes the initial reaction that oxidizes 3-phospho-D- glycerate to yield 3-phosphonooxypyruvate.

Protein biosynthesis starting with transcription and post-transcriptional modifications in the nucleus. Then the mature mRNA is exported to the cytoplasm where it is translated. The polypeptide chain then folds and is post-translationally modified. Protein biosynthesis (or protein synthesis) is a core biological process, occurring inside cells, balancing the loss of cellular proteins (via degradation or export) through the production of new proteins.

Like plants, some fungal species (for example Cercospora rosicola, Botrytis cinerea and Magnaporthe oryzae) have an endogenous biosynthesis pathway for ABA. In fungi, it seems to be the MVA biosynthetic pathway that is predominant (rather than the MEP pathway that is responsible for ABA biosynthesis in plants). One role of ABA produced by these pathogens seems to be to suppress the plant immune responses.

Pathway of plasmalogen synthesis Biosynthesis of plasmalogens (PLs) begins with association of peroxisomal matrix enzymes GNPAT (glycerone phosphate acyl transferase) and AGPS (alkyl-glycerone phosphate synthase) on the luminal side of the peroxisomal membrane.P. Brites, H.R. Waterham, R.J. Wanders, Functions and biosynthesis of plasmalogens in health and disease, Biochim. Biophys. Acta 1636 (2004) 219–231. These two enzymes can physically interact with each other to increase efficiency.

Modern technologies in genetic engineering and metabolic engineering enabled the production of these natural products in microorganisms. Complete biosynthesis of opiate compounds has been achieved in genetically tractable organisms Saccharomyces cerevisiae and Escherichia coli. Morphinone reductase was also successfully expressed in these two organisms. The enzyme represents a promising candidate for downstream modifications of opiate compounds, allowing the biosynthesis of valuable semi-synthetic opiate drugs in microorganisms.

The biosynthesis of azynomycin B includes a type 1 polyketide synthase and several nonribosomal peptide synthetases.Zhao, Qunfei, Qingli He, Wei Ding, Mancheng Tang, Qianjin Kang, Yi Yu, Wei Deng, Qi Zhang, Jie Fang, Gongli Tang, and Wen Liu. "Characterization of the Azinomycin B Biosynthetic Gene Cluster Revealing a Different Iterative Type I Polyketide Synthase for Naphthoate Biosynthesis." Chemistry & Biology 15.7 (2008): 693-705. Web.

The entire biosynthesis pathway of microcystin-LR in Microcystis aeruginosa is illustrated in the figure. The biosynthesis of microcystin-LR by Microcystis aeruginosa. The first steps of the synthesis involve the insertion of several carbon- and oxygen atoms between the acetyl- and phenylgroup. This part of the synthesis is catalyzed by enzyme domains that possess β-ketoacylsynthase, acyltransferase, C-methyltransferase and ketoacyl reductase activity.

The final step of L-carnitine biosynthesis is γ-butyrobetaine hydroxylase, a zinc binding enzyme.Vaz, F. M.; van Gool, S.; Ofman, R.; Ijlst, L.; Wanders, R. J. Carnitine Biosynthesis: Identification of the cDNA Encoding Human γ-Butyrobetaine Hydroxylase. Biochem. Biophys. Res. Commun. 1998, 250, 506–510.Rigault, C.; Le Borgne, F.; Demarquoy, J. Genomic structure, alternative maturation and tissue expression of the human BBOX1 gene. Biochim. Biophys.

Saccharopolyspora erythraea, formerly known as Streptomyces erythraeus, is a species of actinomycete bacteria within the genus Saccharopolyspora. Saccharopolyspora erythraea produces the macrolide antibiotic erythromycin. Cytochrome P450 eryF (CYP107A1) originally from the bacterium is responsible for the biosynthesis of the antibiotic by C6-hydroxylation of the macrolide 6-deoxyerythronolide B. Small non-coding RNAs have been suggested to be involved in regulation of the secondary metabolite biosynthesis.

Mutation experiments altering these enzymes independently stopped the pathway at abrine. This indicates that cooperation between EasE and EasC is necessary. Fig2- ergot alkaloid biosynthesis Fig3 - part 3 in biosynthesis of ergocryptine Chanocalvine-I is then oxidized to chanoclavine-I aldehyde with NAD+ dependent enzyme EasD (FgaDH in A. fumigatus). Chanoclavine-I aldehyde is a branch point, leading to different ergot alkaloids, depending on the specific fungus.

Evidence exists that a specific zeaxanthin-binding protein recruits circulating zeaxanthin and lutein for uptake within the macula. Due to the commercial value of carotenoids, their biosynthesis has been studied extensively in both natural products and non-natural (heterologous) systems such as the bacteria Escherichia coli and yeast Saccharomyces cerevisiae. Zeaxanthin biosynthesis proceeds from beta-carotene via the action of a single protein, known as a beta-carotene hydroxylase, that is able to add a hydroxyl group (-OH) to carbon 3 and 3′ of the beta-carotene molecule. Zeaxanthin biosynthesis therefore proceeds from beta-carotene to zeaxanthin (a di-hydroxylated product) via beta-cryptoxanthin (the mono hydroxylated intermediate).

Genes encoding coproporphyrinogen oxidase, an essential enzyme in the heme biosynthetic pathway were found as well as genes associated with the electron transport chain and oxidative phosphorylation. The citric acid cycle also has a role in its energy metabolism with 18% of metabolic genes relating to TCA cycle function. Saccharide metabolism associated genes were also found for the metabolism of: galactose, fructose, mannose, sucrose, starch, nucleotide sugars, amino sugars, as well as glycoprotein and peptide-protein biosynthesis. Many genes have been identified in this species that support protein biosynthesis and proteolytic systems including: glutamate, methionine and tryptophan metabolism; phenylalanine, valine, leucine and isoleucine degradation; valine, leucine, isoleucine, tyrosine and tryptophan biosynthesis.

A cautionary note on prediction of absolute stereochemistry based on liquid chromatographic elution order of diastereomeric derivatives.Journal of the American Chemical Society 101, 7432-7434 showed that the mevalonate and homomevalonate produced by these enzymes has the same 3S optical isomer configuration as the vertebrate enzymes showed that isopentenyl diphosphate, and its homolog, 3-ethyl-butenyl diphosphate (homoisopentenyl diphosphate) are metabolized to their corresponding allyic diphosphates, DMAPP and homoDMAPP (3-ethyl-3-methylallyl diphosphate). The latter is required for biosynthesis of JH I, JH II, and 4-methylJH I. 2 units of homoDMAPP are required for JH I and 4methyl JH I biosynthesis, and one for JH II biosynthesis.

However, most (80%) of the RNAs are in a position that may correspond to the 5′ UTR, so it is not inconceivable that the RNA has a role as a cis-regulatory element. Many lacto-2 RNAs are present in operons that encode tRNAs and rRNAs, and many are adjacent to genes encoding protein subunits of the ribosome, although they are not necessarily in the same operon as these protein-coding genes. Lacto-2 RNAs also have a weak association with genes involved in nucleotide biosynthesis and transport, including several independent genes within the de-novo purine biosynthesis pathway and some in pyrimidine biosynthesis.

It has been predicted that M. infernorum possess most of the key metabolic pathways for the biosynthesis of all amino acids, nucleotides and cofactors, with the sole exception of the cobalamin cofactor. Genetic studies have shown that the enzymes it uses in several metabolic pathways differs to the ones used by other methylotrophs like for example in the biosynthesis of aromatic amino acids, lipoic acid biosynthesis, urea cycle and in the number and diversity of transporters encoded. The bacteria is able to counteract extreme acidic environments thanks to the presence of various enzymes like glutamate decarboxylase, glutamate/γ-aminobutyrate antiporter, arginine decarboxylase and an arginine/agmatine antiporter.

Nickel insertion into a sirohydrochlorin also requires a chelatase as part of the biosynthesis of cofactor F430. Apparently that chelatase is identical to the cobalt chelatase.

An E2 reaction follows where deprotonation of a proton yields taraxasterol. The enzymes involved in this biosynthesis are oxidosesqualene: lupeopl cyclase and oxidosqualene: B-amyrin cyclase.

However, more than two decades latter it was finely unequivocally established that (S)-norcoclaurine was the central precursor for the biosynthesis of the structurally diverse BIAs.

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.

Duarte, A., Poderoso, C., Cooke, M., Soria, G., Cornejo Maciel, F., et al. (2012). Mitochondrial fusion is essential for steroid biosynthesis. PLoS ONE, 7(9): e45829.

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.

Other names in common use include isoflavone 2'-monooxygenase (ambiguous), and isoflavone 2'-hydroxylase (ambiguous). This enzyme participates in isoflavonoid biosynthesis. It employs one cofactor, heme.

Other names in common use include 5-O-(4-coumaroyl)-D-quinate/shikimate 3'-hydroxylase, and coumaroylquinate(coumaroylshikimate) 3'-monooxygenase. This enzyme participates in phenylpropanoid biosynthesis.

The genes of the S-motility system appear to be homologs of genes involved in the biosynthesis, assembly, and function of twitching motility in other bacteria.

This enzyme participates in selenoamino acid metabolism by recycling Se from selenocysteine during the degradation of selenoproteins, providing an alternate source of Se for selenocysteine biosynthesis.

The four compounds have been shown to be an effective antibiotics against methicillin-resistant strains of Staphylococcus aureus which act through the inhibition of protein biosynthesis.

Paul, H. S.; Sekas, G.; Adibi, S. A. Carnitine biosynthesis in hepatic peroxisomes. Demonstration of γ-butyrobetaine hydroxylase activity. Eur. J. Chem. 1992, 203, 599–605.

"Cytochrome P450 3A enzymes catalyze the O6-demethylation of thebaine, a key step in endogenous mammalian morphine biosynthesis." Journal of Biological Chemistry 290.33 (2015): 20200-20210.

In enzymology, an alpha-N-acetylneuraminate alpha-2,8-sialyltransferase () is an enzyme that catalyzes the chemical reaction :CMP-N-acetylneuraminate + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-R \rightleftharpoons CMP + alpha-N-acetylneuraminyl-2,8-alpha-N-acetylneuraminyl-2,3-beta-D- galactosyl-R Thus, the two substrates of this enzyme are CMP-N-acetylneuraminate and alpha- N-acetylneuraminyl-2,3-beta-D-galactosyl-R, whereas its 3 products are CMP, alpha-N-acetylneuraminyl-2,8-alpha-N-acetylneuraminyl-2,3-beta-D-, and galactosyl-R. This enzyme participates in 4 metabolic pathways: glycosphingolipid biosynthesis - neo-lactoseries, glycosphingolipid biosynthesis - globoseries, glycosphingolipid biosynthesis - ganglioseries, and glycan structures - biosynthesis 2. This enzyme belongs to the family of transferases, specifically those glycosyltransferases that do not transfer hexosyl or pentosyl groups. The systematic name of this enzyme class is CMP-N- acetylneuraminate:alpha-N-acetylneuraminyl-2,3-beta-D-galactos ide alpha-2,8-N-acetylneuraminyltransferase.

The antiandrogenic potency of prorenone in vivo in animals is close to that of spironolactone. Similarly to spironolactone, prorenone is also a potent inhibitor of aldosterone biosynthesis.

Plant based oils are transferred to Danimer Scientific’s proprietary bio-reactors. There, the oil is fed to naturally regenerating, soil borne bacteria who produce PHA through biosynthesis.

Sinapaldehyde is an organic compound that is an intermediate in the formation of lignin.Wout Boerjan, John Ralph, Marie Baucher "Lignin Biosynthesis" Annu. Rev. Plant Biol. 2003, vol.

Uroporphyrinogen III is a tetrapyrrole, the first macrocyclic intermediate in the biosynthesis of heme, chlorophyll, vitamin B12, and siroheme. It is a colorless compound, like other porphyrinogens.

8.1) via the Kennedy pathway.KENNEDY EP, WEISS SB. The function of cytidine coenzymes in the biosynthesis of phospholipides. J Biol Chem. 1956 Sep;222(1):193-214. .

DHICA (5,6- _d_ i _h_ ydroxy _i_ ndole-2- _c_ arboxylic _a_ cid) is an intermediate in the biosynthesis of melanin. It may tautomerise to form Dopachrome.

The enzyme anthocyanin 3-O-glucoside 6-O-hydroxycinnamoyltransferase produces delphinidin 3-(6-p-coumaroyl)glucoside from myrtillin and p-coumaroyl-CoA in the anthocyanin biosynthesis pathway.

Other names in common use include flavonoid 3'-hydroxylase, flavonoid 3-hydroxylase (erroneous), NADPH:flavonoid-3'-hydroxylase, and flavonoid 3-monooxygenase (erroneous). This enzyme participates in flavonoid biosynthesis.

Other names in common use include oxygenase, gibberellin A44 oxidase, and (gibberellin-44), 2-oxoglutarate:oxygen oxidoreductase. This enzyme participates in diterpenoid biosynthesis. It employs one cofactor, iron.

Other names in common use include cholesterol 7alpha-hydroxylase, and CYP7A1. This enzyme participates in bile acid biosynthesis and ppar signaling pathway. It employs one cofactor, heme.

Other names in common use include deacetylcephalosporin C synthase, 3'-methylcephem hydroxylase, DACS, DAOC hydroxylase, and deacetoxycephalosporin C hydroxylase. This enzyme participates in penicillin and cephalosporin biosynthesis.

However, propionyl-CoA instead of acetyl-CoA is used as the primer for the biosynthesis of long-chain fatty acids with an odd number of carbon atoms.

At the molecular level, climacteric fruit ripening is controlled through a multilayered regulatory cascade that involves the interaction of several positive and negative regulators of ethylene biosynthesis.

Other names in common use include 3,9-dihydroxypterocarpan 6a-hydroxylase, and 3,9-dihydroxypterocarpan 6alpha-monooxygenase (erroneous). This enzyme participates in isoflavonoid biosynthesis. It employs one cofactor, heme.

High concentrations of isoleucine also result in the downregulation of aspartate's conversion into the aspartyl-phosphate intermediate, hence halting further biosynthesis of lysine, methionine, threonine, and isoleucine.

Metyrapone blocks cortisol biosynthesis by acting as a reversible inhibitor of 11β-hydroxylase. This stimulates adrenocorticotropic hormone (ACTH) secretion, which in turn increases plasma 11-deoxycortisol levels.

In addition, its role in drug-induced malformations is known: inhibitors of the last step of cholesterol biosynthesis such as AY9944 and BM15766 severely impair brain development.

Bai, T., et al., Operon for biosynthesis of lipstatin, the beta-lactone inhibitor of human pancreatic lipase. Applied and Environmental Microbiology, 2014. 80(24): p. 7473-7483.

Chlorophyllide a and Chlorophyllide b are the biosynthetic precursors of chlorophyll a and chlorophyll b respectively. Their propionic acid groups are converted to phytyl esters by the enzyme chlorophyll synthase in the final step of the pathway. Thus the main interest in these chemical compounds has been in the study of chlorophyll biosynthesis in plants, algae and cyanobacteria. Chlorophyllide a is also an intermediate in the biosynthesis of bacteriochlorophylls.

Fulcher CA, "MetaCyc Chimeric Pathway: superpathway of sialic acid and CMP-sialic acid biosynthesis", "MetaCyc, March 2009" In bacterial systems, sialic acids are biosynthesized by an aldolase enzyme. The enzyme uses a mannose derivative as a substrate, inserting three carbons from pyruvate into the resulting sialic acid structure. These enzymes can be used for chemoenzymatic synthesis of sialic acid derivatives. Biosynthesis of sialic acid by a bacterial aldolase enzyme.

Galactocerebrosides are abundant sphingolipids of the myelin membrane of the central nervous system and peripheral nervous system and are also present in small amounts in kidney. The key enzymatic step in the biosynthesis of galactocerebrosides consists of the transfer of galactose to ceramide catalyzed by UDP-galactose ceramide galactosyltransferase (CGT, EC 2.4.1.45). The enzyme encoded by the CGT gene is the first involved in complex lipid biosynthesis in the myelinating oligodendrocyte.

In Senecio species, biosynthesis of senecionine starts from L-arginine or L-ornithine. Because plants don't have decarboxylase enzyme for L-ornithine, it must be first converted into L-arginine. Arginine can then be readily converted to putrescine and spermidine. Next, in an NAD+-dependent reaction catalyzed by homospermidine synthase (HSS), an aminopropyl group from putrescine is transferred to spermidine to form homospermidine, releasing 1,3-diaminopropane (see biosynthesis scheme).

Schematic representation of a metabolic branch point. The numbers represent chemical compounds, whereas the letters represent enzymes that catalyze the conversion indicated by the nearby arrow. In this scheme, enzyme c catalyzes the committed step in the biosynthesis of compound 6. In enzymology, the committed step (also known as the first committed step) is an effectively irreversible enzymatic reaction that occurs at a branch point during the biosynthesis of some molecules.

Regulation of Biosynthesis Some gliotoxin molecules are not secreted by GliA and remain in the cell. This intracellular gliotoxin activates the transcription factor GliZ, facilitating gli gene cluster expression, and an enzyme called GtmA. GtmA acts as a negative regulator for gliotoxin biosynthesis by adding methyl groups to the two sulfur residues on the dithiol gliotoxin intermediate. These additions prevent the formation of the disulfide bridge by GliT, inhibiting gliotoxin formation.

This is not just because of the philosophical problem of giving some account of what "laws of nature," which CL models encounter, but also the incontrovertible fact that most biological phenomena are not characterizable in nomological terms (i.e., in terms of lawful relationships). For example, protein biosynthesis does not occur according to any law, and therefore, on the DN model, no explanation for the biosynthesis phenomenon could be given.

At this stage, phosphoenolpyruvate and erythrose-4-phosphate react to form 3-deoxy-D-arabinoheptulosonate-7-phosphate (DAHP), in a reaction catalyzed by the enzyme DAHP synthase. :Biosynthesis of DAHP from phosphoenolpyruvate and erythrose-4-phosphate It also used in 3-hydroxy-1-aminoacetone phosphate biosynthesis, which is a precursor of vitamin B6 in DXP-dependent pathway. Erythrose-4-phosphate dehydrogenase is used to produce erythronate-4-phosphate.

The other pathway of glycine biosynthesis is known as the glycolytic pathway. This pathway converts serine synthesized from the intermediates of glycolysis to glycine. In the glycolytic pathway, the enzyme serine hydroxymethyltransferase catalyzes the cleavage of serine to yield glycine and transfers the cleaved carbon group of serine onto tetrahydrofolate, forming 5,10-methylene-tetrahydrofolate. Cysteine biosynthesis is a two-step reaction that involves the incorporation of inorganic sulfur.

It retains 54 genes for biosynthesis of crucial amino acids, but no longer has pathways for those amino acids that the host can synthesize. Pathways for nucleotide biosynthesis are gone from many reduced genomes. Those anabolic pathways that evolved through niche adaptation remain in particular genomes. The hypothesis that unused genes are eventually removed does not explain why many of the removed genes would indeed remain helpful in obligate pathogens.

It is thought that the biosynthesis of calotropin is similar to that of digitoxin, another cardenolide. Digitoxin is more established as a medicine for cardiac insufficiency, and therefore the biosynthesis has been further studied. However, it is believed that many cardenolides are synthesized in plants by a similar process, but this process is not yet well understood. The sterol precursor for this process is similar to precursors for steroidal alkaloids.

Structures of the three commonly occurring monolignols Monolignols are phytochemicals acting as source materials for biosynthesis of both lignans and lignin. The starting material for production of monolignols is the amino acid phenylalanine. The first reactions in the biosynthesis are shared with the phenylpropanoid pathway, and monolignols are considered to be a part of this group of compounds. Three monolignols predominate: coniferyl alcohol, sinapyl alcohol, and paracoumaryl alcohol.

Proposed spectinomycin biosynthesis Biosynthesis of spectinomycin begins similar to all aminoglycosides, with the formation of an inositol ring. The difference is the initial modification that forms the inositol ring of spectinomycin. The process begins with a glucose-6-phosphate (1a), which is reduced by NADH to form a ketone at C2 (2a). This ketone is then formed into a primary amine group through PLP and glutamine transamination (3a).

This gene is oriented telomere to centromere in close proximity to the ribosomal protein S18 gene. The functionality of the encoded protein is limited to ganglioseries glycolipid biosynthesis.

Hydrops-ectopic calcification-moth-eaten skeletal dysplasia is a defect in cholesterol biosynthesis. Greenberg characterized the condition in 1988. It has been associated with the lamin B receptor.

Other names in common use include caffeoyl coenzyme A methyltransferase, caffeoyl-CoA 3-O-methyltransferase, and trans-caffeoyl-CoA 3-O-methyltransferase. This enzyme participates in phenylpropanoid biosynthesis.

It is also shown to have greater enzyme efficiency than OPR1 and OPR2 in Arabidopsis thaliana, showing it is the significant enzyme in the jasmonic acid biosynthesis pathway.

One pathway for butyrate biosynthesis. Relevant enzymes: acetoacetyl-CoA thiolase, NAD- and NADP-dependent 3-hydroxybutyryl-CoA dehydrogenase, 3-hydroxybutyryl-CoA dehydratase, and NAD-dependent butyryl-CoA dehydrogenase.

SpoT works in conjunction with NDPK and both serve as essential enzymes in the (p)ppGpp biosynthesis cycle. NDPK synthesizes the formation of GDP from GTP via dephosphorylation.

Myclobutanil is a triazole chemical used as a fungicide. It is a steroid demethylation inhibitor, specifically inhibiting ergosterol biosynthesis. Ergosterol is a critical component of fungal cell membranes.

However, in mammalian non-hepatic tissues, the main use of the urea cycle is in arginine biosynthesis, so, as an intermediate in metabolic processes, ornithine is quite important.

SF-1 levels is strongly expressed at the onset of follicular development in theca and granulosa cells which precedes expression of the aromatase enzyme responsible for estrogen biosynthesis.

This reduction does not necessarily occur at step (4), but may occur further downstream. With the carboxyl and hydroxyl group in position, the guaiano-lactone [C] formation via dehydration (7) can occur, as proposed for a general guaianolide pathway. Formation of the Absinthin sesquiterpene guaianolide monomer [D] from hydroxylation and double bond rearrangement (8,9) is then postulated to directly precede dimerization to Absinthin [E] via a naturally occurring Diels-Alder reaction [10], which is likely facilitated by the associated synthase even though the reaction itself can occur in good yields spontaneously, albeit slower than typical natural product biosynthesis. Illustration of the proposed biosynthesis of Absinthin as interpreted from similar Guaianolide pathways in Artemisia While no synthases specific to Artemisia absinthium have been sufficiently isolated to recreate this particular sesquiterpene formation in vitro, the general reaction scheme presented here portrays a likely scenario for Absinthin biosynthesis through the use of terpene intermediates utilized in the biosynthesis of Germacrene A, another sesquiterpene lactone.

The human purinosome was thought to have been identified in 2008 by the observation that transiently expressed GFP fusion constructs of purine biosynthesis proteins form macrobodies. A folate enzyme not directly involved in the purine biosynthesis pathway, 5,10-methenyltetrahydrofolate synthase (MTHFS), was later found to be part of purinosome macrobodies by the same approach. The biological relevance of this folate enzyme's inclusion to the purinosome macrobody is unclear: while it provides substrate for a trifunctional folate enzyme C1THF synthase to generate a key cofactor for purine biosynthesis, C1THF synthase is not a part of purinosome macrobodies. Curiously, hypoxanthine levels do not alter purinosome macrobodies, but adenosine or guanosine addition suppresses formation of macromolecular bodies formed by the folate enzyme.

WRKY transcription factors also play a role in regulating pathways for the biosynthesis of pharmaceutically valuable plant-specialized metabolites.Suttipanta, Pattanaik, Kulshrestha, Patra, Singh, et al. (2011) The Transcription Factor CrWRKY1 Positively Regulates the Terpenoid Indole Alkaloid Biosynthesis in Catharanthus roseus. Plant Physiology. 157(4). 2081-2093, Li, Zhang, Zhang, Fu and Yu (2013) Functional analysis of a WRKY transcription factor involved in transcriptional activation of the DBAT gene in Taxus chinensis. Plant Biology. 15(1). 19-26, Ma, Pu, Lei, Ma, Wang, et al. (2009) Isolation and Characterization of AaWRKY1, an Artemisia annua Transcription Factor that Regulates the Amorpha-4,11-diene Synthase Gene, a Key Gene of Artemisinin Biosynthesis. Plant and Cell Physiology. 50(12).

The formation of thienamycin is thought to occur through a different pathway from classic β-lactams (penicillins, cephalosporins). Production of classic β-lactams in both fungi and bacteria occur through two steps: First, the condensation of -cysteine, -valine, and -α-aminoadipic acid by ACV synthetase (ACVS, a nonribosomal peptide synthetase) and then cyclization of this formed tripeptide by isopenicillin N synthetase (IPNS). The gene cluster (thn) for the biosynthesis of thienamycin of S. cattleya was identified and sequenced in 2003, lending insight into the biosynthetic mechanism for thienamycin formation. The biosynthesis is thought to share features with the biosynthesis of the simple carbapenems, beginning with the condensation of malonyl-CoA with glutamate-5-semialdehyde to form the pyrroline ring.

The classical mevalonate pathway or HMG-CoA reductase pathway is a metabolic pathway from the biosynthesis of isoprenoid precursors present in most higher eukaryotes and some bacteria. It is important for the production of IPP and DMAPP, which serve as the basis for the biosynthesis of isoprenoid (terpenoid) molecules used in processes as diverse as protein prenylation, cell membrane maintenance, the synthesis of hormones, protein anchoring and N-glycosylation. Bacteria, plants, and apicomplexan protozoa—such as malaria parasites—are able to produce isoprenoid precursors using an alternative pathway, the MEP pathway, which is a non-mevalonate pathway. In the case of plants and certain protozoa, the biosynthesis of IPP/DMAPP takes place in plastid organelles.

In enzymology, a 3-galactosyl-N-acetylglucosaminide 4-alpha-L- fucosyltransferase () is an enzyme that catalyzes the chemical reaction :GDP- beta-L-fucose + beta-D-galactosyl-(1->3)-N-acetyl-D-glucosaminyl-R \rightleftharpoons GDP + beta-D-galactosyl-(1->3)-[alpha-L- fucosyl-(1->4)]-N-acetyl-beta-D- glucosaminyl-R Thus, the two substrates of this enzyme are GDP-beta-L-fucose and beta-D-galactosyl-(1->3)-N-acetyl-D- glucosaminyl-R, whereas its 3 products are GDP, beta-D- galactosyl-(1->3)-[alpha-L-fucosyl-(1->4)]-N-acetyl-beta-D-, and glucosaminyl-R. This enzyme participates in 3 metabolic pathways: glycosphingolipid biosynthesis - lactoseries, glycosphingolipid biosynthesis - neo-lactoseries, and glycan structures - biosynthesis 2.

Chlormequat has been called the "most important inhibitor of gibberellin biosynthesis." As such, it inhibits cell elongation, resulting in thicker stalks, which are sturdier, facilitating harvesting of cereal crops.

Salinispora is genus of bacteria which belong to family of Micromonosporaceae. They usually occur in marine sedimentsTaxonomy Browser and are the subject of intensive study into natural product biosynthesis.

Pyrimethanil is a broad spectrum fungicide often applied to seeds. It inhibits methionine biosynthesis, thus affecting protein formation and subsequent cell division. Pyrimethanil works best on young fungus infestations.

Although it is not clearly determined what role this switching of the cluster might play, it is postulated to be involved in a critical redox regulation of siroheme biosynthesis.

The genome of P. jirovecii has been sequenced from a bronchoalveolar lavage sample. The genome is small, low in G+C content, and lacks most amino-acid biosynthesis enzymes.

The methanearsonates are the precursors to dimethylarsonates, again by the cycle of reduction (to methylarsonous acid) followed by a second methylation. Related pathways apply to the biosynthesis of methylmercury.

Cell and whole plant physiology, specialising in chloroplasts and mitochondria, cell metabolism, especially energy metabolism, amino acid and vitamin biosynthesis. Biochemistry, molecular biology and structural biology. Botany and ornithology.

The reaction is part of the biosynthesis pathway of queuosine. The enzyme from Escherichia coli can also convert 6-pyruvoyl-5,6,7,8-tetrahydropterin and sepiapterin to 6-carboxy-5,6,7,8-tetrahydropterin.

This enzyme participates in folate biosynthesis and is a critical part of energy conservation in some methanogens such as Methanosarcina barkeri. It has 3 cofactors: iron, nickel, and deazaflavin.

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

Synthesis of nodularins is currently not well understood. The biosynthesis of nodularins is nonribosomal. Synthesis is conducted by multienzyme complexes, such as peptide synthetases, polypeptide synthases, and tailoring enzymes.

The enzyme’s genetic expression is regulated by sterol regulatory element binding protein (SREBP-2), a molecule which also regulates the expression of other enzymes in the cholesterol biosynthesis pathway.

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.

Mutations in the NSDHL gene are associated with CHILD syndrome which is a X-linked dominant disorder of lipid metabolism with disturbed cholesterol biosynthesis, and typically lethal in males.

Biosynthesis of atropine starting from L-Phenylalanine The biosynthesis of atropine starting from l-phenylalanine first undergoes a transamination forming phenylpyruvic acid which is then reduced to phenyl-lactic acid. Coenzyme A then couples phenyl-lactic acid with tropine forming littorine, which then undergoes a radical rearrangement initiated with a P450 enzyme forming hyoscyamine aldehyde. A dehydrogenase then reduces the aldehyde to a primary alcohol making (−)-hyoscyamine, which upon racemization forms atropine.

The chimeric proteins acquired an ability to catalyze an essential reaction in isoprenoid biosynthesis—one of the most diverse pathways of biosynthesis found in nature—that was absent in the parent proteins. Protein engineering through recombination has also produced chimeric enzymes with new function in members of a group of proteins known as the cytochrome P450 family, which in humans is involved in detoxifying foreign compounds like drugs, food additives and preservatives.

The biosynthesis of ginkgolide B While researchers have published chemical pathways to make this molecule, most of the designed syntheses were too complex and produced little of the actual material to run full analyses. Therefore, studying the biosynthesis of the molecule is preferable. Most of the natural product terpenoids start with isopentenyl diphosphate synthesized by the MEP pathway. This pathway also generates dimethylallyl diphosphate, from pyruvate and D-glyercaldehyde 3-phosphate (GAP).

In molecular biology, YgbB is a protein domain. This entry makes reference to a number of proteins from eukaryotes and prokaryotes which share this common N-terminal signature and appear to be involved in terpenoid biosynthesis. The YgbB protein is a putative enzyme thought to aid terpenoid and isoprenoid biosynthesis, a vital chemical in all living organisms. This protein domain is part of an enzyme which catalyses a reaction in a complex pathway.

The GDP-L-colitose biosynthesis pathway. For clarity, groups modified by the previous enzymatic step are highlighted in yellow. The biosynthesis of colitose begins with ColE, a mannose-1-phosphate guanylyltransferase that catalyzes the addition of a GMP moiety to mannose, yielding GDP-mannose. In the next step, ColB, an NADP- dependent short-chain dehydrogenase-reductase enzyme, catalyzes the oxidation at C-4 and the removal of the hydroxyl group at C-6.

Lipid II was estimated to exist at a concentration of less than 2000 molecules per bacterial cell. Lipid II biosynthesis is functional and essential even in organisms without a cell wall like Chlamydia and Wolbachia. It has been hypothesized that maintaining lipid II biosynthesis reflects its role in prokaryotic cell division. In the discovery and mechanism of assembly of pili in gram positive bacteria Lipid II has been implicated as a crucial structural molecule.

Biosynthesis of THCA In the Cannabis plant, THC occurs mainly as tetrahydrocannabinolic acid (THCA, 2-COOH-THC, THC-COOH). Geranyl pyrophosphate and olivetolic acid react, catalysed by an enzyme to produce cannabigerolic acid, which is cyclized by the enzyme THC acid synthase to give THCA. Over time, or when heated, THCA is decarboxylated, producing THC. The pathway for THCA biosynthesis is similar to that which produces the bitter acid humulone in hops.

The name "mycofactocin" is derived from three words, the genus name "Mycobacterium" (across which it is nearly universal), "cofactor" because its presence in a genome predicts the co- occurrence of certain families of enzymes as if it is a cofactor they require, and "bacteriocin" because a radical SAM enzyme critical to its biosynthesis, MftC, is closely related to the key enzyme for the biosynthesis of subtilosin A, a bacteriocin, from its precursor peptide.

The purine biosynthesis enzymes can be co-purified under certain conditions. A complex of two particular pathway enzymes GART and ATIC can be isolated with cofactor production enzyme C1THF synthase and SHMT1. Kinetic studies show evidence of substrate channeling between PPAT and GART, but evidence could not be obtained for their physical protein-protein interaction. Thus far, isolation of a multienzyme complex inclusive of all purine biosynthesis enzymes has not been achieved.

In the main porphyrin biosynthesis pathway, coproporphyrinogen III is derived from uroporphyrinogen III by the action of the enzyme uroporphyrinogen III decarboxylase: alt=Biosynthesis of coproporphyrinogen-III from uroporphyrinogen-III The conversion entails four decarboxylations, which turn the four acetic acid groups into methyl groups , with release of four carbon dioxide molecules. Coproporphyrinogen III is further used as a substrate for the enzyme coproporphyrinogen III oxidase which oxidizes and further decarboxylates it to protoporphyrinogen IX.

FAAH knockout mice also show dramatic increases in tissue and blood NATs. The enzymatic biosynthesis of NATs remains unknown. A distinct circulating enzyme, peptidase M20 domain containing 1 (PM20D1), can catalyze the bidirectional the condensation and hydrolysis of a variety of N-acyl amino acids in vitro. In vivo, PM20D1 overexpression increases the levels of various N-acyl amino acids in blood, demonstrating that this enzyme can contribute to N-acyl amino acid biosynthesis.

The A. pisum genome on the other hand, contains 66 amino acid biosynthesis genes and 93 amino acid degradation genes. Both A. pisum and Buchnera contribute to the metabolic pathways of amino acid biosynthesis. This metabolic complementarity is illustrated by the use of asparagine, a nonessential amino acid in phloem sap, as a major precursor in the production essential and nonessential amino acids necessary for the growth and survival of A. pisum and Buchnera.

SAM-e was first discovered by Giulio Cantoni in 1952. In bacteria, SAM-e is bound by the SAM riboswitch, which regulates genes involved in methionine or cysteine biosynthesis. In eukaryotic cells, SAM-e serves as a regulator of a variety of processes including DNA, tRNA, and rRNA methylation; immune response; amino acid metabolism; transsulfuration; and more. In plants, SAM-e is crucial to the biosynthesis of ethylene, an important plant hormone and signaling molecule.

Biosynthetic pathway for N,N-dimethyltryptamine Dimethyltryptamine is an indole alkaloid derived from the shikimate pathway. Its biosynthesis is relatively simple and summarized in the adjacent picture. In plants, the parent amino acid L-tryptophan is produced endogenously where in animals L-tryptophan is an essential amino acid coming from diet. No matter the source of L-tryptophan, the biosynthesis begins with its decarboxylation by an aromatic amino acid decarboxylase (AADC) enzyme (step 1).

Biosynthesis: The enzyme 3-dehydroquinate dehydratase uses 3-dehydroquinate to produce 3-dehydroshikimate and H2O. 3-Dehydroshikimate is then reduced to shikimic acid by the enzyme shikimate dehydrogenase, which uses nicotinamide adenine dinucleotide phosphate (NADPH) as a cofactor. :Biosynthesis of shikimic acid from 3-dehydroquinate Gallic acid is also formed from 3-dehydroshikimate by the action of the enzyme shikimate dehydrogenase to produce 3,5-didehydroshikimate. This latter compound spontaneously rearranges to gallic acid.

This enzyme participates in 8 metabolic pathways: alanine and aspartate metabolism, methionine metabolism, valine, leucine and isoleucine degradation, tyrosine metabolism, phenylalanine metabolism, tryptophan metabolism, phenylalanine, tyrosine and tryptophan biosynthesis, and alkaloid biosynthesis. It employs one cofactor, flavin adenine dinucleotide (FAD). The enzyme binds to FAD in the first step of the catalytic process, thereby reducing FAD to FADH2. The FAD is regenerated from FADH2 by oxidation as a result of O2 being reduced to H2O2.

In plants and microorganisms, threonine is synthesized from aspartic acid via α-aspartyl-semialdehyde and homoserine. Homoserine undergoes O-phosphorylation; this phosphate ester undergoes hydrolysis concomitant with relocation of the OH group. Enzymes involved in a typical biosynthesis of threonine include aspartokinase, β-aspartate semialdehyde dehydrogenase, homoserine dehydrogenase, homoserine kinase, threonine synthase. The biosynthesis of threonine is regulated via allosteric regulation of its precursor, homoserine, by structurally altering the enzyme homoserine dehydrogenase.

Quinine biosynthesis In the first step of quinine biosynthesis, the enzyme strictosidine synthase catalyzes a stereoselective Pictet–Spengler reaction between tryptamine and secologanin to yield strictosidine. Suitable modification of strictosidine leads to an aldehyde. Hydrolysis and decarboxylation would initially remove one carbon from the iridoid portion and produce corynantheal. Then the tryptamine side- chain were cleaved adjacent to the nitrogen, and this nitrogen was then bonded to the acetaldehyde function to yield cinchonaminal.

Biosynthesis of oxylipins is initiated by dioxygenases or monooxygenases; however also non-enzymatic autoxidative processes contribute to oxylipin formation (phytoprostanes, isoprostanes). Dioxygenases include lipoxygenases (plants, animals, fungi), heme-dependent fatty acid oxygenases (plants, fungi), and cyclooxygenases (animals). Fatty acid hydroperoxides or endoperoxides are formed by action of these enzymes. Monooxygenases involved in oxylipin biosynthesis are members of the cytochrome P450 superfamily and can oxidize double bonds with epoxide formation or saturated carbons forming alcohols.

Biosynthesis of linear polyketide precursor. The AbyB1, AbyB2, and AbyB3 genes code for the seven- module polyketide synthase complex that assembled the polyketide backbone. Next, the linear polyketide precursor fused with glyceryl-ACP to form intermediate 2. Based on the observation made for the biosynthesis of agglomerin, it has been proposed that AbyA4 acetylates intermediate 2 and AbyA5 catalyzes the elimination of acetic acid to form the exocyclic double bond in intermediate 4.

"Beta-Carbolines: Occurrence, Biosynthesis, and Biodegredation." By Hans Rommelspacher. The coincident occurrence of β-carboline alkaloids and serotonin in P. harmala indicates the presence of two very similar, interrelated biosynthetic pathways, which makes it difficult to definitively identify whether free tryptamine or L-tryptophan is the precursor in the biosynthesis of harmine. However, it is postulated that L-tryptophan is the most likely precursor, with tryptamine existing as an intermediate in the pathway.

The cyclization of FPP to yield the (+)-costunolide precursor, Germacrene A. Following the formation of the 10-member ring system of (+)-germacrene A, two subsequent oxidation steps formed germacrene acid. Germacrene acid could then be hydoxylated and undergo lactonization to form (+)-costunolide, a branching point for the biosynthesis of sesquiterpene lactones. (Fig. 2) From here, the biosynthesis of guaianolides can follow two proposed pathways. In the first pathway, (+)-costunolide undergoes enzymatic epoxidation forming parthenolide.

Salutaridinol is a product of the enzyme salutaridine: NADPH 7-oxidoreductase and the substrate for the enzyme salutaridinol 7-O-acetyltransferase, which are two of the four enzymes in the morphine biosynthesis pathway that generates morphine from (R)-reticuline.Lenz, Rainer, and Meinhart H. Zenk. "Acetyl coenzyme A: salutaridinol-7-O-acetyltransferase from Papaver somniferum plant cell cultures: The enzyme catalyzing the formation of thebaine in morphine biosynthesis." Journal of Biological Chemistry 270.52 (1995): 31091-31096.

Dehydrodolichyl diphosphate (dedol-PP) synthase catalyzes cis-prenyl chain elongation to produce the polyprenyl backbone of dolichol, a glycosyl carrier lipid required for the biosynthesis of several classes of glycoproteins.

7,8-Dihydroneopterin triphosphate (DHNTP) is an intermediate in tetrahydrobiopterin biosynthesis. It is transformed by 6-pyruvoyltetrahydropterin synthase into 6-pyruvoyl-tetrahydropterin. It is also used in the Queuosine/Archeosine Pathway.

Other routes are from butadiene, allyl acetate and succinic acid. A biological route to BDO has been commercialized that uses a genetically modified organism. The biosynthesis proceeds via 4-hydroxybutyrate.

Uroporphyrinogen I is an isomer of uroporphyrinogen III, a metabolic intermediate in the biosynthesis of heme. A type of porphyria is caused by production of uroporphyrinogen I instead of III.

A biosynthesis of silver nanoparticles (NPs) mediated by fungal proteins of Coriolus versicolor has been undertaken for the first time last year.Verma, Preeti, and Rashmi Sanghi. "Bioresource Technology." Research GATE.N.p.

5-Hydroxytryptophan (5-HTP), also known as oxitriptan, is a naturally occurring amino acid and chemical precursor as well as a metabolic intermediate in the biosynthesis of the neurotransmitter serotonin.

So this enzyme plays an important role in the biosynthesis of estrogens. Testosterone is normally converted to estradiol, one of the main estrogens, through the action of the enzyme aromatase.

"Mechanism of biosynthesis of unsaturated fatty acids in Pseudomonas sp. strain E-3, a psychrotrophic bacterium." Journal of Bacteriology 171.8 (1989):4267-71.Subramanian, Chitra, Charles ORock, and Yong-MeiZhang.

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).

Other names in common use include hyoscyamine 6beta-hydroxylase, hyoscyamine 6beta- dioxygenase, and hyoscyamine 6-hydroxylase. This enzyme participates in alkaloid biosynthesis ii. It has 2 cofactors: iron, and Ascorbate.

Other names in common use include desacetoxyvindoline 4-hydroxylase, desacetyoxyvindoline-17-hydroxylase, D17H, desacetoxyvindoline,2-oxoglutarate:oxygen oxidoreductase, and (4beta- hydroxylating). This enzyme participates in terpene indole and ipecac alkaloid biosynthesis.

However, a role of PSMA5 was also indicated in neuroendocrine pulmonary tumors. The PSMA5 protein has further been associated with the biosynthesis of conjugated linoleic acid (CLA) in mammary tissue.

The main contributors to pathogenesis by the ShB pathogen, is from secreted hormones, Cytochrome P450s (a family of enzymes that is involved in the biosynthesis of plant hormones), and growth hormones.

Schwenk et al. (2016) Unexpected Metabolic Versatility in a Combined Fungal Fomannoxin/Vibralactone Biosynthesis. Journal of Natural Products. Additionally, a new prenylphenol, termed cloquetin, was identified from the fungus by NMR.

GDP-perosamine synthase is a PLP-dependent enzyme that transfers a nitrogen from glutamate to the 4-keto position of GDP-4-keto-6-deoxymannose during the biosynthesis of GDP-perosamine.

Early work by Mowshowitz focused on pure biochemistry, in areas such as enzyme assays and biosynthesis in yeast. She has also published in the Journal of Virology and in Analytical Biochemistry.

131-139 The enzyme leading to its formation is currently unknown. Tabersonine is the first intermediate leading to the formation of vindoline one of the two precursors required for vinblastine biosynthesis.

Other names in common use include gibberellin 3beta-hydroxylase, (gibberrellin-20),2-oxoglutarate: oxygen oxidoreductase, and (3beta- hydroxylating). This enzyme participates in diterpenoid biosynthesis. It has 2 cofactors: iron, and Ascorbate.

This enzyme is involved in the biosynthesis of pyrethrins, highly potent insecticides found in some flowers. The systematic name of this enzyme class is dimethylallyl- diphosphate:dimethylallyl-diphosphate dimethylallyltransferase (chrysanthemyl- diphosphate-forming).

Within the biosynthesis of M-cluster, radical SAM enzyme NifB has been recognized to catalyze a carbon insertion reaction, leading to formation of a Mo/homocitrate-free precursor of M-cluster.

Camalexin is a phytoalexin which is induced independently of RLM1-mediated resistance and mutants disrupted in camalexin biosynthesis show susceptibility to L. maculans, indicating that this is a critical resistance mechanism.

The biosynthesis of swainsonine has been investigated in the fungus Rhizoctonia leguminicola, and it initially involves the conversion of lysine into pipecolic acid. The pyrrolidine ring is then formed via retention of the carbon atom of the pipecolate's carboxyl group, as well as the coupling of two more carbon atoms from either acetate or malonate to form a pipecolylacetate. The retention of the carboxyl carbon is striking, since it is normally lost in the biosynthesis of most other alkaloids. Swainsonine biosynthesis scheme The resulting oxoindolizidine is then reduced to (1R,8aS)- 1-hydroxyindolizidine, which is subsequently hydroxylated at the C2 carbon atom to yield 1,2-dihydroxyindolizidine. Finally, an 8-hydroxyl group is introduced through epimerization at C-8a to yield swainsonine.

Biosynthesis of β-sitosterol (6) from cycloartenol (7) The regulation of the biosynthesis of both sterols and some specific lipids occurs during membrane biogenesis. Through 13C-labeling patterns, it has been determined that both the mevalonate and deoxyxylulose pathways are involved in the formation of β-sitosterol. The precise mechanism of β-sitosterol formation varies according to the organism, but is generally found to come from cycloartenol.Dewick, P. M. Medicinal Natural Products: A Biosynthetic Approach. 3 ed.

Dirigent proteins are members of a class of proteins which dictate the stereochemistry of a compound synthesized by other enzymes. The first dirigent protein was discovered in Forsythia intermedia. This protein has been found to direct the stereoselective biosynthesis of (+)-pinoresinol from coniferyl alcohol monomers: Reaction of monolignol radicals in the presence of dirigent protein to form (+)-pinoresinol Lignan biosynthesis is catalysed by oxidative enzymes. In the test tube the reaction results in a heteregenous mixture of dimeric compounds.

Females produce a sex pheromone in the pheromone gland on their abdominal tips that attracts males for mating. Biosynthesis of the sex pheromone is controlled by a neurohormone called pheromone biosynthesis activating neuropeptide (PBAN). This 33-amino- acid-long peptide is present in both sexes in the brain-suboesophageal ganglions (Br-SOG) during both scotophase and photophase. It has been shown that the juvenile hormone is involved in the release of PBAN in both males and females.

The unconditioned biosynthesis of lycopene in eukaryotic plants and in prokaryotic cyanobacteria is similar, as are the enzymes involved. Synthesis begins with mevalonic acid, which is converted into dimethylallyl pyrophosphate. This is then condensed with three molecules of isopentenyl pyrophosphate (an isomer of dimethylallyl pyrophosphate), to give the 20-carbon geranylgeranyl pyrophosphate. Two molecules of this product are then condensed in a tail-to-tail configuration to give the 40-carbon phytoene, the first committed step in carotenoid biosynthesis.

The trimethyllysine dioxygenase enzyme catalyzes the first step in the carnitine biosynthesis pathway, which is part of amine biosynthesis. Carnitine is a molecule that play an essential role in the transport of activated fatty acids across the inner mitochondrial membrane where they are metabolized. The encoded protein converts trimethyllysine into hydroxytrimethyllysine with the reaction (EC 1.14.11.8): N6,N6,N(6)-trimethyl-L-lysine + 2-oxoglutarate + O2 = 3-hydroxy-N6,N6,N(6)-trimethyl-L-lysine + succinate + CO2.

Cofitness data is data representing the similarity of growth fitness under various conditions between any two different deletion strains. Under the assumption that strains lacking the diphthamide synthetase gene should have high cofitness with strain lacking other diphthamide biosynthesis genes, they identified ylr143w as the strain with the highest cofitness to the all other strains lacking known diphthamide biosynthesis genes. Subsequent experimental assays confirmed that YLR143W was required for diphthamide synthesis and was the missing diphthamide synthetase.

Although it is known that the biosynthesis of polyamines is highly regulated, the biological function of polyamines is only partly elucidated. In their cationic ammonium form, they bind to DNA, and, in structure, they represent compounds with cations that are found at regularly spaced intervals (in contrast to or , which are point charges). They have also been found to act as promoters of programmed ribosomal frameshifting during translation. Inhibition of polyamine biosynthesis, retards or stops cell growth.

Spheroidene monooxygenase (, CrtA, acyclic carotenoid 2-ketolase, spirilloxantin monooxygenase, 2-oxo-spirilloxanthin monooxygenase) is an enzyme with systematic name spheroidene,reduced-ferredoxin:oxygen oxidoreductase (spheroiden-2-one-forming). This enzyme catalyses the following chemical reaction : spheroidene + reduced ferredoxin + O2 \rightleftharpoons spheroiden-2-one + oxidized ferredoxin + H2O : spirilloxantin + reduced ferredoxin + O2 \rightleftharpoons 2-oxospirilloxanthin + oxidized ferredoxin + H2O : 2'-oxospirilloxanthin + reduced ferredoxin + O2 \rightleftharpoons 2,2'-dioxospirilloxanthin + oxidized ferredoxin + H2O The enzyme is involved in spheroidenone biosynthesis and in 2,2'-dioxospirilloxanthin biosynthesis.

The biosynthesis of cyclopamine begins with cholesterol. A steroid skeleton has a classic 6-member ring, adjacent to another 6, 6, then a five or “6-6-6-5”. Veratrum was determined to contain five types of alkaloids, each of which had a common cholesterol precursor: (1) solanidine alkaloids, (2) verazine alkaloids, (3) vertramine alkaloids, (4) jervine alkaloids, and (5) the cevanine alkaloids. In biosynthesis, Cyclopamine has a solanide (1) precursor, which itself is made from cholesterol.

This addition is not predicted in the current biosynthesis, although the absence of this post-NRPS modification would produce the analogue previously mentioned, deacetylhectochlorin. Figure1. A) Predicted biosynthesis of hectochlorin. B) P450 oxidation of side chain. C)Formation of thiazole ring Currently in the MarinLit database, other compounds (besides deacetylhectochlorin and hectochlorin) that contain this fairly unusual gem-dichloro group are lyngbyabellin A-N, 27-deoxylyngbyabellin A and dolabellin, all of those synthesized from Moorea species.

The biosynthesis of coniine is still being investigated, much of the pathway has been elucidated. Originally thought to use 4 acetyl groups as feed compounds for the polyketide synthase that forms coniine,Leete E (1964) Biosynthesis of the hemlock alkaloids. The incorporation of acetate-1-C14 into coniine and conhydrine. J Am Chem Soc 86, 2509–2513 it is in fact derived from two malonyl and a butyryl CoA, which are derived in the usual way from acetyl-CoA.

Lineatin is a monoterprene with unique tricyclic acetal structure. Most of the studies regarding lineatin were focused on the total synthesis; little attentions were put on its biosynthesis. It is suggested that lineatin is derived through oxidation and cyclization of a monoterponid precursor, but no experimental has been done on proving this route. Based on its partial structure similarity to iridoid class of terprenoids, here, a possible biosynthesis pathway was proposed and outlined in figure 2.

"The biosynthesis of C5-C25 terpenoid compounds". Nat. Prod. Rep. 16', 97-130 Crystal structures of recombinant tobacco 5-epi-aristolochene synthase (TEAS), alone and also complexed with two FPP analogues have been reported and analyzed to suggest the following mechanism of biosynthesis.Starks C.M.; Back K.; Chappell J.; Noel J.P.; (1997) Structural Basis for Cyclic Terpene Biosynthesis by Tobacco 5-Epi- Aristolochene Synthase. Science 277, 1815-1820 The E,E-farnesyl cation undergoes cyclization to form the germacryl cation.

349, 365 center Biosynthesis of ergot alkaloids begins with the alkylation of tryptophan by dimethylallyl pyrophosphate (DMAPP), where the carbon atom C(4) in the indole nucleus plays the role of the nucleophile. The resulting 4-dimethylallyl-L-tryptophan undergoes N-methylation. Further products of biosynthesis are chanoclavine-I and agroclavine – the latter is hydroxylated to elymoclavine, which in turn oxidizes into paspalic acid. In the process of allyl rearrangement, paspalic acid is converted to lysergic acid.

The enzymes are organized in modules that are responsible for the introduction of one additional amino acid. Each module consists of several domains with defined functions, separated by short spacer regions of about 15 amino acids. The biosynthesis of nonribosomal peptides shares characteristics with the polyketide and fatty acid biosynthesis. Due to these structural and mechanistic similarities, some nonribosomal peptide synthetases contain polyketide synthase modules for the insertion of acetate or propionate-derived subunits into the peptide chain.

In contrast to the huge amount of information available on the chemical composition of mango flavor, the biosynthesis of these chemicals has not been studied in depth; only a handful of genes encoding the enzymes of flavor biosynthetic pathways have been characterized to date.Kulkarni RS, Chidley HG, Deshpande A, Schmidt A, Pujari KH, Giri AP and Gershenzon J, Gupta VS, 2013, An oxidoreductase from ‘Alphonso’ mango catalyzing biosynthesis of furaneol and reduction of reactive carbonyls, SpringerPlus, 2, 494.

The biosynthesis of colistin requires the use of three amino acids threonine, leucine, and 2,4-diaminobutryic acid. It is important to synthesis the linear form of colistin before cycliziation. Elongation of non ribosomal peptide biosynthesis begins by a loading module and then the addition of each subsequent amino acid. The subsequent amino acids are added with the help of an adenylation domain (A), a peptidyl carrier protein domain (PCP), an epimerization domain (E), and a condensation domain (C).

Isolation from Streptomyces platensis, PLM is produces. Genes PnT1 and PnT2 regulate the post-synthesis of PLM to form PLM B by the phosphorylation and added the amine group . Figure 4 is based on the biosynthesis analysis on the Gene journal introduced that PLM B is used to produce PLM A, and 4 more PLMs C-F. The PLM A-F are the post synthesis product of the biosynthesis of PLM with the modification of many enzyme PnT1-T8.

Sucrose-phosphate synthase is a plant enzyme involved in sucrose biosynthesis. Specifically, this enzyme catalyzes the transfer of a hexosyl group from uridine diphosphate glucose (UDP-glucose) to D-fructose 6-phosphate to form UDP and D-sucrose-6-phosphate. This reversible step acts as the key regulatory control point in sucrose biosynthesis, and is an excellent example of various key enzyme regulation strategies such as allosteric control and reversible phosphorylation. This enzyme participates in starch and sucrose metabolism.

In E. coli, MviN is an essential protein which when defective results in the accumulation of polyprenyl diphosphate-N-acetylmuramic acid-(pentapeptide)-N-acetyl-glucosamine, thought to be the peptidoglycan intermediated exported via MviN. In Mycobacterium tuberculosis, MviN is thought to play an essential role in peptidoglycan biosynthesis. Another MVF protein, MurJ, functions as a peptidoglycan biosynthesis protein. A 3-d structureal model shows that MurJ contains a solvent-exposed cavity within the plane of the membrane.

In molecular biology, the iron-sulfur cluster biosynthesis protein family of includes proteins involved in biogenesis of Fe-S clusters (iron-sulfur cluster insertion protein, Fe/S biogenesis protein). This family includes IscA, HesB, YadR and YfhF-like proteins. The hesB gene is expressed only under nitrogen fixation conditions, within nitrogen fixing cyanobacteria. IscA, an 11 kDa member of the hesB family of proteins, binds iron and [2Fe-2S] clusters, and participates in the biosynthesis of iron-sulfur proteins.

There are numerous branches of body psychotherapy, often tracing their origins to particular individuals: for example, 'Bioenergetic analysis' to the work of Lowen and Pierrakos; 'Radix' to the work of Chuck Kelley; Organismic Psychotherapy to the work of Malcolm and Katherine Brown; 'Biosynthesis' to the work of David Boadella;Boadella. D. (1987) Lifestreams: An introduction to Biosynthesis. Routledge & Kegan Paul. 'Biodynamic Psychology' to that of Gerda Boyesen; 'Rubenfeld Synergy' to Ilana Rubenfeld's work;Steckler, L. H. (2006).

Plants and algae produce furan fatty acids during the biosynthesis from polyunsaturated fatty acids (PUFA). These are seemingly used in these organisms as protection against free radicals generated by sunlight.G. G. Habermehl u. a. Naturstoffchemie Verlag Springer, 2008, , S. 566 The biosynthesis of furan fatty acids Occasionally it is speculated that the health-promoting properties originally attributed to omega-3 fatty acids may not be based on themself, but on the furan fatty acids also present in the fish.

Elymoclavine is then oxidized by four electrons by a P450 monooxygenase to give paspalic acid. Paspalic acid then undergoes isomerization of the carbon-carbon double bond that is in conjugation with the acid, to give D-lysergic acid. Fig4 - part 4 in biosynthesis of ergot alkaloid ergocryptine Lysergic Acid is a branch point in the biosynthesis of ergoamides and ergopeptines. On the path to ergocryptine, an ergopeptine, the tripeptide is installed by a Non-Ribosomal Peptide Synthase (NRPS).

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.

Cobinamide is the final compound in the biosynthesis of cobalamin. It has greater affinity for the cyanide than cobalamin itself, which suggests that it could be a better option for emergency treatment.

1554-1559 Several WRKY transcription factors also respond to gibberellin treatment.Suttipanta, Pattanaik, Kulshrestha, Patra, Singh, et al. (2011) The Transcription Factor CrWRKY1 Positively Regulates the Terpenoid Indole Alkaloid Biosynthesis in Catharanthus roseus.

Biosynthesis of TPP is feedback inhibited through actions of a riboswitch. Research is ongoing towards understanding biochemistry involved and towards facilitating technologies of socioeconomic value for supply of thiamine in various forms.

The biosynthesis of coumarin in plants is via hydroxylation, glycolysis, and cyclization of cinnamic acid. In humans, the enzyme encoded by the gene UGT1A8 has glucuronidase activity with many substrates, including coumarins.

Michelle C. Y. Chang is a chemist at the department of chemistry, University of California, Berkeley, a recipient of several young scientist awards for her research in biosynthesis of biofuels and pharmaceuticals.

Rita Harriet Harradence (16 September 1915 − 6 November 2012) was an Australian biochemist who pioneered the synthesis of penicillamine and steroids, and the stereochemistry of molecules involved in the biosynthesis of cholesterol.

Increased levels of these ribotides may cause feedback inhibition of amidophosphoribosyl transferase, the first and rate-limiting enzyme of purine biosynthesis. Allopurinol, therefore, decreases uric acid formation and may also inhibit purine synthesis.

Several biosynthesis routes lead to the thiazole ring as required for the formation of thiamine. Sulfur of the thiazole is derived from cysteine. In anaerobic bacteria, the CN group is derived from dehydroglycine.

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.

Its biosynthesis from mannose-1-phosphate follows a pathway similar to that of colitose, but is different in that it is aminated and does not undergo 3-OH deoxygenation or C-5 epimerization.

This enzyme participates in 6 metabolic pathways: lysine degradation, arginine and proline metabolism, phenylalanine metabolism, D-arginine and D-ornithine metabolism, D-alanine metabolism, and peptidoglycan biosynthesis. It employs one cofactor, pyridoxal phosphate.

This enzyme participates in glycine, serine and threonine metabolism and lysine biosynthesis. Aspartate-semialdehyde dehydrogenase may be cis-regulated by an Asd RNA motif found in the 5' UTR of some Asd genes.

The biosynthesis of aspartate and asparagine from oxaloacetate. Two asparagine synthetases are found in bacteria. Both are referred to as the AsnC protein. They are coded for by the genes AsnA and AsnB.

This enzyme participates in flavonoid biosynthesis. The Petunia hybrida (Petunia) genome contains two genes coding for very similar enzymes, ChiA and ChiB, but only the first seems to encode a functional chalcone isomerase.

Sterol-4-alpha-carboxylate 3-dehydrogenase, decarboxylating is an enzyme that in humans is encoded by the NSDHL gene. This enzyme is localized in the endoplasmic reticulum and is involved in cholesterol biosynthesis.

In bacterial cells the enzyme MurA is of vital importance, as it is responsible for the cytoplasmic biosynthesis of peptidoglycan precursor molecules. Cynaropicrin inhibits this enzyme, and thus it has potent antibacterial activity.

Alkaloids are known to play an important role in the defense of plants against herbivores.Ziegler, J. and P.J. Facchini, Alkaloid biosynthesis: metabolism and trafficking. Annu. Rev. Plant Biol., 2008. 59: p. 735-769.

The precursor to lipoic acid, octanoic acid, is made via fatty acid biosynthesis in the form of octanoyl-acyl carrier protein. In eukaryotes, a second fatty acid biosynthetic pathway in mitochondria is used for this purpose. The octanoate is transferred as a thioester of acyl carrier protein from fatty acid biosynthesis to an amide of the lipoyl domain protein by an enzyme called an octanoyltransferase. Two hydrogens of octanoate are replaced with sulfur groups via a radical SAM mechanism, by lipoyl synthase.

The systematic name of this enzyme class is UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L- lysine:D-alanyl-D-alanine ligase (ADP-forming). Other names in common use include MurF synthetase, UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D- alanyl-D-alanine, synthetase, UDP-N-acetylmuramoylalanyl-D-glutamyl-lysine-D- alanyl-D-alanine, ligase, uridine diphosphoacetylmuramoylpentapeptide synthetase, UDPacetylmuramoylpentapeptide synthetase, and UDP-MurNAc-L-Ala-D- Glu-L-Lys:D-Ala-D-Ala ligase. This enzyme participates in lysine biosynthesis and peptidoglycan biosynthesis.

This enzyme participates in phenylalanine, tyrosine and tryptophan biosynthesis and aminoacyl-tRNA biosynthesis. Phenylalanine- tRNA synthetase (PheRS) is known to be among the most complex enzymes of the aaRS (Aminoacyl-tRNA synthetase) family. Bacterial and mitochondrial PheRSs share a ferredoxin-fold anticodon binding (FDX-ACB) domain, which represents a canonical double split alpha+beta motif having no insertions. The FDX-ACB domain displays a typical RNA recognition fold (RRM) formed by the four- stranded antiparallel beta sheet, with two helices packed against it.

The mitochondria’s energetic and metabolic functions have been established to be non-essential for yeast cell viability. The only function that has been implicated in being necessary for survival is the biosynthesis of Fe/S clusters. RLI is the only known essential cytoplasmic Fe/S protein that is absolutely dependent on the mitochondrial Fe/S synthesis and export system for proper maturation. Rli1p is therefore a novel link between the mitochondria and ribosome function and biosynthesis, and therefore the viability of the cell.

UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 3 is an enzyme that in humans is encoded by the B3GNT3 gene. This gene encodes a member of the beta-1,3-N-acetylglucosaminyltransferase family. This enzyme is a type II transmembrane protein and contains a signal anchor that is not cleaved. It prefers the substrates of lacto-N-tetraose and lacto-N-neotetraose, and is involved in the biosynthesis of poly-N-acetyllactosamine chains and the biosynthesis of the backbone structure of dimeric sialyl Lewis a.

Biosynthesis of α-terpinene. "P" indicates a phosphate group, -PO32− The biosynthesis of α-terpinene and other terpenoids occurs via the mevalonate pathway because its starting reactant, dimethylallyl pyrophosphate (DMAPP), is derived from mevalonic acid. Geranyl pyrophosphate (GPP) is produced from the reaction of a resonance-stable allylic cation, formed from the loss of the pyrophosphate group from DMAPP, and isopentenyl pyrophosphate (IPP), and the subsequent loss of a proton. GPP then loses the pyrophosphate group to form the resonance-stable geranyl cation.

Chemical structure of cocaine The biosynthesis of cocaine has long attracted the attention of biochemists and organic chemists. This interest is partly motivated by the strong physiological effects of cocaine, but a further incentive was the unusual bicyclic structure of the molecule. The biosynthesis can be viewed as occurring in two phases, one phase leading to the N-methylpyrrolinium ring, which is preserved in the final product. The second phase incorporates a C4 unit with formation of the bicyclic tropane core.

Deoxyuridine monophosphate (dUMP) is the deoxygenated form of uridine monophosphate (UMP), and is the precursor to deoxythymine monophosphate (dTMP), a component of DNA nucleotide biosynthesis. By replacing the hydroxyl group at the 2' carbon of ribose with a hydrogen, UMP becomes deoxygenated to dUMP. The synthesis of deoxyuridine monophosphate (dUMP) is a multi-step process that begins with uridine monophosphate (UMP), the product of pyrimidine biosynthesis. The enzyme nucleoside monophosphate kinase converts UMP and ATP to uridine diphosphate (UDP) and ADP.

He is a co- founder, among many other well-known scientists, of the fields of glycomics and glycobiology. His research, which has been funded by the National Institutes of Health since 1984, has focused on the biochemical and molecular regulation of cellular metabolism and function. His work emphasizes the roles of glycoconjugates in cell adhesion and cell signaling. In his biochemical studies he is exploring the fundamental pathways of glycoconjugate biosynthesis and alterations in biosynthesis in human and animal diseases.

The general biosynthetic pathway of capsaicin and other capsaicinoids was elucidated in the 1960s by Bennett and Kirby, and Leete and Louden. Radiolabeling studies identified phenylalanine and valine as the precursors to capsaicin.Bennett DJ, Kirby GW (1968) Constitution and biosynthesis of capsaicin. J Chem Soc C 4:442–446 Enzymes of the phenylpropanoid pathway, phenylalanine ammonia lyase (PAL), cinnamate 4-hydroxylase (C4H), caffeic acid O-methyltransferase (COMT) and their function in capsaicinoid biosynthesis were identified later by Fujiwake et al.

The phenylpropanoids are a diverse family of organic compounds that are synthesized by plants from the amino acids phenylalanine and tyrosine. Their name is derived from the six-carbon, aromatic phenyl group and the three- carbon propene tail of coumaric acid, which is the central intermediate in phenylpropanoid biosynthesis. From 4-coumaroyl-CoA emanates the biosynthesis of myriad natural products including lignols (precursors to lignin and lignocellulose), flavonoids, isoflavonoids, coumarins, aurones, stilbenes, catechin, and phenylpropanoids. The coumaroyl component is produced from cinnamic acid.

The oxidation of germacratrien-12-ol to germacratrien-12-oic acid via the intermediate germacratrien-12-al is done by NADP+-dependent dehydrogenase(s). Germacratrien-12-oic acid is then hydroxylated at C6 subsequently followed by lactonization forming (+)-costunolide.1\. de Kraker, J.W.; Franssen, M.C.; Dalm M.C.; de Groot, A.; Bouwmeester, H.J.; “Biosynthesis of germacrene A carboxylic acid in chicory roots. Demonstration of a cytochrome P450 (+)-germacrene a hydroxylase and NADP+-dependent sesquiterpenoid dehydrogenase(s) involved in sesquiterpene lactone biosynthesis”. (2001).

The biosynthesis of the rapamycin core is accomplished by a type I polyketide synthase (PKS) in conjunction with a nonribosomal peptide synthetase (NRPS). The domains responsible for the biosynthesis of the linear polyketide of rapamycin are organized into three multienzymes, RapA, RapB, and RapC, which contain a total of 14 modules (figure 1). The three multienzymes are organized such that the first four modules of polyketide chain elongation are in RapA, the following six modules for continued elongation are in RapB, and the final four modules to complete the biosynthesis of the linear polyketide are in RapC. Then, the linear polyketide is modified by the NRPS, RapP, which attaches L-pipecolate to the terminal end of the polyketide, and then cyclizes the molecule, yielding the unbound product, prerapamycin.

In 2018, using growth conditions known to induce domoic acid production in Pseudo-nitzschia multiseries, transcriptome sequencing successfully identified candidate domoic acid biosynthesis genes responsible for the pyrrolidine core. These domoic acid biosynthesis genes, or ‘Dab’ enzymes were heterologously expressed, characterized, and annotated as dabA (terpene cyclase), dabB (hypothetical protein), dabC (α-ketoglutarate–dependent dioxygenase), and dabD (CYP450).centerDomoic acid biosynthesis begins with the DabA-catalyzed geranylation of L-glutamic acid (L-Glu) with geranyl pyrophosphate (GPP) to form N-geranyl-L-glutamic acid (L-NGG). DabD then performs three successive oxidation reactions at the 7′-methyl of L-NGG to produce 7′-carboxy-L-NGG, which is then cyclized by DabC to generate the naturally occurring isodomoic acid A. Finally, an uncharacterized isomerase could convert isodomoic acid A to domoic acid.

Leucine and β-hydroxy β-methylbutyric acid, a minor leucine metabolite, exhibit pharmacological activity in humans and have been demonstrated to promote protein biosynthesis via the phosphorylation of the mechanistic target of rapamycin (mTOR).

This enzyme is a part of the pathway of indole alkaloid biosynthesis. The indole alkaloids that result from this metabolic pathway are used by many plant species as a defense against herbivores and parasites.

The biosynthesis pathway of Neu5Gc from Neu5Ac was discovered by Shaw and Schauer in 1988, while the protein and DNA sequences for Neu5Gc, Neu5Ac, and CMAHP were described by Irie et al. in 1998.

Trimethyllysine dioxygenase, mitochondrial is an enzyme that in humans is encoded by the TMLHE gene in chromosome X. Mutations in the TMLHE gene resulting in carnitine biosynthesis disruption have been associated with autism symptoms.

Dyspropterin (6-pyruvoyltetrahydropterin, 6-PTHB) is an intermediate in tetrahydrobiopterin biosynthesis. It is the product of the enzyme 6-pyruvoyltetrahydropterin synthase and the substrate of two enzymes, 6-pyruvoyltetrahydropterin 2'-reductase and sepiapterin reductase.

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.

It is not known how mevalonate kinase mutations cause the febrile episodes, although it is presumed that other products of the cholesterol biosynthesis pathway, the prenylation chains (geranylgeraniol and farnesol) might play a role.

Weed Science. 43:445-453. Clomazone suppresses the biosynthesis of chlorophyll and other plant pigments.Storzer, Werner "The residue behaviour of new herbicides in crop plants" Nachrichtenblatt des Deutschen Pflanzenschutzdienstes 2002, vol. 54, 193-203.

Streptomyces cyaneofuscatus is a bacterium species from the genus of Streptomyces which has been isolated from soil in Daghestan in Russia.Deutsche Sammlung von Mikroorganismen und Zellkulturen Streptomyces cyaneofuscatus can be used for valinomycin biosynthesis.

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.

Other names in common use include cinnamic acid 2-hydroxylase, cinnamate 2-monooxygenase, cinnamic 2-hydroxylase, cinnamate 2-hydroxylase, and trans- cinnamic acid 2-hydroxylase. This enzyme participates in phenylalanine metabolism and phenylpropanoid biosynthesis.

Other names in common use include methyltetrahydroprotoberberine 14-hydroxylase, (S)-cis-N-methyltetrahydroberberine 14-monooxygenase, and (S)-cis-N-methyltetrahydroprotoberberine-14-hydroxylase. This enzyme participates in alkaloid biosynthesis i. It employs one cofactor, heme.

Bobera, R., & Rafaeli, A. (2010). Gene-silencing reveals the functional significance of pheromone biosynthesis activating neuropeptide receptor (PBAN-R) in a male moth. Proceedings of the National Academy of Sciences, 107 (39), 16858-16862.

Duportets, Line, et al. “The Pheromone Biosynthesis Activating Neuropeptide (PBAN) of the Black Cutworm Moth, Agrotis Ipsilon: Immunohistochemistry, Molecular Characterization and Bioassay of Its Peptide Sequence.” Insect Biochemistry and Molecular Biology, vol. 28, no.

IUBMB Life 2010, 62, 357–362. L-Carnitine is biosynthesized from Nε- trimethyllysine.Hulse, J. D.; Ellis, S. R.; Henderson, L. M. Carnitine biosynthesis. β-Hydroxylation of trimethyllysine by an α-ketoglutarate- dependent mitochondrial dioxygenase.

However, no specific evidence exists to suggest that leuA-Halobacteria motif RNAs function using these mechanisms. In addition, as of 2018, no mechanism is known for the regulation of leucine biosynthesis genes in archaea.

"Biosynthesis of isoprenoids (carotenoids, sterols, prenyl side-chains of chlorophylls and plastoquinone) via a novel pyruvate/glyceraldehyde 3-phosphate non-mevalonate pathway in the green alga Scenedesmus obliquus." Biochemical Journal 316.Pt 1 (1996): 73.

Auxin also regulates GA biosynthesis during fruit development in peas. These discoveries in different plant species suggest the auxin regulation of GA metabolism may be a universal mechanism. Ethylene decreases the concentration of bioactive GAs.

In aquatic habitats, nitrogen is often a limiting nutrient in regards to productivity and fixing it from the atmosphere is necessary to allow organisms to utilize it for the biosynthesis of molecules necessary for life.

"Voet's Biochemistry", 2nd edition, pp. 538, 1995. Anabolism is the biosynthesis phase of metabolism in which smaller simple precursors are converted to large and complex molecules of the cell. Anabolism has two classes of reactions.

Coumaroyl-coenzyme A is a central intermediate in the biosynthesis of myriad natural products found in plants. These products include lignols (precursors to lignin and lignocellulose), flavonoids, isoflavonoids, coumarins, aurones, stilbenes, catechin, and other phenylpropanoids.

The family of enzymes is important in amino acid and nucleotide metabolism as well as biodegradation of agricultural and industrial compounds. NagA participates in amino-sugar metabolism, specifically in the biosynthesis of amino-sugar-nucleotides.

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.

Even more surprising is the intracellular pathogen Chlamydia trachomatis, which lacks recognizable candidates for any genes involved in the biosynthesis or salvage of both NAD and NADP, and must acquire these coenzymes from its host.

Choi, Man-Yeon, et al. "Identification of a G protein-coupled receptor for pheromone biosynthesis activating neuropeptide from pheromone glands of the moth Helicoverpa zea." Proceedings of the National Academy of Sciences100.17 (2003): 9721-9726.

Mevalonic acid Mevalonate kinase deficiency (MKD), is an autosomal recessive metabolic disorder that disrupts the biosynthesis of cholesterol and isoprenoids. It is characterized by an elevated level of immunoglobin D in the blood. Mevalonate kinase (MVK) is an enzyme involved in biosynthesis of cholesterols and isoprenoids and is necessary for the conversion of mevalonate to mevalonate-5-phosphate in the presence of Mg2+. MKD is due to a mutation in the gene that encodes mevalonate kinase which results in a reduced or deficient activity of this enzyme.

The pathway for ethylene biosynthesis is named the Yang cycle after the scientist Shang Fa Yang who made key contributions to elucidating this pathway. Ethylene is biosynthesized from the amino acid methionine to S-adenosyl-L-methionine (SAM, also called Adomet) by the enzyme Met adenosyltransferase. SAM is then converted to 1-aminocyclopropane-1-carboxylic acid (ACC) by the enzyme ACC synthase (ACS). The activity of ACS determines the rate of ethylene production, therefore regulation of this enzyme is key for the ethylene biosynthesis.

Catsup regulates production of dopamine by serving as a negative regulator of rate-limiting enzymes in dopamine and pteridine synthesis pathways, both of which are required to occur for production of dopamine. In dopamine synthesis pathway, Catsup negatively regulates Tyrosine hydroxylase (TH) activity, preventing TH catalyzed conversion of tyrosine to the precursor of dopamine, L-Dopa. In pteridine biosynthesis pathway, Catsup negatively regulates the activity of GTP Cyclohydrolase I (GTPCH), preventing GTPCH catalyzed biosynthesis of TH cofactor required for TH catalytic activity and regulation, tetrahydrobiopterin (BH4).

The biosynthesis of plantazolicin (PZN) entails modification of a precursor peptide by several enzymes. In bacteria, plantazolicin (PZN) is synthesized first as an unmodified peptide via translation at the ribosome. A series of enzymes then chemically alter the peptide to install its post-translational modifications, including several azole heterocycles and an N-terminal amine dimethylation. Specifically, during the biosynthesis of PZN in B. velezensis, a ribosomally-synthesized precursor peptide undergoes extensive post- translational modification, including cyclodehydrations and dehydrogenations, catalyzed by a trimeric enzyme complex.

While Andrographolide is a relatively simple diterpene lactone, the biosynthesis by Andrographis paniculata was determined in the 2010s. Andrographolide is a member of the isoprenoid family of natural products. The precursors to isoprenoid biosynthesis, isopentenyl pyrophosphate (IPP) and dimethylallyl pyrophosphate (DMAPP), can be synthesized through either the mevalonic acid pathway (MVA) or deoxyxylulose pathway (DXP). Through selective C13 labeling of the precursors to both the MVA and DXP pathways, it was determined that the majority of the andrographolide precursors are synthesized through the DXP pathway.

Uridine monophosphate (UMP) biosynthesis Other DNA and RNA nucleotide bases that are linked to the ribose sugar via a glycosidic bond are thymine, cytosine and uracil (which is only found in RNA). Uridine monophosphate biosynthesis involves an enzyme that is located in the mitochondrial inner membrane and multifunctional enzymes that are located in the cytosol. # The first step involves the enzyme carbamoyl phosphate synthase combining glutamine with CO2 in an ATP dependent reaction to form carbamoyl phosphate. # Aspartate carbamoyltransferase condenses carbamoyl phosphate with aspartate to form uridosuccinate.

There are several possible ways of biosynthesis of tacrolimus. The fundamental units for biosynthesis are following: one molecule of 4,5-dihydroxycyclohex-1-enecarboxylic acid (DHCHC) as a starter unit, four molecules of malonyl-CoA, five molecules of methylmalonyl-CoA, one molecule of allylmalonyl-CoA as elongation units. However, two molecules of malonyl-CoA are able to be replaced by two molecules of methoxymalonyl CoA. Once two malonyl-CoA molecules are replaced, post- synthase tailoring steps are no longer required where two methoxymalonyl CoA molecules are substituted.

See Leukotriene#Biosynthesis, Hydroxyeicosatetraenoic acid, and Eoxin#Human biosynthesis. The enzyme 5-lipoxygenase (5-LO or ALOX5) converts arachidonic acid into 5-hydroperoxyeicosatetraenoic acid (5-HPETE), which may be released and rapidly reduced to 5-hydroxyeicosatetraenoic acid (5-HETE) by ubiquitous cellular glutathione-dependent peroxidases. Alternately, ALOX5 uses its LTA synthase activity to act convert 5-HPETE to leukotriene A4 (LTA4). LTA4 is then metabolized either to LTB4 by Leukotriene A4 hydrolase or Leukotriene C4 (LTC4) by either LTC4 synthase or microsomal glutathione S-transferase 2 (MGST2).

Due to its close phylogenetic relationship with the well-studied model plant species Arabidopsis thaliana, E. crepidifolium has been proposed as a suitable system for investigating the cardenolide biosynthetic pathway. Progesterone 5-beta-reductase, which was initially proposed as an enzyme of cardenolide biosynthesis in Digitalis, also has been cloned from E. crepidifolium. However, the natural substrate of this E. crepidifolium enzyme has not yet been identified. 3-beta-hydroxysteroid dehydrogenases represent another enzyme class that is predicted to be involved in cardenolide biosynthesis.

Peroxisome biogenesis disorders are autosomal recessive disorders often characterized by impaired plasmalogen biosynthesis. In these cases, the peroxisomal enzyme GNPAT, necessary for the initial steps of plasmalogen biosynthesis, is mislocalized to the cytoplasm where it is inactive. In addition, genetic mutations in the GNPAT or AGPS genes can result in plasmalogen deficiencies, which lead to the development of rhizomelic chondrodysplasia punctata (RCDP) type 2 or 3, respectively. In such cases, both copies of the GNPAT or AGPS gene must be mutated in order for disease to manifest.

The development of simvastatin was closely linked with lovastatin. Biochemist Jesse Huff and his colleagues at Merck began researching the biosynthesis of cholesterol in the early 1950s. In 1956, mevalonic acid was isolated from a yeast extract by Karl Folkers, Carl Hoffman, and others at Merck, while Huff and his associates confirmed that mevalonic acid was an intermediate in cholesterol biosynthesis. In 1959, the HMG-CoA reductase enzyme (a major contributor of internal cholesterol production) was discovered by researchers at the Max Planck Institute.

In enzymology, a polypeptide N-acetylgalactosaminyltransferase () is an enzyme that catalyzes the chemical reaction :UDP-N-acetyl-D-galactosamine + polypeptide \rightleftharpoons UDP + N-acetyl-D-galactosaminyl-polypeptide Thus, the two substrates of this enzyme are UDP-N-acetyl-D-galactosamine and polypeptide, whereas its two products are UDP and N-acetyl-D-galactosaminyl- polypeptide. This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. This enzyme participates in o-glycan biosynthesis and glycan structures - biosynthesis 1. It has 2 cofactors: manganese, and calcium.

In enzymology, a glucose-1-phosphate thymidylyltransferase () is an enzyme that catalyzes the chemical reaction :dTTP + alpha-D-glucose 1-phosphate \rightleftharpoons diphosphate + dTDP-glucose Thus, the two substrates of this enzyme are dTTP and alpha-D-glucose 1-phosphate, whereas its two products are pyrophosphate and dTDP-glucose. This enzyme belongs to the family of transferases, to be specific, those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). This enzyme participates in 3 metabolic pathways: nucleotide sugars metabolism, streptomycin biosynthesis, and polyketide sugar unit biosynthesis.

It also carries genes for the biosynthesis of the plant hormones, auxin and cytokinins, and for the biosynthesis of opines, providing a carbon and nitrogen source for the bacteria that most other micro-organisms can't use, giving Agrobacterium a selective advantage. By altering the hormone balance in the plant cell, the division of those cells cannot be controlled by the plant, and tumors form. The ratio of auxin to cytokinin produced by the tumor genes determines the morphology of the tumor (root-like, disorganized or shoot-like).

Brown's research interests focused on metabolic biochemistry, particularly in prokaryotes. His PhD work involved isolating and identifying a compound needed for the growth of Lactobacillus bulgaricus, which proved to be pantethine, an intermediate in the synthesis of coenzyme A. He based his research as a faculty member on broadening this work to identifying additional coenzymes and studying their biosynthesis. He was particularly instrumental in understanding the biosynthesis of folic acid and related pteridine compounds, and later described this work as the research he was most proud of.

Cynaropicrin is synthesized in the leaves of the artichoke plant and was found to accumulate in the trichomes. While the full mechanism of biosynthesis of cynaropicrin is unknown, it is proposed that biosynthesis starts with three isoprene C5-units, which are processed by the mevalonate pathway to form farnesyl pyrophosphate (FPP). With germacrene A and germacrene A acid as intermediates, FPP is converted into costunolide using two syntheses and a cytochrome P450 oxidase. Multiple yet unknown reactions occur to first form guaianolide and later cynaropicrin.

Insight into the biosynthesis of the isopropoxy-2-naphthonate appendage was similarly gained by comparative analysis of the ked cluster to those of neocarzinostatin and maduropeptin, enediynes with naphthonate or benzoate substructures, respectively. Five genes, KedN1–N5, bear high sequence homology with the enzymes responsible for naphthonate synthesis in neocarzinostatin—consequently, the intermediacy of 3,6,8-trihydroxy-2-naphthoic acid is proposed in kedarcidin biosynthesis. This compound is believed to be oxygenated to the 3,6,7,8-tetrahydroxy derivative, then triply O-methylated by KedN1, an O-methyltransferase.

SCS facilitates the flux of molecules into other metabolic pathways by controlling the interconversion between succinyl CoA and succinate. This is important because succinyl CoA is an intermediate necessary for porphyrin, heme, and ketone body biosynthesis.

Lysophosphatidylcholine acyltransferase 1 is a protein in humans that is encoded by the LPCAT1 gene. Lysophosphatidylcholine (LPC) acyltransferase (LPCAT; EC 2.3.1.23) catalyzes the conversion of LPC to phosphatidylcholine (PC) in the remodeling pathway of PC biosynthesis.

According to the Kyoto Encyclopedia of Genes and Genomes (KEGG), Rathayibacter toxicus strain WAC3373 is capable of performing glycolysis, citric acid cycle (TCA), arginine biosynthesis, amino acid metabolism, carbohydrate metabolism, and various bacterial DNA repair mechanisms.

54, pp. 519–46. In Arabidopsis thaliana, this compound is part of the lignin biosynthesis pathway. The enzyme dihydroflavonol 4-reductase uses sinapaldehyde and NADPH to produce sinapyl alcohol and NADP+.Dihydroflavonol 4-reductase on arabidopsisreactome.

The Embeden–Meyerhof pathway and the Krebs cycle are the centre of metabolism in nearly all bacteria and eukaryotes. They provide not only energy but also precursors for biosynthesis of macromolecules that make up living systems.

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.

Synthesis of steviol glycoside begins with isoprene units created via the DXP or MEP pathway.Lichtenhalter, H.K., 1999. The 1-deoxy-D-xylulose-5-phosphate pathway of isoprenoid biosynthesis in plants. Annu. Rev. Plant Physiol. PlantMol. Biol.

MCAT is also involved in bacterial polyketide biosynthesis. The enzyme MCAT together with an acyl carrier protein (ACP), and a polyketide synthase (PKS) and chain-length factor heterodimer, constitutes the minimal PKS of type II polyketides.

Glycosylphosphatidylinositol (GPI) is a complex glycolipid that anchors many proteins to the cell surface. PIGW acts in the third step of GPI biosynthesis and acylates the inositol ring of phosphatidylinositol (Murakami et al., 2003 [PubMed 14517336]).

Howard Sachs (July 12, 1926 – December 6, 2011), was a biochemist who helped pioneer the study of neuroendocrinology. His discoveries concerning the production of the hormone vasopressin laid the foundation for the field of hormone biosynthesis.

Am. J. Clin. Nutr. 1986, 43, 234–238. The carnitine biosynthesis pathway is highly conserved among many eukaryotes and some prokaryotes.Lindstedt, G.; Lindstedt, S.; Midtvedt, T.; Tofft, M. The formation and degradation of carnitine in Pseudomonas.

Proprotein convertase 1 is the enzyme largely responsible for the first step in the biosynthesis of insulin. Following the action of proprotein convertase 1, a carboxypeptidase is required to remove the basic residues from the processing intermediate and generate the bioactive form of insulin. Another prohormone convertase, proprotein convertase 2 plays a more minor role in the first step of insulin biosynthesis, but a greater role in the first step of glucagon biosynthesis. The knockout of proprotein convertase 1 is not lethal in mice or humans, most likely due to the presence of the second convertase, although mice lacking proprotein convertase 1 activity show a number of defects including slow growth. Proprotein convertase 1 is a calcium (Ca2+) activated serine endoprotease (meaning that a serine residue is part of the active site that hydrolyzes the peptide bond within the substrate).

A steroidogenesis inhibitor, also known as a steroid biosynthesis inhibitor, is a type of drug which inhibits one or more of the enzymes that are involved in the process of steroidogenesis, the biosynthesis of endogenous steroids and steroid hormones. They may inhibit the production of cholesterol and other sterols, sex steroids such as androgens, estrogens, and progestogens, corticosteroids such as glucocorticoids and mineralocorticoids, and neurosteroids. They are used in the treatment of a variety of medical conditions that depend on endogenous steroids. Steroidogenesis inhibitors are analogous in effect and use to antigonadotropins (which specifically inhibit sex steroid production), but work via a different mechanism of action; whereas antigonadotropins suppress gonadal production of sex steroids by effecting negative feedback on and thereby suppressing the hypothalamic-pituitary- gonadal axis, steroidogenesis inhibitors directly inhibit the enzymatic biosynthesis of steroids.

350x350px The difficulty distinguishing between L-tryptophan and free tryptamine as the precursor of harmine biosynthesis originates from the presence of the serotonin biosynthetic pathway, which closely resembles that of harmine, yet necessitates the availability of free tryptamine as its precursor. As such, it is unclear if the decarboxylation of L-tryptophan, or the incorporation of pyruvate into the basic tryptamine structure is the first step of harmine biosynthesis. However, feeding experiments involving the feeding of one of tryptamine to hairy root cultures of P. harmala showed that the feeding of tryptamine yielded a great increase in serotonin levels with little to no effect on β-carboline levels, confirming that tryptamine is the precursor for serotonin, and indicating that it is likely only an intermediate in the biosynthesis of harmine; otherwise, comparable increases in harmine levels would have been observed.

The route of biosynthesis and physiological function of sulfoquinovosyl diacylglycerol is still under investigation. From recent studies it is evident that sulfite it the likely sulfur precursor for the formation of the sulfoquinovose group of this lipid.

Hydroxyphenylpyruvate reductase is also an enzyme involved in this biosynthesis.Two new enzymes of rosmarinic acid biosynthesis from cell cultures of Coleus blumei: hydroxyphenylpyruvate reductase and rosmarinic acid synthase. Petersen M and Alfermann AW, Z. Naturforsch. C: Biosci.

GAD1 – essential for the biosynthesis of the neurotransmitter GABA – is expressed in interneurons. Proteins expressed in glial cells include astrocyte markers GFAP and S100B whereas myelin basic protein and the transcription factor OLIG2 are expressed in oligodendrocytes.

Elymoclavine is an ergot alkaloid (ergoline alkaloid). It can be produced from C. fusiformis from Pennisetum typhoideum. It is a precursor in the biosynthesis of D-(+)-lysergic acid. Ergot alkaloids are natural products derived from L-tryptophan.

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.

Its mechanism of action was found to be correlated to the ability to inactivate two vital enzymes that play a significant role in mycobacterial cell wall biosynthesis namely UDP-galactopyranose mutase (UGM) and arylamine-N-acetyltransferase (TBNAT).

2-C-Methyl--erythritol 4-phosphate (MEP) is an intermediate on the MEP pathway (non-mevalonate pathway) of isoprenoid precursor biosynthesis. It is the first committed metabolite on that pathway on the route to IPP and DMAPP.

The ε-amino groups of the lysine residues in urease and phosphotriesterase also feature carbamate. The carbamate derived from aminoimidazole is an intermediate in the biosynthesis of inosine. Carbamoyl phosphate is generated from carboxyphosphate rather than CO2.

Subsequent condensatiions yield triketides, tetraketide, etc. Biosynthesis of orsellinic acid from polyketide intermediate. The polyketide chains produced by a minimal polyketide synthase are almost invariably modified. Modifications include reduction of the keto groups to methylene and cyclization.

1,2-Dimethoxybenzene is naturally occurring. Its biosynthesis entails the methylation of guaiacol by guaiacol O-methyltransferase. 1,2-Dimethoxybenzene is an insect attractant. Guaiacol O-methyltransferase gene is first scent gene discovered so far in any plant species.

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.

In the Golgi, SREBF1 is cleaved and released as a transcriptionally active mature protein. It is then free to translocate to the nucleus and activate the expression of its target genes.Proteolytic activation of SREBF-controlled lipid biosynthesis.

Lanosterol Lanosterol 14α-demethylase (CYP51A1) is a cytochrome P450 enzyme that is involved in the conversion of lanosterol to 4,4-dimethylcholesta-8(9),14,24-trien-3β-ol. The cytochrome P450 isoenzymes are a conserved group of proteins that serve as key players in the metabolism of organic substances and the biosynthesis of important steroids, lipids, and vitamins in eukaryotes. As a member of this family, lanosterol 14α-demethylase is responsible for an essential step in the biosynthesis of sterols. In particular, this protein catalyzes the removal of the C-14α-methyl group from lanosterol.

Despite anisomycin's wide usage as a protein synthesis inhibitor, there have been a lot of studies centered on the biosynthesis of anisomycin. One study by Butler in 1974 proposed possible precursors to this natural product. Fermentation of Streptomyces with labeled amino acids was followed by a degradation of the radioactive anisomycin and deacetylanisomycin products to determine the locations of the labeled carbons. Although its pyrrolidine-based structure suggests that it is derived from proline, the results from the experiments indicated that tyrosine, glycine, methionine, and acetate are the primary precursors for the biosynthesis of anisomycin.

When synthesized in bacteria, DHPG requires 5 enzymes, DpgA-D and 4-hydroxyphenylglycine transferase (Pgat), in order to be synthesized.Pfeifer, V., Nicholson, G. J., Ries, J., Recktenwalk, J., Schefer, A. B., Shawky, R. M., Schröder, J., Wohlleben, W., Pelzer, S. "A Polyketide Synthase in glycopeptide Biosynthesis: the Biosynthesis of the Non-Proteogenic Amino Acid (S)-3,5-Dihydroxyphenylglycine." The Journal of Biological Chemistry, 2001, 276 (42/19), 38370-38377. DpgA is a type III polyketide synthase and initiates the synthesis by condensing acetyl-CoA with three molecules of malonyl-CoA.

Streptomyces cattleya is a Gram-positive bacterium which makes cephamycin, penicillin and thienamycin. The bacterium expresses a fluorinase enzyme, and the organism has been used to understand the biosynthesis of fluoroacetate and the antibacterial 4-fluoro-L-threonine. The γ-Glu-βes pathway to biosynthesis of non-traditional amino acids β-ethynylserine (βes) and L-propargylglycine (Pra) was first characterized in this species. The genome, which was sequenced in 2011, contains one chromosome with 6,283,062 base pairs and one megaplasmid with 1,809,491 bp, with an overall guanine-cytosine content of 73%.

The tricarboxylate transport protein is located within the inner mitochondria membrane. It provides a link between the mitochondrial matrix and cytosol by transporting citrate through the impermeable inner mitochondrial membrane in exchange for malate from the cytosol. The citrate transported out of the mitochondrial matrix by the tricarboxylate transport protein is catalyzed by citrate lyase to acetyl CoA, the starting material for fatty acid biosynthesis, and oxaloacetate. As well, cytosolic NADPH + H+ necessary for fatty acid biosynthesis is generated in the reduction of oxaloacetate to malate and pyruvate by malate deydrogenase and the malic enzyme.

Many cofactors (non-protein-based helper molecules) feature thiols. The biosynthesis and degradation of fatty acids and related long-chain hydrocarbons is conducted on a scaffold that anchors the growing chain through a thioester derived from the thiol Coenzyme A. The biosynthesis of methane, the principal hydrocarbon on Earth, arises from the reaction mediated by coenzyme M, 2-mercaptoethyl sulfonic acid. Thiolates, the conjugate bases derived from thiols, form strong complexes with many metal ions, especially those classified as soft. The stability of metal thiolates parallels that of the corresponding sulfide minerals.

The biosynthesis of staurosporine starts with the amino acid L-tryptophan in its zwitterionic form. Tryptophan is converted to an imine by enzyme StaO which is an L-amino acid oxidase (that may be FAD dependent). The imine is acted upon by StaD to form an uncharacterized intermediate proposed to be the dimerization product between 2 imine molecules. Chromopyrrolic acid is the molecule formed from this intermediate after the loss of VioE (used in the biosynthesis of violacein – a natural product formed from a branch point in this pathway that also diverges to form rebeccamycin.

Carbidopa inhibits aromatic-L-amino-acid decarboxylase (DOPA decarboxylase or DDC), an enzyme important in the biosynthesis of L-tryptophan to serotonin and in the biosynthesis of L-DOPA to dopamine (DA). DDC exists both outside of (body periphery) and within the confines of the blood–brain barrier. Carbidopa is used in the treatment of, among other diseases, Parkinson's disease (PD), a condition characterized by death of dopaminergic neurons in the substantia nigra. Increased dopamine availability may increase the effectiveness of the remaining neurons and alleviate symptoms for a time.

A novel aspect of PQQ is its biosynthesis in bacteria from a ribosomally translated precursor peptide, PqqA. A glutamic acid and a tyrosine in PqqA are cross-linked by the radical SAM enzyme PqqE in the first step of PqqA modification. Efforts to understand PQQ biosynthesis have contributed to broad interest in radical SAM enzymes and their ability to modify proteins, and an analogous radical SAM enzyme-dependent pathway has since been found that produces the putative electron carrier mycofactocin, using a valine and a tyrosine from the precursor peptide, MftA.

The intermediates of the biosynthesis of clavulanic acid Clavulanic acid is biosynthesized from the amino acid arginine and the sugar glyceraldehyde 3-phosphate. With the β-lactam like structure, clavulanic acid looks structurally similar to penicillin, but the biosynthesis of this molecule involves a different pathway and set of enzymes. Clavulanic acid is biosynthesized by the bacterium Streptomyces clavuligerus, using glyceraldehyde-3-phosphate and L-arginine as the starting materials of the pathway. Although all of the intermediates of the pathway are known, the exact mechanism of each enzymatic reaction is not fully understood.

The biosynthesis of Tyrocidine is similar to Gramicidin S, and is achieved through the use of nonribosomal protein synthetases (NRPSs). Its biosynthesis is via an enzymatic assembly consisting of 3 peptide synthetase proteins, TycA, TycB, and TycC, which contain 10 modules. The different tyrocidine analogues (A–D) are not produced by different enzymes, but rather by an enzyme system that is capable of incorporating different amino acids of structural similarity at specified sites. The amino acid sequence is determined by the organization of the enzyme and not by any RNA template.

Botrydial originates from the BcBOT2 (Botrytiscinerea BOTrydial biosynthesis) mediated cyclization of farnesyl diphosphate (FPP) to key intermediate tricyclic alcohol presilphiperfolan-8β-ol. Pinedo et al. demonstrated that BcBOT2 is in fact a sesquiterpene synthase by incubation of FPP with recombinant BcBOT2 protein, which yielded the expected presilphiperfolan-8-ol as the major product. Image:GeneralBiosynBotrydial.png 4 other genes are then involved in the biosynthesis of botrydial: 3 genes that encode for a P450 monooxygenase (BcBOT3, BcBOT1, BcBOT4) and a BcBOT5 gene whose amino acid sequence showed high homology to known acetyl transferases.

Unlike many other cofactors, molybdenum cofactor (Moco) cannot be taken up as a nutrient. The cofactor thus requires de novo biosynthesis. Molybdenum cofactor biosynthesis occurs in four steps: (i) the radical-mediated cyclization of nucleotide, guanosine triphosphate (GTP), to (8S)‑3',8‐cyclo‑7,8‑dihydroguanosine 5'‑triphosphate (), (ii) the formation of cyclic pyranopterin monophosphate (cPMP) from the , (iii) the conversion of cPMP into molybdopterin (MPT), (iv) the insertion of molybdate into MPT to form Moco. Two enzyme-mediated reactions convert guanosine triphosphate to the cyclic phosphate of pyranopterin.

The neurohormone pheromone biosynthesis activating neuropeptide is found in the ant that activates the biosynthesis of pheromones from the Dufour's gland. The spermatheca gland is found in queens, which functions in sperm maintenance. Males appear to lack these glands, but those associated with its head are morphologically similar to those found in workers, but these glands may act differently. Water loss rates of workers and female alates in S. invicta and S. richteri The ant faces many respiratory challenges due to its highly variable environment, which can cause increased desiccation, hypoxia, and hypercapnia.

The discovery of this gene provided the first experimental data to support the hypotheses that the precursors for tabtoxin originate from the lysine biosynthetic pathway. The deduced amino acid sequence of tabA showed significant relatedness to lysA, which encodes DAP decarboxylase in bacteria. Although tabA was not required for lysine biosynthesis, the deduced product of a tabB, also located in the TβL biosynthetic region, showed relatedness todapD, a gene encoding THDPA succinyl-CoA succinyltransferase (THDPA-ST). DapB is essential for both lysine and tabtoxin biosynthesis and THDPA may be an intermediate in both pathways.

Most lipids are synthesized in yeast either in the endoplasmic reticulum, lipid particles, or the mitochondrion, with little or no lipid synthesis occurring in the plasma membrane or nuclear membrane. Sphingolipid biosynthesis begins in the endoplasmic reticulum, but is completed in the Golgi apparatus. The situation is similar in mammals, with the exception of the first few steps in ether lipid biosynthesis, which occur in peroxisomes. The various membranes that enclose the other subcellular organelles must therefore be constructed by transfer of lipids from these sites of synthesis.

Based on basic polyketide synthesis, the biosynthesis of annonacin is likely accomplished by a modular polyketide synthase (PKS). The biosynthesis likely involves the use of 17 modules consisting of a number of enzymes commonly found in PKS. These include the acyl carrier protein (ACP), acetyl transferase (AT), ketosynthase (KS), malonyl transferase (MT; which can come carrying a variety of functionalities), ketoreductase (KR), dehydratase (DH), and enoyl reductase (ER). An example of the possible modular biosynthetic pathway detailing the combination of these enzymes and the subsequent modules can be seen in the figure below.

Biosynthesis from farnesol ⁠— ⁠bonds to be formed and major atoms to be added are in while bonds to be broken and atoms/structural segments to be removed are in The complete mechanism of the biosynthesis of cantharidin is unknown. Its framework formally consists of two isoprene units. However, feeding studies indicate that the biosynthetic process is more complicated and not a simple product of geranyl pyrophosphate or related ten-carbon parent structure as the seeming monoterpene nature would suggest. Instead, there is a farnesol (15-carbon) precursor from which certain carbon segments are later excised.

In the (p)ppGpp biosynthesis cycle, NDPK serves an important role. When there is an absence of a charged tRNA in the A site of a ribosome, the ribosome will stall and trigger the synthesis of the guanosine pentaphosphate ((p)ppGpp) molecule. (p)ppGpp biosynthesis is a part of the purine metabolism pathway and coordinates a series of cellular activities in response to nutritional abundances. Synthesis of (p)ppGpp is triggered by carbon starvation, or the lack of carbon in the cell's environment, and causes the protein SpoT to activate.

Photosynthesizing plants, algae and cyanobacteria synthesize tocochromanols, the chemical family of compounds made up of four tocopherols and four tocotrienols; in a nutrition context this family is referred to as Vitamin E. Biosynthesis starts with formation of the closed-ring part of the molecule as homogentisic acid (HGA). The side chain is attached (saturated for tocopherols, polyunsaturated for tocotrienols). The pathway for both is the same, so that gamma- is created and from that alpha-, or delta- is created and from that the beta- compounds. Biosynthesis takes place in the plastids.

Biosysnthesis by the transsulfuration pathway starts with aspartic acid. Relevant enzymes include aspartokinase, aspartate-semialdehyde dehydrogenase, homoserine dehydrogenase, homoserine O-transsuccinylase, cystathionine-γ-synthase, Cystathionine-β-lyase (in mammals, this step is performed by homocysteine methyltransferase or betaine—homocysteine S-methyltransferase.) Methionine biosynthesis is subject to tight regulation. The repressor protein MetJ, in cooperation with the corepressor protein S-adenosyl-methionine, mediates the repression of methionine's biosynthesis. The regulator MetR is required for MetE and MetH gene expression and functions as a transactivator of transcription for these genes.

SpeF is a putative cis-acting element identified in several gram negative alpha proteobacteria. It is proposed to be involved in regulating expression of genes involved in polyamide biosynthesis. SpeF is one of five putative regulatory elements identified by a computational screen of Agrobacterium tumefaciens and other alpha-proteobacterial genomes for conserved sequence motifs in operon leaders. In the majority of species analysed it is located in the leader of an operon containing the speF gene an ornithine decarboxylase enzyme that catalyses one of the first steps in polyamine biosynthesis.

However, the efficacy and safety of statins has been recently scrutinized in a number of reports. This is largely because blocking the cholesterol biosynthesis pathway before squalene has been found to disrupt the synthesis of isoprenoids, which are used for the biosynthesis of key molecules in RNA transcription, ATP synthesis, and other essential cell activities. Oxidosqualene cyclase, which is downstream of squalene in the pathway, is an attractive target for inhibition. Many inhibitors have been proposed, among them steroid analogs, phenol-based compounds, benzamide and carboxamide derivatives, and nitrogen- containing heterocyclic compounds.

The proposed biosynthesis of ginsenoside Rb1 in left The biosynthesis of GRb1 in Panax ginseng starts from farnesyl diphosphate (FPP), which is converted to squalene with squalene synthase (SQS), then to 2,3-oxidosqualene with squalene epoxidase (SE). The 2,3-oxidasqualene is then converted to dammarenediol-II by cyclization, with dammarenediol-II synthase (DS) as the catalyst. The dammarenediol-II is converted to protopanaxadiol and then to ginsenoside Rd. Finally, GRb1 is synthesized from ginsenoside Rd, catalysed by UDPG:ginsenoside Rd glucosyltransferase (UGRdGT), a biosynthetic enzyme of GRb1 first discovered in 2005.

There is some information on serum vitamin C concentrations maintained in animal species that are able to synthesize vitamin C. One study of several breeds of dogs reported an average of 35.9 μmol/L. A report on goats, sheep and cattle reported ranges of 100–110, 265-270 and 160-350 μmol/L, respectively. Vitamin C biosynthesis in vertebrates The biosynthesis of ascorbic acid in vertebrates starts with the formation of UDP-glucuronic acid. UDP-glucuronic acid is formed when UDP-glucose undergoes two oxidations catalyzed by the enzyme UDP- glucose 6-dehydrogenase.

Current knowledge indicates mitosomes probably play a role in Fe-S cluster assembly, since they do not display any of the proteins involved in other major mitochondrial functions (aerobic respiration, haem biosynthesis) and they do display proteins required for Fe-S cluster biosynthesis (like frataxin, cysteine desulfurase, Isu1 and a mitochondrial Hsp70). Unlike mitochondria, mitosomes do not have genes within them. The genes for mitosomal components are contained in the nuclear genome. An early report suggested the presence of DNA in this organelle, but more recent research has shown this not to be the case.

The precise regulatory mechanisms exerted by PBAN on the different steps of pheromone biosynthesis remain to be determined. However, the receptor of this neuropeptide has been already cloned. The receptor belongs to the G-protein coupled receptors, and its activation leads to an increase of intracellular Calcium levels. According to the effects of gene disruption in the pheromone synthesis of Bombykol (the main pheromone component of the silk moth Bombyx mori and the corn earworm moth), the increase in intracellular calcium levels turns to activate different key enzymes of the last steps of pheromone biosynthesis.

The N-terminal domain is the carbamoyl phosphate binding domain. The C-terminal domain is an aspartate/ornithine-binding domain. Aspartate carbamoyltransferase (ATCase) catalyses the conversion of aspartate and carbamoyl phosphate to carbamoylaspartate, the second step in the de novo biosynthesis of pyrimidine nucleotides. In prokaryotes ATCase consists of two subunits: a catalytic chain (gene ) and a regulatory chain (gene pyrI), while in eukaryotes it is a domain in a multi- functional enzyme (called URA2 in yeast, rudimentary in Drosophila, and CAD in mammals) that also catalyzes other steps of the biosynthesis of pyrimidines.

Ubiquinone is an essential electron carrier in prokaryotes. In Escherichia coli, the Ubiquinone biosynthesis pathway involves at least nine reactions whereby 3-octaprenyl4-hydroxybenzoate decarboxylase (UbiD) is an enzyme on the pathway which catalyses the conversion of the substrate 3-octaprenyl-4-hydroxybenzoate to the product, 2-octaprenyl phenol. E. coli ubiD- mutants have defects in Q8 biosynthesis, accumulate 4-hydroxy-3-octaprenylbenzoicacid (HP8B), and lack decarboxylase activity in vitro. However, E. coli ubiD- mutants retained the ability to produce about 20–25% of the normal levels of Q 4-hydroxy-3-octaprenylbenzoic acid.

Such epoxidation in post-PKS modications has been seen in epothilone biosynthesis by EpoK. In EpoK, the consensus mechanism of epoxidation by P450 involves the formation of a pi-complex between an oxoferryl pi-cation radical species (FeIV) and the olefin pi bond, followed by electron transfer, formation of the olefin pi-cation radical and finally epoxidation. However, it is also possible that in addition to cytochrome p450, a FAD-dependent monoxygenase is also required to install the epoxide. This codependent process is seen in tirandamycin biosynthesis by TamL.

Nicotine biosynthesis The biosynthetic pathway of nicotine involves a coupling reaction between the two cyclic structures that comprise nicotine. Metabolic studies show that the pyridine ring of nicotine is derived from niacin (nicotinic acid) while the pyrrolidine is derived from N-methyl-Δ1-pyrrollidium cation. Biosynthesis of the two component structures proceeds via two independent syntheses, the NAD pathway for niacin and the tropane pathway for N-methyl-Δ1-pyrrollidium cation. The NAD pathway in the genus Nicotiana begins with the oxidation of aspartic acid into α-imino succinate by aspartate oxidase (AO).

She has studied the biosynthesis of piperidine alkaloids. She has studied the biodiversity of Brazil, and called for new technologies and scientific policy to support preservation of the Brazilian rainforest. She has since studied phytochemistry and endophytic fungi.

Proposed PKS-NRPS organization responsible for production of (1) in the biosynthesis of chaetoglobosin A. Chaetoglobosin A is a fungal isolate with anticancer activity in vitro. Derivatives of the compound include MBJ-0038, MBJ-0039, and MBJ-0040.

Resveratrol is a biologically important stilbenoid. Stilbenoids are hydroxylated derivatives of stilbene. They have a C6–C2–C6 structure. In biochemical terms, they belong to the family of phenylpropanoids and share most of their biosynthesis pathway with chalcones.

Dr. Sattely completed her graduate training at Boston College in organic chemistry with Amir Hoveyda and her postdoctoral studies in biochemistry at Harvard Medical School with Christopher T. Walsh, where she worked on natural product biosynthesis in bacteria.

Since phospholipase A2 is required for the biosynthesis of the potent mediators of inflammation, prostaglandins, and leukotrienes, annexin A1 may have potential anti-inflammatory activity. Glucocorticoids stimulate production of lipocortin. In this way, synthesis of eicosanoids are inhibited.

Other names in common use include bornyl pyrophosphate synthase, bornyl pyrophosphate synthetase, (+)-bornylpyrophosphate cyclase, and geranyl-diphosphate cyclase (ambiguous). This enzyme participates in monoterpenoid biosynthesis and belongs to the family of isomerases, specifically the class of intramolecular lyases.

The biosynthesis of 4-hydroxycoumarin and dicoumarol by Aspergillus fumigatus Fresenius. Biochemical Journal 117, 237-245. The identification of Dicoumarol in 1940 is the precursor of the drug class known as 4-Hydroxycoumarin. See warfarin for this history.

In higher plants, DMSP is biosynthesized from S-methylmethionine. Two intermediates in this conversion are dimethylsulfoniumpropylamine and dimethylsulfoniumpropionaldehyde. In algae, however, the biosynthesis starts with the removal of the amino group from methionine, rather than from S-methylmethionine.

Ze339 brand extract is not an antihistamine and represents a symptomatic treatment with very different properties. In-vitro studies show that petasins in Ze339 brand extract inhibit leukotriene biosynthesis and block degranulation in activated mast cells and eosinophils.

Based on the hypothesized biosynthesis of palau'amine, a proposed pathway to this dimeric pyrrole-imidazole alkaloid includes a key oxidation of a β-ketoester with manganese(III) acetate to initiate a cascade radical cyclization, producing an ageliferin skeleton.

The genome of the tulsi plant has been sequenced and reported as a draft, estimated to be 612 mega bases, with results showing genes for biosynthesis of anthocyanins in Shyama Tulsi, ursolic acid and eugenol in Rama Tulsi.

4-(γ-Glutamylamino)butanoic acid is molecule that consists of L-glutamate conjugated to γ-aminobutyric acid (GABA). It is the substrate of the enzyme γ-glutamyl-γ-aminobutyrate hydrolase, which is involved in the biosynthesis of polyamines.

Haslinger, K., Peschke, M., Brieke, C., Maximowitsch. E., Cryle, M. J. "X-domain of peptide synthetases recruits oxygenases crucial for glycopeptide biosynthesis." Nature, 2015, 521, 105-110. Finally, the TE, or thioesterase, region releases chloroeremomycin from the NRPS complex.

The biosynthesis of malvalic acid starts with oleic acid, an 18-carbon monounsaturated fatty acid, leading to sterculic acid. An α-oxidation reaction removes one carbon from the chain to form the 17-carbon- chain structure of malvalic acid.

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.

The haloacid dehydrogenase superfamily (HAD superfamily) is a superfamily of enzymes that include phosphatases, phosphonatases, P-type ATPases, beta- phosphoglucomutases, phosphomannomutases, and dehalogenases, and are involved in a variety of cellular processes ranging from amino acid biosynthesis to detoxification.

In the typical porphyrin biosynthesis pathway, four molecules of porphobilinogen are concatenated by carbons 2 and 5 of the pyrrole ring (adjacent to the nitrogen atom) into hydroxymethyl bilane by the enzyme porphobilinogen deaminase, also known as hydroxymethylbilane synthase.

Zymosterol is an intermediate in cholesterol biosynthesis. Disregarding some intermediate compounds (e.g. 4-4-dimethylzymosterol) lanosterol can be considered a precursor of zymosterol in the cholesterol synthesis pathway. The conversion of zymosterol into cholesterol happens in the endoplasmic reticulum.

C6orf52 has one identified paralog, tRNA selenocysteine 1-associated protein 1 (TRNAU1AP), which is located on chromosome one at 1p35.3. TRNAU1AP is involved selenocysteine biosynthesis, selenoproteins synthesis efficiency enhancement and may be involved in the methylation of tRNA(Sec).

ERG4 or Delta(24(24(1)))-sterol reductase or Delta(24(28))-sterol reductase is a enzyme that catalyzes the last step of ergosterol biosynthesis pathway in fungi Saccharomyces cerevisiae (Baker's yeast), which 5,7,22,24(28)-ergostatetraenol converted into ergosterol.

Biosynthesis of bleomycin is completed by glycosylation of the aglycones. Bleomycin naturally occurring- analogues have two to three sugar molecules, and DNA cleavage activities of these analogues have been assessed, primarily by the plasmid relaxation and break light assays.

However, reports of ABS in some offspring of mothers who were treated with fluconazole, an antifungal agent which interferes with cholesterol biosynthesis at the level of CYP51 activity - indicate that disordered drug metabolism may result from deficient POR activity.

Sbrissa D, Ikonomov OC, Deeb R, Shisheva A. Phosphatidylinositol 5-phosphate biosynthesis is linked to PIKfyve and is involved in osmotic response pathway in mammalian cells. J Biol Chem. 2002 Dec 6;277(49):47276-84. Epub 2002 Sep 20.

New N-halogenoacetyl derivatives leading to a strong in situ inhibition of AANAT. The concept behind the mechanism of action of these precursors was studied by following the biosynthesis of the inhibitor from tritiated-BAT in a living cell.

The biosynthesis of the tropane alkaloid, however, is still uncertain. Hemscheidt proposes that Robinson's acetonedicarboxylate emerges as a potential intermediate for this reaction. Condensation of N-methylpyrrolinium and acetonedicarboxylate would generate the oxobutyrate. Decarboxylation leads to tropane alkaloid formation.

Current model of monolignol biosynthesis in land plants. Three most common lignin monomers shown in green, all other compounds shown in orange. CCR step highlighted. CCoA-OMT: caffeoyl- CoA O-methyltransferase; CAD: cinnamyl alcohol dehydrogenase; COMT: caffeate O-methyltransferase.

Iminoaspartic acid (also known as iminosuccinate or iminoaspartate) is a dicarboxylic acid in the biosynthesis of nicotinic acid. It is synthesised by the oxidation of aspartate and is condensed by quinolinate synthase with glycerone phosphate to form quinolinic acid.

Cytochrome P450 family 107 subfamily G member 1 (abbreviated CYP107G1) is a Actinobacteria Cytochrome P450 enzyme originally from Streptomyces rapamycinicus, which catalyzes the oxidation reaction of C27 of pre-rapamycin in the biosynthesis pathway of the macrolide antibiotic rapamycin.

1, Biosynthesis of glyceollins I, II and III in soybean. Stephen W. Banks and Paul M. Dewick, Phytochemistry, Volume 22, Issue 12, 1983, pp. 2729-2733, It has an antiestrogenic effect.Antiestrogenic glyceollins suppress human breast and ovarian carcinoma tumorigenesis.

Mespirenone is also a potent and specific enzyme inhibitor of 18-hydroxylase and thus of mineralocorticoid biosynthesis. The drug was under development by Schering (now Bayer Schering Pharma) and reached phase II clinical trials but was discontinued in 1989.

Genes for Xanthan gum biosynthesis comprise the gum operon (gumB-gymM) coding for 12 enzymes. Xanthan production by Xanthomonas spp. that thrive in vascular plant systems might block the water flow of the plant and as a result cause wilting.

Spermine biosynthesis in animals starts with decarboxylation of ornithine by the enzyme Ornithine decarboxylase in the presence of PLP. This decarboxylation gives putrescine. Thereafter the enzyme spermidine synthase effects two N-alkylation by decarboxy-S-Adenosyl methionine. The intermediate is spermidine.

This stands in contrast to the 1'-4 linkages that are much more common in isoprene biosynthesis than 4-4' linkages. The reaction mechanism of SQS requires a divalent cation, often Mg2+, to facilitate binding of the pyrophosphate groups on FPP.

In fact, because of similarities in the pathways for biosynthesis of staphyloxanthin and human cholesterol, a drug developed in the context of cholesterol-lowering therapy was shown to block S. aureus pigmentation and disease progression in a mouse infection model.

Thiostrepton was discovered by Donovick et al. who described its antibacterial properties in 1955. Dorothy Crowfoot Hodgkin solved the structure of thiostrepton in 1970. Early in 1978, Bycroft and Gowland proposed the biosynthesis of thiostrepton, which was still unclear until 2009.

In plants, sanguinarine biosynthesis begins with 4-hydroxyphenyl-acetaldehyde and dopamine. These two compounds are combined to form norcoclaurine. Next, methyl groups are added to form N-methylcoclaurine. The enzyme CYP80B1 subsequently adds a hydroxyl group, forming 3'-hydroxy-N-methylcoclaurine.

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.

It is possible to produce the hormone industrially using microorganisms.Camara, M. C. et al (2015) General Aspects and Applications of Gibberelins and Gibberellic Acid in Plants. In: Hardy, J.. (Org.). Gibberellins and Gibberellic Acid: Biosynthesis, Regulation and Physiological Effects. 1ed.

Bifonazole has a dual mode of action. It inhibits fungal ergosterol biosynthesis at two points, via transformation of 24-methylendihydrolanosterol to desmethylsterol, together with inhibition of HMG-CoA. This enables fungicidal properties against dermatophytes and distinguishes bifonazole from other antifungal drugs.

Substituted pteridines are intermediates in the biosynthesis of dihydrofolic acid in many microorganisms.Voet, D.; Voet, J.G. (2004). Biochemistry (3rd ed.). John Wiley & Sons. The enzyme dihydropteroate synthetase converts pteridine and 4-aminobenzoic acid to dihydrofolic acid in the presence of glutamate.

This gene encodes a bifunctional enzyme that is involved in the biosynthesis of sphingolipids in human skin and in other phytosphingolipid-containing tissues. This enzyme can act as a sphingolipid delta(4)-desaturase, and also as a sphingolipid C4-hydroxylase.

17β-Hydroxysteroid dehydrogenase III deficiency is a rare autosomal recessive disorder of sexual development, or intersex condition, affecting testosterone biosynthesis by 17β-hydroxysteroid dehydrogenase III (17β-HSD III), which can produce impaired virilization (historically termed male pseudohermaphroditism) of genetically male infants.

The enzyme O-GlcNAcase is involved in removal of N-acetylglucosamine groups from serine and threonine residues in the cytoplasm and nucleus of the cell. The glycoside hydrolases are involved in the biosynthesis and degradation of glycogen in the body.

Its genome does not code for any secondary metabolite synthesis pathways such as antibiotic biosynthesis, and no known xenobiotic degradation pathways are encoded. The absence of these self-defense mechanisms may help explain why M. flagellatus has no pathogenic qualities.

Desmosterolosis is a defect in cholesterol biosynthesis. It results in an accumulation of desmosterol and a variety of associated symptoms. Only two cases have been reported as of 2007. The condition is due to inactivating mutations in 24-dehydrocholesterol reductase.

15α-Hydroxydehydroepiandrosterone, abbreviated as 15α-hydroxy-DHEA or 15α-OH- DHEA, is an endogenous metabolite of dehydroepiandrosterone (DHEA). Both 15α-OH-DHEA and its 3β-sulfate ester, 15α-OH-DHEA-S, are intermediates in the biosynthesis of estetrol from dehydroepiandrosterone (DHEA).

Nervonic acid is an important component in myelin biosynthesis in the central and peripheral nervous system, and has been proposed to enhance human brain function. To aid this research its 1.51 Gigabase genome has been sequenced by researchers in China.

Lantibiotics show substantial specificity for some components (e.g., lipid II) of bacterial cell membranes especially of Gram- positive bacteria. Type A lantibiotics kill rapidly by pore formation, type B lantibiotics inhibit peptidoglycan biosynthesis. They are active in very low concentrations.

ATP is continually reformed from lower-energy species ADP and AMP. The biosynthesis of ATP is achieved throughout processes such as substrate-level phosphorylation, oxidative phosphorylation, and photophosphorylation, all of which facilitate the addition of a phosphate group to ADP.

Osbourn was born in Bingley, West Yorkshire and attended Bingley Grammar School. She is married to John Richer, Professor of Physics at the Cavendish Laboratory, Cambridge. She is sister to Professor Anne Osbourn FRS who investigates plant natural product biosynthesis.

Some Gram-positive bacteria also encode a soluble diacylglycerol kinase capable of reintroducing DAG into the phospholipid biosynthesis pathway. DAG accumulates in Gram- positive bacteria as a result of the transfer of glycerol-1-phosphate moieties from phosphatidylglycerol to lipotechoic acid.

It is synthesized via the phenylpropanoid biochemical pathway. Esters of p-coumaryl alcohol and fatty acids are the basis of epicuticular waxes covering the surfaces of apples. p-Coumaryl alcohol is an intermediate in biosynthesis of chavicol, stilbenoids, and coumarin.

Since it was reported that melatonin is a competitive inhibitor of AANAT, this neurotransmitter seems to exert an autoregulatory control on its own biosynthesis. Thus, loose structural analogues of the indolamine hormone were evaluated on AANAT, and moderate inhibitors were discovered.

Recently, γ-butyrobetaine hydroxylase, an enzyme that is involved in the human carnitine biosynthesis pathway, was found to catalyze a C-C bond formation reaction in a fashion analogous to a Stevens type rearrangement. The substrate for the reaction is meldonium.

Picimbon JF. Biochemistry and evolution of CSP and OBP proteins. In: Blomquist GJ, Vogt RG, editors. Insect Pheromone Biochemistry and Molecular Biology, The Biosynthesis and Detection of Pheromones and Plant Volatiles. Elsevier Academic Press, London, San Diego. 2003; 539-566. 5\.

Another unconventional function of complex II is seen in the malaria parasite Plasmodium falciparum. Here, the reversed action of complex II as an oxidase is important in regenerating ubiquinol, which the parasite uses in an unusual form of pyrimidine biosynthesis.

Homoaconitatic acid (homoaconitate) is related to aconitic acid but with one extra carbon. It is part of the α-aminoadipate pathway for lysine biosynthesis, where it is made from homocitrate by homoaconitase. It is converted to homoisocitrate by homoisocitrate dehydrogenase.

In fact, because of similarities in the pathways for biosynthesis of staphyloxanthin and human cholesterol, a drug developed in the context of cholesterol-lowering therapy was shown to block S. aureus pigmentation and disease progression in a mouse infection model.

However, hypomethioninemia remains an inconsistent symptom. Decreased MeCbl alongside normal cobalamin uptake is suggestive of decreased intracellular methionine biosynthesis. Occurring mainly in childhood, 15 pathogenic mutations can be associated with CblE type homocystinuria. Additionally, vascular abnormalities are associated with this defect.

Archaeoglobus profundus is a sulphate-reducing archaea. Archaeoglobus can be found in high-temperature oil fields where it may contribute to oil field souring. A. profundus grows lithotrophically, and while it needs acetate and CO2 for biosynthesis it is heterotrophic.

Sepiapterin reductase (7,8-dihydrobiopterin:NADP+ oxidoreductase; EC 1.1.1.153) catalyzes the NADPH-dependent reduction of various carbonyl substances, including derivatives of pteridines, and belongs to a group of enzymes called aldo-keto reductases. SPR plays an important role in the biosynthesis of tetrahydrobiopterin.

Edifenphos (O-ethyl-S,S-diphenyldithiophosphate, EDDP) is a systemic fungicide that inhibits phosphatidylcholine biosynthesis. It was introduced in 1966 by Bayer to combat blast fungus and Pellicularia sasakii in rice cultivation. It was never authorized for use in the EU.

Salutaridinol levels are indicative of the flux through the morphine biosynthesis pathway and the efficacy of both salutaridine: NADPH 7-oxidoreductase and salutaridinol 7-O-acetyltransferase.Fossati, Elena, et al. "Synthesis of morphinan alkaloids in Saccharomyces cerevisiae." PLoS ONE 10.4 (2015): e0124459.

Biosynthesis of Radicicol has been best studied in Pochonia chlamydosporia, in which the majority of the core structure is produced in vivo through iterative type I polyketide synthases. This structure produced is the earliest intermediate in the radicicol biosynthesis, monocillin II. This intermediate is transformed to radicicol through halogenation and epoxide formation performed by RadH and RadP respectively. These enzymes are coded by the genes Rdc2 and Rdc4 in the pathway, and removing either of these results in a product that has the monocillin II core, but does not have either the epoxide or halogen added. Proposed biosynthetic pathway of Radicicol.

Arginine, also known as -arginine (symbol Arg or R), is an α-amino acid that is used in the biosynthesis of proteins. It contains an α-amino group, an α-carboxylic acid group, and a side chain consisting of a 3-carbon aliphatic straight chain ending in a guanidino group. At physiological pH, the carboxylic acid is deprotonated (−COO−), the amino group is protonated (−NH3+), and the guanidino group is also protonated to give the guanidinium form (-C-(NH2)2+), making arginine a charged, aliphatic amino acid. It is the precursor for the biosynthesis of nitric oxide.

The drug acts by inhibiting 24-dehydrocholesterol reductase, which catalyzes the final step of cholesterol biosynthesis, the conversion of desmosterol into cholesterol. This results in tissue accumulation of desmosterol, which in turn is responsible for the side effects of triparanol. Unlike statins, triparanol does not inhibit HMG-CoA reductase, the rate-limiting enzyme in cholesterol biosynthesis, and in contrast to triparanol, statins can significantly lower cholesterol levels without resulting in accumulation of intermediates like desmosterol. The developmental code name of triparanol, MER/29, became so well known that it became the registered trade name of the drug.

Due to the commercial value of carotenoids, their biosynthesis has been studied extensively in both natural producers, and non-natural (heterologous) systems such as the bacteria Escherichia coli and yeast Saccharomyces cerevisiae. Canthanaxanthin biosynthesis proceeds from beta-carotene via the action of a single protein, known as a beta-carotene ketolase, that is able to add a carbonyl group to carbon 4 and 4' of the beta carotene molecule. Although functionally identical, several distinct beta-carotene ketolase proteins are known. That is to say they differ from an evolutionary perspective in their primary amino acid/protein sequence.

Aconitine is biosynthesized by the monkshood plant via the terpenoid biosynthesis pathway (MEP chloroplast pathway). Approximately 700 naturally occurring C19-diterpenoid alkaloids have been isolated and identified, but the biosynthesis of only a few of these alkaloids are well understood. Likewise, only a few alkaloids of the aconitine family have been synthesized in the laboratory. In particular, despite over one hundred years having elapsed since its isolation, the prototypical member of its family of norditerpenoid alkaloids, aconitine itself, represents a rare example of a well-known natural product that has yet to succumb to efforts towards its total synthesis.

The pathway o-succinylbenzoate CoA ligase belongs to is called 1, 4-dihydroxy-2-napthoate biosynthesis I. Other organisms that contain this pathway are eukaryotic bacteria such as Bacillus anthracis. Organisms that contain a pathway similar to this include Arabidopsis thaliana (gene AAE14), Mycobacterium phlei, and Synechocystis sp. (gene PCC 6803). The reason for the difference in pathways is due to the varying functions of Vitamin K. Eukaryotic bacteria use vitamin K II while other organisms use vitamin K I. Other pathways that include o-succinylbenzoate CoA ligase include 1, 4-diydroxy-2-naphthoate biosynthesis II (i.e.

Because of the toxicity, the interest in citrinin decreased, but there still was a lot of research. In 1948 the chemical structure was solved by W.B. Whalley and coworkers. Citrinin is a natural compound and it was first isolated from Penicillium citrinum, but it is also produced by other Penicillium species, the Monascus species and the Aspergillus species, which are all fungi. During the 1950s W.B. Whalley and A.J. Birch and others identified citrinin as a polyketide and investigated its biosynthesis using radioisotopes. During the 1980s and 1990s J. Staunton, U. Sankawa and others also investigated its biosynthesis using stable isotopes and NMR.

Diagram showing the schematic synthesis of avermectins The gene cluster for biosynthesis of avermectin from S. avermitilis has been sequenced. The avermectin biosynthesis gene cluster encodes enzymes responsible for four steps of avermectin production: 1) production of the avermectin aglycon by polyketide synthases, 2) modification of the aglycon, 3) synthesis of modified sugars, and 4) glycosylation of the modified avermectin aglycon. This gene cluster can produce eight avermectins which have minor structural differences. Organization of the avermectin polyketide synthase The avermectin initial aglycon is synthesized by the polyketide synthase activity of four proteins (AVES 1, AVES 2, AVES 3, and AVES 4).

In the fifth step, a P450 enzyme closes the 5 + 7 guaianolide structure. The ring closing is important, because it will proceed via 1,10 - epoxidation in order to retain the 4,5 - double bond needed in thapsigargin. It is not known whether the secondary modifications to the guaianolide occur before, or after the formation of thapsigargin, but will need to be considered when elucidating the true biosynthesis. It should also be noted, that several of these enzymes are P450s, therefore oxygen and NADPH are likely crucial to this biosynthesis as well as other cofactors such as Mg2+ and Mn2+ may be needed.

These observations implied that the aporphine prestephanine (10) would be an obligatory intermediate in the biosynthesis, which would involve the intermediacy of the proaporphines orientalinone (8) and orientalinol (9) via the known intramolecular dienone-dienol-phenol sequence for the transformation of benzyltetrahydroisoquinolines to aporphines. A potential role for CYP80G2, a cytochrome P450 that has been demonstrated to catalyze the intramolecular C-C phenol coupling of several benzyltetrahydroisoquinolines, in this orientaline (7) to prestephanine (10) transformation has been suggested. (±)‑[aryl‑3H]‑Prestephanine was incorporated into AA-I confirming its intermediacy in the biosynthesis; and also (±)‑[aryl‑3H]‑stephanine was incorporated into AA-I.

The transcribed protein is the first and rate-limiting enzyme in tetrahydrobiopterin (THB, BH4) biosynthesis, catalyzing the conversion of GTP into 7,8-DHNP-3'-TP. THB is an essential cofactor required by the aromatic amino acid hydroxylase (AAAH) and nitric oxide synthase (NOS) enzymes in the biosynthesis of the monoamine neurotransmitters serotonin (5-hydroxytryptamine (5-HT)), melatonin, dopamine, norepinephrine (noradrenaline), and epinephrine (adrenaline), and nitric oxide (NO), respectively. GTPCH (GCH1) and tetrahydrobiopterin were found to protect against cell death by ferroptosis. Tetrahydrobiopterin (BH4) acts as a potent, diffusable antioxidant that resists oxidative stress and enables cancer cell survival.

Gelsemine's biosynthesis, as of 1998, is thought to proceed from 3α(S)-strictosidine (isovincoside), the common precursor for essentially all monoterpenoid indole alkaloids—itself deriving directly from mevalonic acid-derived secologanin and tryptamine. From strictosidine, the biosynthesis proceeds through five intermediates—including koumicine (akkuammidine), koumidine, vobasindiol, anhydrovobasindiol, and gelsenidine (humantienine-type). The related alkaloids koumine and gelsemicine also derive from this pathway (koumine from anhydrovobasindiol via oxidation and rearrangement, and gelsemicine from gelsemine itself, via aromatic oxidation and O-methylation). For the chemical synthesis (natural product synthesis, studies and total synthesis), see the separate section below.

Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase is an enzyme that in humans is encoded by the GNE gene. The bifunctional enzyme, UDP-N-acetylglucosamine 2-epimerase (UDP-GlcNAc 2-epimerase/N-acetylmannosamine kinase) regulates and initiates biosynthesis of N-acetylneuraminic acid (NeuAc), a precursor of sialic acids. UDP-GlcNAc 2-epimerase activity is rate-limiting for the biosynthesis of sialic acid and is required for sialylation in hematopoietic cells. The activity of the enzyme can be controlled at the transcriptional level and can affect the sialylation and function of specific cell surface molecules expressed on B cells and myeloid cells.

Biosynthesis of choline in plants In plants, the first step in de novo biosynthesis of choline is the decarboxylation of serine into ethanolamine, which is catalyzed by a serine decarboxylase. The synthesis of choline from ethanolamine may take place in three parallel pathways, where three consecutive N-methylation steps catalyzed by a methyl transferase are carried out on either the free-base, phospho- bases, or phosphatidyl-bases. The source of the methyl group is S-adenosyl-- methionine and S-adenosyl--homocysteine is generated as a side product. Main pathways of choline (Chol) metabolism, synthesis and excretion.

This enzyme catalyses the first step in the biosynthesis of histidine in bacteria, fungi and plants. It is a member of the larger phosphoribosyltransferase superfamily of enzymes which catalyse the condensation of 5-phospho-alpha-D-ribose 1-diphosphate with nitrogenous bases in the presence of divalent metal ions. Histidine biosynthesis is an energetically expensive process and ATP phosphoribosyltransferase activity is subject to control at several levels. Transcriptional regulation is based primarily on nutrient conditions and determines the amount of enzyme present in the cell, while feedback inhibition rapidly modulates activity in response to cellular conditions.

Studies determining the Michaelis-Menten kinetic parameters for these enzymes revealed that UCK2 had a four to sixfold higher binding affinity, faster maximal rates, and greater efficiencies for uridine and cytidine substrates than did UCK1. Both uridine-cytidine kinases, however, plays a crucial role in the biosynthesis of the pyrimidine nucleotides that compose RNA and DNA. Pyrimidine biosynthesis can occur through two pathways: de novo synthesis, which relies on L-glutamine as the pathway precursor, and salvage, which recycles cellular uridine and cytidine. UCK2 catalyzes the first step of pyrimidine salvage, and is the rate limiting enzyme in the pathway.

Sachs H, Takabatake Y. Evidence for a Precursor in Vasopressin Biosynthesis. Endocrinology. 1964; 75943-8. Sachs' hypothesis preceded the discovery of proinsulin by 3 years, and his research laid the foundation for understanding the biosynthesis of all brain peptides and many proteins, which are major constituents involved in brain and neuroendocrine functions. Sachs showed that vasopressin was first synthesized as a prohormone in specialized nerve cells (called neurosecretory cells) in the hypothalamus and was then transported to the nerve terminals in the posterior pituitary where the vasopressin peptide was completely processed during axonal transport in secretory granules and ultimately secreted into the blood.

Mary Ellen Jones (December 25, 1922 – August 23, 1996) was an American biochemist.New York Times:Mary Ellen Jones, 73, Crucial Researcher on DNA, By HENRY FOUNTAIN, September 7, 1996 She was notable for discovery of carbamoyl phosphate, a chemical substance that is key to the biosynthesis of arginine and urea, and for the biosynthesis of pyrimidine nucleotides. Jones became the first woman to hold a chair at the University of North Carolina at Chapel Hill, and the first woman to become a department chair at the medical school. She was a member of the National Academy of Sciences.

Mutants in signaling and biosynthesis of the traditional plant disease resistance hormones salicylic acid (SA), jasmonic acid (JA) and ethylene (ET) do not disrupt A. thaliana resistance to L. maculans. On the other hand, are mutants disrupted in abscisic acid (ABA) biosynthesis or signaling susceptible to L. maculans. Interestingly, however, is SA and JA contributing to tolerance in a compatible interaction where RLM1 and camalexin-mediated resistances have been mutated, and a quadruple mutant (where RLM1, camalexin, JA and SA-dependent responses are blocked) is hyper- susceptible. In contrast, ET appears to be detrimental for disease resistance.

Both, abscisic acid (ABA) and strigolactones have a common group of enzymes that carried out the synthesis of the two compounds, previously it had been demonstrated the existence of a correlation of the two biosynthesis pathways, and it has been supported by different studies. The ABA biosynthesis relies in a set of enzymes, called 9-cis-epoxycarotenoid dyoxygenase (NCED). But, mutants plants that were defective in the production of the NCED enzymes, not just presented low levels of ABA, rather they also present low levels of strigolactones, specifically in the roots extracts where this hormone is mostly synthesized, this finding provided the basis for the existence of a common enzymatic machinery, Other experiments that consist in blocking the NCED enzymes and using mutants unable to detect ABA changes, were used to support this theory. So far there is a clear correlation of both synthesis that is related to the used of NCED enzymes in both biosynthesis, but the exact mechanism in which they are connected remains unclear.

BC200 RNA Biosynthesis The biosynthesis of BC200 RNA occurs at the cell body of a neuron and requires upstream promoter elements, downstream internal promoter elements (intragenic A and B boxes), at least two transcription factor binding sites, a TATA-like sequence, TATA-box binding protein (TBP), and RNA polymerase III. There is a deletion of sequences between -100 to -1 in the DNA that blocks transcription activity, revealing that the transcription complex must interact with this 100-bp sequence of the upstream region for proper synthesis of BC200 RNA. The TATA-box binding protein (TBP) binds here, and when inhibited, BC200 RNA levels decrease, indicating that the 100 base pair region and TBP are critical players in the biosynthesis of BC200 RNA. In addition to upstream elements, there is an upstream TATGAAA sequence (similar to TATA box sequence) at positions -28 to -22 which, when deleted, compromises transcription, revealing this TATA-like sequence as another critical player in the synthesis of BC200 RNA.

PBAN aids in pheromone production in females and pheromone responsiveness in males.Duportets, Line, et al. "The Pheromone Biosynthesis Activating Neuropeptide (PBAN) of the Black Cutworm Moth, Agrotis ipsilon: Immunohistochemistry, Molecular Characterization and Bioassay of Its Peptide Sequence." Insect Biochemistry and Molecular Biology, vol.

Plants employ additional routes to spermine. In one pathway L-glutamine is the precursor to L-ornithine, after which the synthesis of spermine from L-ornithine follows the same pathway as in animals. Biosynthesis of spermidine and spermine from putrescine. Ado = 5'-adenosyl.

Isoleucine is synthesized from pyruvate employing leucine biosynthesis enzymes in other organisms such as bacteria. It is encoded by the codons AUU, AUC, and AUA. Inability to break down isoleucine, along with other amino acids, is associated with maple syrup urine disease.

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.

The triazole antifungal drugs include fluconazole, isavuconazole, itraconazole, voriconazole, pramiconazole, ravuconazole, and posaconazole. The triazole plant protection fungicides include epoxiconazole, , propiconazole, prothioconazole, metconazole, cyproconazole, tebuconazole, flusilazole and paclobutrazol. Paclobutrazol, uniconazole, , and triadimefon are used as plant growth retardants. Brassinazole is Brassinosteroid Biosynthesis Inhibitor.

This enzyme participates in glycerophospholipid metabolism. This is a family of proteins that acts as a mitochondrial phosphatase in cardiolipin biosynthesis. Cardiolipin is a unique dimeric phosphoglycerolipid predominantly present in mitochondrial membranes. The inverted phosphatase motif includes the highly conserved DKD triad.

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.

In angiosperms, this is done at the step of aminolevulinic acid (ALA), one of the intermediate compounds in the biosynthesis pathway. Plants that are fed by ALA accumulate high and toxic levels of protochlorophyllide; so do the mutants with a damaged regulatory system.

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

Embryo and root development also require WRKY transcription factors.Grunewald, De Smet, Lewis, Löfke, Jansen, et al. (2012) Transcription factor WRKY23 assists auxin distribution patterns during Arabidopsis root development through local control on flavonol biosynthesis. Proceedings of the National Academy of Sciences. 109(5).

Two equivalents of 10-CHO-THF are required in purine biosynthesis through the pentose phosphate pathway, where 10-CHO-THF is a substrate for phosphoribosylaminoimidazolecarboxamide formyltransferase. 10-CHO-THF is required for the formylation of methionyl-tRNA formyltransferase to give fMet- tRNA.

They concluded that pathways of which the genes are clusters across many species are rare. They found seven universally clustered pathways: glycolysis, aminoacyl-tRNA biosynthesis, ATP synthase, DNA polymerase, hexachlorocyclohexane degradation, cyanoamino acid metabolism, and photosynthesis (ATP synthesis in non plant species).

Other names in common use include naringenin 3-hydroxylase, flavanone 3-hydroxylase, flavanone 3beta-hydroxylase, flavanone synthase I, (2S)-flavanone 3-hydroxylase, and naringenin,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating). This enzyme participates in flavonoid biosynthesis. It has 2 cofactors: iron, and Ascorbate.

Etamsylate (sometimes spelled ethamsylate) is an antihemorrhagic agent which is believed to work by increasing resistance in the endothelium of capillaries and promoting platelet adhesion. It also inhibits biosynthesis and action of those prostaglandins which cause platelet disaggregation, vasodilation and increased capillary permeability.

Peroxides play important roles in biology. Hundreds of peroxides and hydroperoxides are known, being derived from fatty acids, steroids, and terpenes. Derived from fatty acids are a number of 1,2-dioxenes. The biosynthesis prostaglandins proceeds via an endoperoxide, a class of bicyclic peroxides.

Allylglycine is a glycine derivative. It is an inhibitor of glutamate decarboxylase. Inhibition of glutamate decarboxylase blocks GABA biosynthesis, leading to lower levels of the neurotransmitter. Allylglycine is known to induce seizures in animals studies, presumably due to this GDC-inhibiting activity.

French Dystonia, N. (2009). Exhaustive analysis of BH4 and dopamine biosynthesis genes in patients with Dopa-responsive dystonia. Brain, 132, 1753-1763. The disruption of dopamine and serotonin production leads to the visible symptoms present in patients suffering from sepiapterin reductase deficiency.

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.

Glutamate racemase (MurI) serves two distinct metabolic functions: primarily, it is a critical enzyme in cell wall biosynthesis, but also plays a role in gyrase inhibition. The ability of glutamate racemase and other proteins to serve two distinct functions is known as "moonlighting".

Episterol is a sterol involved in the biosynthesis of steroids. Episterol is converted from 24-methylenelophenol. Episterol is converted to 5-dehydroepisterol by ERG3, the C-5 sterol desaturase in the yeast. Episterol is also known to be a precursor to ergosterol.

806 requiring energy rendered from ATP. Malonyl-CoA is utilised in fatty acid biosynthesis by the enzyme malonyl coenzyme A:acyl carrier protein transacylase (MCAT). MCAT serves to transfer malonate from malonyl-CoA to the terminal thiol of holo-acyl carrier protein (ACP).

Lyngbyatoxin Biosynthesis reported by Gerwick et al. and Neilan et al. Lyngbyatoxin is a terpenoid indole alkaloid that belongs to the class of non-ribosomal peptides (NRP). Lyngbyatoxin contains a nucleophilic indole ring that takes part in the activation of protein kinases.

Glutamate-1-semialdehyde is a molecule formed from by the reduction of tRNA bound glutamate, catalyzed by glutamyl-tRNA reductase. It is isomerized by glutamate-1-semialdehyde 2,1-aminomutase to give aminolevulinic acid in the biosynthesis of porphyrins, including heme and chlorophyll.

Aspartyl-tRNA synthetase, cytoplasmic is an enzyme that in humans is encoded by the DARS gene. Aspartyl-tRNA synthetase (DARS) is part of a multienzyme complex of aminoacyl-tRNA synthetases. Aspartyl-tRNA synthetase charges its cognate tRNA with aspartate during protein biosynthesis.

Using FTR, reduced Ferredoxin then reduces Thioredoxin. Thioredoxin, through thiol/disulfide exchange, then activates carbohydrate synthesis enzymes such as chloroplast fructose-1,6-bisphosphatase, Sedoheptulose-bisphosphatase, and phosphoribulokinase. As a result, light uses FTR to activate carbohydrate biosynthesis. In the dark, Ferredoxin remains oxidized.

Lathosterol oxidase is an enzyme that in humans is encoded by the SC5DL gene. This gene encodes an enzyme of cholesterol biosynthesis. The encoded protein catalyzes the conversion of lathosterol into 7-dehydrocholesterol. Mutations in this gene have been associated with lathosterolosis.

Cephalosporin C is the product of the biosynthesis pathway of third generation cephalosporins. This is done by exchanging the acetyl CoA into DAC. To achieve cephalosporin C as the end product, there are 6 genes reported to be in control of the pathway.

For peptides three main types of methods are used, namely chemical synthesis, extraction from natural substances, and biosynthesis. Chemical synthesis is used for smaller peptides made of up to 30–40 amino acids. One distinguishes between “liquid phase” and “solid phase” synthesis.

8,180 base pairs upstream of RUFY2 is the protein-coding gene for phenazine biosynthesis-like protein domain containing (PBLD). While 6,770 base pairs downstream from RUFY2 is a DNA2 conserved helicase/nuclease involved in the maintenance of mitochondrial and nuclear DNA stability.

Sirohydrochlorin is a tetrapyrrole macrocyclic metabolic intermediate in the biosynthesis of sirohaem, the iron-containing prosthetic group in sulfite reductase enzymes. It is also the biosynthetic precursor to cofactor F430, an enzyme which catalyzes the release of methane in the final step of methanogenesis.

This gene encodes a membrane- associated enzyme located at a branch point in the mevalonate pathway. The encoded protein is the first specific enzyme in cholesterol biosynthesis, catalyzing the dimerization of two molecules of farnesyl diphosphate in a two- step reaction to form squalene.

Some evidence suggests that the enzyme is a soluble, non-membrane bound protein in the few prokaryotes that produce it. Due to the enzyme's role in cholesterol biosynthesis, there is interest in lanosterol synthase inhibitors as potential cholesterol-reducing drugs, to complement existing statins.

Parasitic plants germinate and follow a concentration gradient of these compounds in the soil toward the host plants if close enough. These compounds are called strigolactones. Strigolactone stimulates ethylene biosynthesis in seeds causing them to germinate. There are a variety of chemical germination stimulants.

Methyltransferases are very common in the catecholamine synthesis and deactivation pathways. PNMT is also involved in the biosynthesis of N-methylated trace amines: it metabolizes phenethylamine into N-methylphenethylamine (a positional isomer of amphetamine), p-octopamine into synephrine, and p-tyramine into N-methyltyramine.

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.

Ectoine is synthesized in three successive enzymatic reactions starting from aspartic β-semialdehyde. The genes involved in the biosynthesis are called ectA, ectB and ectC, and they encode the enzymes L-2,4-diaminobutyric acid acetyltransferase, L-2,4-diaminobutyric acid transaminase and L-ectoine synthase, respectively.

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.

Increased amounts of methyl jasmonate in plant roots have shown to inhibit their growth.Wasternack, C. Jasmonates: An Update on Biosynthesis, Signal Transduction and Action in Plant Stress Response, Growth and Development. Annals of Botany (2007) 100(4):681-697. . Retrieved on 2010-10-27.

The encoded protein may play a role in regulating the availability of serum glycoproteins, oncogenesis, and differentiation. Its affinities for donors of acceptors are lower than that of MGAT4A so it is suggested that it is not the main contributor in N-glycan biosynthesis.

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.

Glucomannan is also a constituent of bacterial, plant and yeast cell wall with differences in the branches or glycosidic linkages in the linear structure.Elbein, A. D. (1969). Biosynthesis of a cell wall glucomannan in mung bean seedlings. Journal of Biological Chemistry, 244(6), 1608-1616.

The biosynthesis of cyanidin 3-O-glucoside in Escherichia coli was demonstrated by means of genetic engineering. In Arabidopsis thaliana, a glycosyltransferase, UGT79B1, is involved in the anthocyanin biosynthetic pathway. UGT79B1 protein converts cyanidin 3-O-glucoside to cyanidin 3-O-xylosyl(1→2)glucoside.

AdoMet is a methyl donor for transmethylation. It gives away its methyl group and is also the propylamino donor in polyamine biosynthesis. S-adenosylmethionine synthesis can be considered the rate-limiting step of the methionine cycle. As a methyl donor SAM allows DNA methylation.

Structurally CDKAL1 contains two iron (Fe) sulfur (S) clusters, therefore its function can be reduced by inhibiting Fe-S cluster biosynthesis. Enzymatically, CDKAL1 catalyzes methylthiolation of N6-threonylcarbamoyl adenosine 37 (t6A37) in cytosolic tRNA, which has been determined to stabilize anticodon-codon interactions during translation.

Biological precursors of most alkaloids are amino acids, such as ornithine, lysine, phenylalanine, tyrosine, tryptophan, histidine, aspartic acid, and anthranilic acid.Plemenkov, p. 253 Nicotinic acid can be synthesized from tryptophan or aspartic acid. Ways of alkaloid biosynthesis are too numerous and cannot be easily classified.

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.

The biosynthesis of the β-lactam ring of tabtoxin mirrors that of the clavams and carbapenems. The closure of the lactam ring in the other monobactams, such as sulfazecin and the nocardicins, may involve a third mechanism involving inversion of configuration at the β-carbon.

Although all commercially available DBU is produced synthetically, it can also be isolated from the sea sponge Niphates digitalis.Regalado, E.L. et al., Nat. Prod. Commun., 2010, 5, 1187- 1190 The biosynthesis of DBU has been proposed to begin with 1,6-hexanedial and 1,3-diaminopropane.

Then, in 1979, he discovered aminocylopropane-1-carboxylic acid (ACC) as an intermediate. His discovery of ACC-synthase opened the way to the understanding of the regulating process of ethylene biosynthesis. Yang died on February 12, 2007 in a Davis hospital from complications of pneumonia.

Functionally, the antiangiogenic activity of itraconazole has been shown to be linked to inhibition of glycosylation, VEGFR2 phosphorylation, trafficking, and cholesterol biosynthesis pathways. Evidence suggests the structural determinants for inhibition of hedgehog signaling by itraconazole are recognizably different from those associated with antiangiogenic activity.

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.

Steroidogenesis, including corticosteroid biosynthesis. The corticosteroids are synthesized from cholesterol within the adrenal cortex. Most steroidogenic reactions are catalysed by enzymes of the cytochrome P450 family. They are located within the mitochondria and require adrenodoxin as a cofactor (except 21-hydroxylase and 17α-hydroxylase).

Cholesterol can be made from acetyl-CoA through a multiple- step pathway known as isoprenoid pathway. Cholesterols are essential because they can be modified to form different hormones in the body such as progesterone. 70% of cholesterol biosynthesis occurs in the cytosol of liver cells.

To increase flux through the cycle, some of the PEP is converted to oxaloacetate by PEP carboxylase. Since the citric acid cycle intermediates provide a hub for metabolism, increasing flux is important for the biosynthesis of many molecules, such as for example amino acids.

Anabolism () is the set of metabolic pathways that construct molecules from smaller units. These reactions require energy, known also as an endergonic process. Anabolism is the building-up aspect of metabolism, whereas catabolism is the breaking-down aspect. Anabolism is usually synonymous with biosynthesis.

But in this case, the product is used in biosynthesis, e.g. for the production of cysteine. The latter process is called assimilatory sulfate reduction because the sulfate sulfur is assimilated.M. T. Madigan, J. M. Martinko, J. Parker “Brock Biology of Microorganisms” Prentice Hall, 1997. .

16α-Hydroxydehydroepiandrosterone (16α-hydroxy-DHEA or 16α-OH-DHEA) is an endogenous metabolite of dehydroepiandrosterone (DHEA). Both 16α-OH-DHEA and its 3β-sulfate ester, 16α-OH-DHEA-S, are intermediates in the biosynthesis of estriol from dehydroepiandrosterone (DHEA). 16α-OH-DHEA has estrogenic activity.

Proposed biosynthesis of the activated aza-β-tyrosine subunit. The 2-aza-β-tyrosine subunit of kedarcidin chromophore is altogether unknown in any other natural product; this lack of precedence frustrates any attempt at a priori identification of the genes responsible for synthesizing this structure.

The current consensus theory about the origin of Nε-trimethyllysine in mammals is that mammals utilise lysosomal or proteasomal degradation of proteins containing Nε-trimethyllysine residues as starting point for carnitine biosynthesis.Bremer, J. Biosynthesis of carnitine in vivo. Biochim. Biophys. Acta 1961, 48, 622–624.

The catalytic conversion of uridine triphosphate (UTP) to cytidine triphosphate (CTP) is accomplished by the enzyme cytidine-5-prime-triphosphate synthetase. This enzyme is important in the biosynthesis of phospholipids and nucleic acids, and plays a key role in cell growth, development, and tumorigenesis.

The activated substance inhibits ATP citrate lyase, which is involved in the liver's biosynthesis of cholesterol upstream of HMG-CoA reductase, the enzyme that is blocked by statins. The substance also activates AMP-activated protein kinase, but this effect is likely not relevant in humans.

The biosynthesis of vancosamine and epivancosamine are identical, except in the last step.Chen, H., Thomas, M. G., Hubbard, B. K., Losey, H. C., Walsh, C. T., Burkart, M. D. "Deoxysugars in glycopeptide antibiotics: Enzymatic synthesis of TDP-L-epivancosamine in chloroeremomycin biosynthesis." PNAS, 2000, 97 (22), 11942-11947 The enzymes that catalyze the reactions have been designated EvaA-E. A molecule of TDP-D-glucose enters the pathway via conversion to molecule 1 by an oxidoreductase enzyme and then a dehydratase enzyme. In the next step, EvaA dehydrates molecule 1 by deprotonating at 3-C to form and enolate, which then eliminates 2-OH, to form molecule 2.

Notably, these elevated values disappear during the Cambrian, and the ratio of 24-isopropyl cholestane to 24-n-propyl cholestane is used an age-specific proxy for the Proterozoic-Phanerozoic transition. Recent research in molecular clocks has argued that the ability to produce 24-isopropyl cholesterol evolved independently in both the demosponge and algae. However, it appears that the biosynthesis evolved earlier in the sponges, during the Neoproterozoic, and that the ability to perform the biosynthesis was not present in algae until the Phanerozoic. If correct, these results would give scientists much more confidence in interpreting elevated levels of 24-isopropyl cholestane in ancient rocks as reflecting the presence of sponges.

Engaging in moderate-high intensity aerobic exercise such as running, swimming, and cycling increases BDNF biosynthesis through myokine signaling, resulting in up to a threefold increase in blood plasma and BDNF levels; exercise intensity is positively correlated with the magnitude of increased BDNF biosynthesis and expression. A meta-analysis of studies involving the effect of exercise on BDNF levels found that consistent exercise modestly increases resting BDNF levels as well. This has important implications for exercise as a mechanism to reduce stress since stress is closely linked with decreased levels of BDNF in the hippocampus. In fact, studies suggest that BDNF contributes to the anxiety-reducing effects of antidepressants.

In enzymology, a [heparan sulfate]-glucosamine 3-sulfotransferase 3 () is an enzyme that catalyzes the chemical reaction :3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine \rightleftharpoons adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate Thus, the two substrates of this enzyme are 3'-phosphoadenylyl sulfate and heparan sulfate-glucosamine, whereas its two products are adenosine 3',5'-bisphosphate and heparan sulfate- glucosamine 3-sulfate. This enzyme belongs to the family of transferases, specifically the sulfotransferases, which transfer sulfur-containing groups. The systematic name of this enzyme class is 3'-phosphoadenylyl- sulfate:[heparan sulfate]-glucosamine 3-sulfotransferase. This enzyme participates in heparan sulfate biosynthesis and glycan structures - biosynthesis 1.

The first information on the biosynthesis of the rifamycins came from studies using the stable isotope Carbon-13 and NMR spectroscopy to establish the origin of the carbon skeleton. These studies showed that the ansa chain was derived from acetate and propionate, in common with other polyketide antibiotics. The naphthalenic chromophore was shown to derive from a propionate unit coupled with a seven carbon amino moiety of unknown origin. The general scheme of biosynthesis starts with the uncommon starting unit, 3-amino-5-hydroxybenzoic acid (AHBA), via type I polyketide pathway (PKS I) in which chain extension is performed using 2 acetate and 8 propionate units.

The 5 methyl groups are added via S-adenosyl methionine (SAM) methylation, as opposed to incorporation of propionate (instead of acetate) to the growing compound during biosynthesis. The following internal cyclization proceeds through a Diels–Alder reaction catalyzed by an unknown enzyme. The origin of the subsequent oxidations at positions 1, 2 and 8 have yet to be characterized, but they have been shown not to originate from acetate. It has been theorized that cytochrome P-450 is responsible for the oxidation at these three positions since its inhibition produces probetaenone 1, the non-oxidized form of betaenone B. Biosynthesis of betaenone B as proposed by Oikawa et al.

Alan Battersby realised that these techniques could be used to study alkaloid biosynthesis and that it was timely to do so because simple one-carbon precursors had become commercially available. By using radiolabelled starting materials incorporating tritium or, especially, 14C to follow intermediates on the pathway, he determined the sequence in which the multiple alkaloids found together in a given organism were formed. For example, the biosynthesis of morphine was shown to proceed from L-tyrosine via reticuline, salutaridine, thebaine, codeinone and codeine. The Battersby group worked on many other alkaloids, for example colchicine, (from the autumn crocus Colchicum autumnale) which is used to treat gout.

A schematic outline of stepwise synthesis of NCS Chromophore The biosynthesis of neocarzinostatin takes place through a convergence of the activities of a gene cluster, which includes two separate iterative type I polyketide synthase (PKS) and deoxy sugar biosynthetic pathways. The first type I PKS gene, NcsE, codes for the enediyne moiety. The second type I PKS gene, NcsB, codes for the naphthoic acid moiety. Additionally, a cluster of NcsC genes are responsible for coding enzymes for the synthesis of the deoxyamino sugar moiety of NCS chromophore. The biosynthesis can be divided into three preliminary steps with a final convergence of the three moieties: 1\.

Biosynthetic pathway Biosynthesis of mevastatin is primarily accomplished via a type 1 PKS pathway it proceeds in the PKS pathway as seen in figure 1 until it reaches a hexaketide state where it undergoes a Diels- Alder cyclization. After cyclization it continues via the PKS pathway to a nonaketide after which it is released and undergoes oxidation and dehydration. It is presumed that the oxidations are preformed by a polypeptide that is similar to cytochrome p450 monooxygenase, which is encoded by mlcC within the mevastatin gene. Lastly the biosynthesis is completed by the PKS facilitating the addition of a diketide sidechain and a methylation by SAM.

This was thought to result from the inability to produce critical defensive mechanisms including increased PR gene expression. Other studies conducted by injecting tobacco plants and Arabidopsis with salicylic acid resulted in higher resistance of infection by the alfalfa and tobacco mosaic viruses, indicating a role for SA biosynthesis in reducing viral replication. Additionally, studies performed using Arabidopsis with mutated jasmonic acid biosynthesis pathways have shown JA mutants to be at an increased risk of infection by soil pathogens. Along with SA and JA, other defensive chemicals have been implicated in plant viral pathogen defenses including abscisic acid (ABA), gibberellic acid (GA), auxin, and peptide hormones.

The UV-B photoreceptor, UV Resistance Locus8 (UVR8) detects UV-B rays and elicits photomorphogenic responses. These response are important for initiating hypocotyl elongation, leaf expansion, biosynthesis of flavonoids and many other important processes that affect the root-shoot system. Exposure to UV-B rays can be damaging to DNA inside of the plant cells, however, UVR8 induces genes required to acclimate plants to UV-B radiation, these genes are responsible for many biosynthesis pathways that involve protection from UV damage, oxidative stress, and photorepair of DNA damage. There is still much to be discovered about the mechanisms involved in UV-B radiation and UVR8.

In enzymology, a β-ketoacyl-[acyl-carrier-protein] synthase III () is an enzyme that catalyzes the chemical reaction :acetyl-CoA + malonyl-[acyl carrier protein] \rightleftharpoons acetoacetyl-[acyl carrier protein] \+ CoA + CO2 Thus, the two substrates of this enzyme are acetyl-CoA and malonyl-[acyl-carrier-protein], whereas its 3 products are acetoacetyl-[acyl- carrier-protein], CoA, and CO2. This enzyme belongs to the family of transferases, to be specific those acyltransferases transferring groups other than aminoacyl groups. This enzyme participates in fatty acid biosynthesis. β-Ketoacyl-acyl-carrier-protein synthase III is involved in the dissociated (or type II) fatty-acid biosynthesis system that occurs in plants and bacteria.

These enzymes clearly demonstrate regulated production of ROS as their sole function. Genetic analyses have implicated NOX/DUOX derived ROS in biological roles and pathological conditions including hypertension (NOX1), innate immunity (NOX2/DUOX), otoconia formation in the inner ear (NOX3) and thyroid hormone biosynthesis (DUOX1/2). It has been suggested that DUOX2 is the isoform to generate H2O2 utilized by thyroid peroxidase (TPO) for the biosynthesis of thyroid hormones, supported by the discovery of congenital hypothyroidism resultant from an inactivating mutation in the DUOX2 gene. The family currently has seven members including NOX1, NOX2 (formerly known as gp91phox), NOX3, NOX4, NOX5, DUOX1 and DUOX2.

These divergent enzymes differ from CHS in their preference for starter molecules, the number of acetyl additions (often through malonyl-CoA) and even in the mechanism of ring formation used to cyclize identical polyketide intermediates. The enzyme function of CHS and CHS-like enzymes function very similarly to fatty acid biosynthesis, but without the involvement of acyl-carrier proteins (ACP). Structural evidence suggests that these enzymes emerged by gain of function from ketoacyl synthase (KAS) III, an early stage enzyme of type II fatty acid biosynthesis. Although higher plant chalcone synthases have been extensively studied, little information is available on the enzymes from bryophytes (primitive plants).

Goss specialises in the biosynthesis of natural products at the chemical and genetic level. Goss joined the University of Cambridge in 2000 to study the chemistry and molecular biology of polyketide biosynthesis in the research group of Professors Jim Staunton (FRS) and Peter Leadlay (FRS). She held a one-year teaching fellowship at the School of Chemistry, University of Nottingham between 2002 and 2003 before obtaining a lectureship at the School of Biological and Chemical Science, University of Exeter in 2003. Between 2005 and 2010 Goss held a lectureship at the University of East Anglia before being promoted to senior lecturer in 2010 and then reader in organic chemistry in 2012.

Metabolically, (S)-canadine is derived from (S)-reticuline, a pivotal intermediate in the biosynthesis of numerous BIA structural subgroups, through three enzymatic steps: 1) Berberine bridge enzyme to (S)-scoulerine; 2) (S)-scoulerine 9-O-methyltransferase to (S)-tetrahydrocolumbamine; and 3) (S)-canadine synthase/CYP719A21 to (S)-canadine. (S)-Canadine is the immediate metabolic precursor of berberine, which is obtained through the action of the enzyme (S)-tetrahydroprotoberberine oxidase. It is also an intermediate in the complex biosynthesis of noscapine, which is likewise a benzylisoquinoline alkaloid, but of the phthalideisoquinoline structural subgroup. (S)-Canadine, berberine, palmatine, and hydrastine are the major alkaloids present in goldenseal.

The principal requirements are energy (lipids, lactose, and protein), biosynthesis of non-essential amino acids supplied by proteins (essential amino acids and amino groups), essential fatty acids, vitamins and inorganic elements, and water.Fox, P.F. Advanced Dairy Chemistry, Vol. 3: Lactose, Water, Salts and Vitamins. 2nd ed.

Katanosin antibiotics target the bacterial cell wall biosynthesis. They are highly potent against problematic Gram-positive hospital pathogens such as staphylococci and enterococci. Their promising biological activity attracted various biological and chemical research groups. Their in-vitro potency is comparable with the current “last defence” antibiotic vancomycin.

A study of the production of misakinolide revealed that it was attributed to the Theonella symbiont bacterium Candidatus Entotheonella via the discovery of a trans-AT polyketides synthase (PKS) biosynthesis gene cluster. This demonstrates that the true origin of swinholides is symbiotic bacteria that inhabit sponges.

Some of these genes are for wax biosynthesis, which is known to be involved in tolerance to abiotic stresses in pearl millet. ICRISAT is currently evaluating crop wild relatives and will introgress abiotic tolerant traits into cultivated genotypes and make them available for pearl millet improvement.

Chemical structure of vinclozolin, a dicarboximide fungicide Dicarboximide (or dicarboxamide) fungicides are a family of agricultural fungicides that include vinclozolin, iprodione, and procymidone. Dicarboximides are believed to inhibit triglyceride biosynthesis in sclerotia-forming fungi, including Botrytis cinerea.Copping, L. G. (1998). "Review of major agrochemical classes and uses".

5-Histidylcysteine sulfoxide synthase is the first enzyme in the biosynthesis of ovothiol, catalyzing the oxidative addition of cysteine to histidine, forming 5-histidylcysteine sulfoxide.Braunshausen, A. & Seebeck, F. P. Identification and characterization of the first ovothiol biosynthetic enzyme. J. Am. Chem. Soc. 133, 1757-1759 (2011).

This gene belongs to the sulfotransferase gene family. Sulfotransferases generate sulfated glycosaminoglycan (GAG) moieties during chondroitin sulfate biosynthesis. They create considerable structural diversity among chondroitin sulfates by transferring sulfate with remarkable specificity for the underlying oligosaccharide substrate. This gene product mainly transfers sulfate to N-acetylgalactosamine.

Phosphoribosylaminoimidazolesuccinocarboxamide (SAICAR) is an intermediate in the formation of purines. The conversion of ATP, L-aspartate, and 5-aminoimidazole-4-carboxyribonucleotide (CAIR) to 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide, ADP, and phosphate by phosphoribosylaminoimidazolesuccinocarboxamide synthetase (SAICAR synthetase) represents the eighth step of de novo purine nucleotide biosynthesis.

It has been used as a model species to study photosynthesis, carrageenan biosynthesis, and stress responses. The nuclear genome was sequenced in 2013. The genome size is 105 Mbp and is coding for 9,606 genes. It is characterised by relatively few genes with very few introns.

ColD is a PLP-dependent enzyme responsible for the removal of the C-3' hydroxyl group during the biosynthesis of GDP-colitose. It is a product of the Wbdk or ColD genes in Escherichia coli O55 or Salmonella enterica, respectively, and is commonly referred to as ColD.

They produce Hydrogen gas as a by-product. Hydrogenosomes have been formed from mitochondria through loss of aerobic life stages. The biosynthesis of iron-sulfur clusters has transitioned to be a cytosolic function through a lateral gene transfer event. Other species have reduced mitochondrial organelles called mitosomes.

This typically involves impaired function leading to decreased GSH biosynthesis, reduced cellular antioxidant capacity, and the induction of oxidative stress. However, in cancer, GCL expression and activity is enhanced, which serves to both support the high level of cell proliferation and confer resistance to many chemotherapeutic agents.

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.

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.

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.

UDP-glucuronic acid decarboxylase 1 is an enzyme that in humans is encoded by the UXS1 gene. UDP-glucuronate decarboxylase (UGD; EC 4.1.1.35) catalyzes the formation of UDP-xylose from UDP-glucuronate. UDP-xylose is then used to initiate glycosaminoglycan biosynthesis on the core protein of proteoglycans.

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,.

It is an osmolyte with antioxidant properties. Hypotaurine is derived from cysteine (and homocysteine). In mammals, the biosynthesis of hypotaurine from cysteine occurs in the pancreas. In the cysteine sulfinic acid pathway, cysteine is first oxidized to its sulfinic acid, catalyzed by the enzyme cysteine dioxygenase.

It is made up of 3 ring subunits: 2-deoxystreptamine (DOS), neosamine C, and ribose.Subba, B.; Kharel, M.K.; Lee, H.C.; Liou, K.; Kim, B.G; Sohng, J.K.; The Ribostamycin Biosynthetic Gene Cluster in Streptomyces ribosidificus: Comparison With Butirosin Biosynthesis. Molecules and Cells. 2005, 20 (1), 90-96.

The biosynthesis begins with L-glutamine, which is derived from L-ornithine in plants. The roles of L-ornithine and L-arginine was confirmed by Edward Leete. Ornithine then undergoes a PLP-dependent decarboxylation to form putrescine. In animals, however, the urea cycle derives putrescine from ornithine.

Bacillithiol is produced via the enzymes BshA, BshB, and BshC. BshA replaces the UDP group on UDP-N- acetylglucosamine with an L-malyl group. BshB then removes the acetyl group. L-Cysteine is added to the resulting free amine, which completes the biosynthesis of the molecule.

Two gene clusters are related to the production of aryl polyenes, which function as antioxidants that protect the bacteria from reactive oxygen species. Another gene cluster seems to be involved in terpene biosynthesis, most likely to produce pigments. Other bacteria identified are Thiomicrospira sp., and Desulfocapsa sp.

Tryptophan tryptophylquinone (TTQ) is an enzyme cofactor, generated by posttranslational modification of amino acids within the protein. Methylamine dehydrogenase (MADH), an amine dehydrogenase, requires TTQ for its catalytic function.Davidson VL, Liu A: Uncovering novel biochemistry in the mechanism of tryptophan tryptophylquinone cofactor biosynthesis Curr. Op. Chem. Biol.

Androstenedione is a substrate for estrogen production in granulosa cells which produce aromatase. Thus, theca cells and granulosa cells work together to form estrogens. Androstanedione is a 5α-reduced metabolite of 4-androstenedione which serves as an intermediate in the biosynthesis of the androgen and neurosteroid androsterone.

In enzymology, a (RS)-1-benzyl-1,2,3,4-tetrahydroisoquinoline N-methyltransferase is an enzyme that catalyzes the chemical reaction: 500px : S-adenosyl-L-methionine + (RS)-1-benzyl-1,2,3,4-tetrahydroisoquinoline \rightleftharpoons S-adenosyl-L-homocysteine + N-methyl-(RS)-1-benzyl-1,2,3,4-tetrahydroisoquinoline This enzyme participates in alkaloid biosynthesis.

A product of the bacterial biosynthesis of tryptophan is indole. The excess of tryptophan in hypertryptophanemia also results in substantial excretion of indoleic acids. These findings suggest a possible congenital defect in the metabolic pathway where tryptophan is converted to kynurenine. Kynurenine, a metabolite of tryptophan.

GTP cyclohydrolase I (GTPCH) () is a member of the GTP cyclohydrolase family of enzymes. GTPCH is part of the folate and biopterin biosynthesis pathways. It is responsible for the hydrolysis of guanosine triphosphate (GTP) to form 7,8-dihydroneopterin triphosphate (7,8-DHNP-3'-TP, 7,8-NH2-3'-TP).

Figure 1. The domain structure of MmpA, MmpC, and MmpD for the synthesis of monic acid. The biosynthesis of monic acid is not colinear but has been rearranged in this diagram. The protein name is displayed inside of the arrow with module and domain structure listed below.

Recently, transcriptome analysis of P. multiseries was used to identify a four-gene cluster linked to DA biosynthesis. The identification of these genes presents an opportunity to monitor toxic blooms of Pseudo-nitzschia genetically in order to better understand the toxicity and environmental conditions that cause them.

However, enzymes involved in biosynthesis/inactivation of endocannabinoids and endocannabinoid signalling in general (involving targets other than CB1/2-type receptors) occur throughout the animal kingdom. Although the cannabinoid receptors are unique to Chordates, other organisms are still able to process the endocannabinoids through other techniques.

Serine, formed from 3-phosphoglycerate, is the precursor of glycine and cysteine. Tyrosine is synthesized by the hydroxylation of phenylalanine, an essential amino acid. The pathways for the biosynthesis of essential amino acids are much more complex than those for the nonessential ones. Cortisol inhibits protein synthesis.

Celia White Tabor (November 15, 1918 – December 2, 2012) was an American biochemist and physician-scientist who was an expert on the biosynthesis of polyamines. She was a researcher at the National Institute of Diabetes and Digestive and Kidney Diseases from 1952 until her retirement in 2005.

Several of the genes responsible for pyoverdine biosynthesis (e.g., pvdH, pvdA, and pvdF) are involved in the generation of precursor and alternate amino acids necessary for various portions of the molecule. Several others (e.g., pvdI, and pvdJ) are directly responsible for "stitching" together the peptide chain.

Exostosin-1 is a protein that in humans is encoded by the EXT1 gene. This gene encodes an endoplasmic reticulum-resident type II transmembrane glycosyltransferase involved in the chain elongation step of heparan sulfate biosynthesis. Mutations in this gene cause the type I form of Multiple Exostoses.

This enzyme participates in alanine and aspartate metabolism and D-alanine metabolism. It employs one cofactor, pyridoxal phosphate. At least two compounds, 3-Fluoro-D- alanine and D-Cycloserine are known to inhibit this enzyme. The D-alanine produced by alanine racemase is used for peptidoglycan biosynthesis.

Exostosin glycosyltransferase-2 is a protein that in humans is encoded by the EXT2 gene. This gene encodes one of two glycosyltransferases involved in the chain elongation step of heparan sulfate biosynthesis. Mutations in this gene cause the type II form of Hereditary Multiple Exostoses (HME).

One aspect will be if the neurological disorder are medically actionable (i.e. is there a simple metabolic pathway that a therapy can target). For example, specific cases of ASD have been associated with microdeletions on TMLHE gene. This gene codes for the enzyme of carnitine biosynthesis.

Biosynthesis of eicosanoids Prostaglandins are found in most tissues and organs. They are produced by almost all nucleated cells. They are autocrine and paracrine lipid mediators that act upon platelets, endothelium, uterine and mast cells. They are synthesized in the cell from the fatty acid arachidonic acid.

Certain methyl groups can be deprotonated. For example, the acidity of the methyl groups in acetone ((CH3)2CO) is about 1020 times more acidic than methane. The resulting carbanions are key intermediates in many reactions in organic synthesis and biosynthesis. Fatty acids are produced in this way.

Oxidosqualene cyclase is a key enzyme in the cholesterol biosynthesis pathway. It catalyzes the formation of lanosterol, which is then converted through many steps into cholesterol. The body uses cholesterol for temperature regulation. It is also a precursor for testosterone in males and oestradiol in females.

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.

Stenusin is a piperidine alkaloid molecule synthesized by rove beetles of the genus Stenus Latreille. By lowering its abdomen and releasing stenusin, this genus of rove beetle are able to quickly escape predators through a process called skimming.Lusebrink, Inka; Dettner, Konrad; Seifert, Karlheinz. Biosynthesis of Stenusine.

Pimelic acid is the organic compound with the formula HO2C(CH2)5CO2H. Derivatives of pimelic acid are involved in the biosynthesis of the amino acid called lysine. Pimelic acid is one unit longer than a related dicarboxylic acid, adipic acid, a precursor to many polyesters and polyamides.

TPO uses I− ions and H2O2 to generate iodine, and plays a central role in the biosynthesis of thyroid hormones T3 and T4. Myeloperoxidase (), for example, resides in the human nucleus and lysosome and acts as a defense response to oxidative stress, preventing apoptosis of the cell.

Cynaropicrin binds to the thiol group of the Cys115 in the bacterial enzyme MurA through Michael addition reaction. The unsaturated ester side chain of cynaropicrin appears to mimic the substrate phosphoenolpyruvate (PEP). The irreversible inhibition of this enzyme stops the cytoplasmic biosynthesis of peptidoglycan precursor molecules.

Spirodiclofen is an acaricide and insecticide used in agriculture to control mites and San Jose scale. In the United States, it is used on citrus, grapes, pome fruit, stone fruit, and tree nut crops. Spirodiclofen belongs to the tetronic acid class and acts by inhibiting lipid biosynthesis.

Microsomal triglyceride transfer protein (MTTP) is an endoplasmic reticulum lipid transfer protein involved in the biosynthesis and lipid loading of apolipoprotein B. MTTP is also involved in the late stage of CD1d trafficking in the lysosomal compartment, CD1d being the MHC I-like lipid antigen presenting molecule.

"Closure of the oxide bridge in morphine biosynthesis." Tetrahedron letters 35.23 (1994): 3897-3900. This second step does not require an enzyme. Thebaine can then be converted to morphine through two slightly different biosynthetic routes, one of which makes use of the fourth enzyme codeinone reductase.

Ergocryptine is a mixture of two very similar compounds, alpha- and beta-ergocryptine. The beta differs from the alpha form only in the position of a single methyl group, which is a consequence of the biosynthesis in which the proteinogenic amino acid leucine is replaced by isoleucine.

In Aspergillus fumigatus, the enzymes needed for gliotoxin biosynthesis are encoded in 13 genes within the gli gene cluster. When this gene cluster is activated, these enzymes mediate the production of gliotoxin from serine and phenylalanine residues. Enzymes Involved in Biosynthesis (in order of activity) :GliZ: transcription factor that regulates expression of gli gene cluster :GliP: facilitates formation of cyclo-phenylalanyl-serine intermediate from serine and :phenylalanine residues :GliC: adds hydroxyl group to the alpha carbon of the phenylalanine residue in the :cyclo-phenylalanyl-serine intermediate :GliG: glutathione S-transferase (GST) that adds two glutathione molecules forming a :bis-glutathionylated intermediate :GliK: gamma-glutamyl transferase that removes gamma-glutamyl moieties from :glutathione additions :GliN: adds a methyl group to nitrogen to form the dithiol gliotoxin intermediate :GliT: oxidoreductase that mediates closure of the disulfide-bridge Conversion of dithiol gliotoxin to gliotoxin by the enzyme GliT. :GliA: Major Facilitator Superfamily transporter that secretes gliotoxin across cell membrane :Enzymes GliJ, GliI, GliF, and GliH are necessary for biosynthesis, but their exact function is unknown.

Biomimetic synthesis is an area of organic chemical synthesis that is specifically biologically inspired. The term encompasses both the testing of a "biogenetic hypothesis" (conjectured course of a biosynthesis in nature) through execution of a series of reactions designed to parallel the proposed biosynthesis, as well as programs of study where a synthetic reaction or reactions aimed at a desired synthetic goal are designed to mimic a one or more known enzymic transformations of an established biosynthetic pathway. The earliest generally cited example of a biomimetic synthesis is Sir Robert Robinson's organic synthesis of the alkaloid tropinone. 500px A more recent example is E.J. Corey's carbenium-mediated cyclization of an engineered linear polyene to provide a tetracyclic steroid ring system, which built upon studies of cationic cyclizations of linear polyenes by the Albert Eschenmoser and Gilbert Stork, and the extensive studies of the W.S. Johnson to define the requirements to initiate and terminate the cyclization, and to stabilize the cationic carbenium group during the cyclization (as nature accomplishes via enzymes during biosynthesis of steroids such as cholesterol).

This acid was studied for the first time by Jacobus H. van 't Hoff in 1874. It was later shown to be produced by Clostridium tetanomorphum. Further studies showed that this organic compound is involved in the biosynthesis of vitamin B12. It is a competitive inhibitor of fumarate reduction.

A recent study has shown that the anthraquinone component of lac dye also possess antineoplastic or anticancer effects. It is proposed that lac insects employ polyketide pathway catalysed by polyketide synthase to produce laccaic acid D, a common precursor molecule for the biosynthesis of other lac dye constituents.

TrkA has the highest affinity to the binding nerve growth factor (NGF). NGF is important in both local and nuclear actions, regulating growth cones, motility, and expression of genes encoding the biosynthesis of enzymes for neurotransmitters. Peptidergic nociceptive sensory neurons express mostly trkA and not trkB or trkC.

One of the most significant character of sequence-controlled biosynthesis against other chemical synthetic methods is that the biomolecules (including DNA and RNA) can initiate their polymerization using highly programmed templates. Hence, biosynthetic methods, like PCR, are still considered one of most cogent manner to develop sequence- controlled polymers.

Until the 1950s, dopamine was thought to only contribute to the biosynthesis of norepinephrine and epinephrine. It was not until dopamine was found in the brain in similar levels as norepinephrine that the possibility was considered that its biological role might be other than the synthesis of the catecholamines.

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.

Gersemia fruticosa has been used in the laboratory to study the synthesis of prostaglandins by corals. It has been possible to demonstrate the biosynthesis in vitro in this coral but not in other species studied, and a novel LO pathway or a new COX-isozyme may be involved.

Insulin biosynthesis is regulated by transcriptional and translational levels. The β-cells promote their protein transcription in response to nutrients. The exposure of rat Langerhans islets to glucose for 1 hour is able to remarkably induce the intracellular proinsulin levels. It was noted that the proinsulin mRNA remained stable.

Braesel et al. (2016) Biochemical and genetic basis of orsellinic acid biosynthesis and prenylation in a stereaceous basidiomycete. Fungal Genetics and Biology. Overexpression of two annotated non-reducing polyketide synthases (PKS1 and PKS2) in Aspergillus niger and subsequent characterization of the proteins identified them as orsellinic acid synthases.

PUS 6 has one that only modifies U31 of cytoplasmic and mitochondrial tRNA. Pus 6 is also known to modify mRNA. PUS 8 also known as Rib2 modifies cytoplasmic tRNA at position U32. On the C-terminus there is a DRAP-deaminase domain related to the biosynthesis of riboflavin.

The final step requires oxygen and involves the action of the enzyme ACC-oxidase (ACO), formerly known as the ethylene forming enzyme (EFE). Ethylene biosynthesis can be induced by endogenous or exogenous ethylene. ACC synthesis increases with high levels of auxins, especially indole acetic acid (IAA) and cytokinins.

Streptosolen jamesonii has been found to contain alkaloids which are also present in various Nicotiana species and also in Salpiglossis sinuata: nornicotine (principal alkaloid), nicotine and anabasine.Eich, Prof. Dr. Eckhart, 2008, Solanaceae and Convolvulaceae : Secondary Metabolites - Biosynthesis, Chemotaxonomy, Biological and Economic Significance (A Handbook) pub. Springer-Verlag Berlin Heidelberg, .

As the formation of glucosamine-6-phosphate is the first step for the synthesis of these products, glucosamine may be important in regulating their production; however, the way that the hexosamine biosynthesis pathway is actually regulated, and whether this could be involved in contributing to human disease remains unclear.

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.

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.

Paul, F. "Revival of 2-(difluoromethyl) ornithine (DFMO), an inhibitor of polyamine biosynthesis, as a cancer chemopreventive agent." Biochemical Society Transactions 35.Pt 2 (2007): 353-355. It was found that inhibition of ODC by eflornithine does not kill proliferating cells, making eflornithine ineffective as a chemotherapeutic agent.

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.

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.

The biosynthesis of allopregnanolone in the brain starts with the conversion of progesterone into 5α-dihydroprogesterone by 5α-reductase. After that, 3α-hydroxysteroid dehydrogenase converts this intermediate into allopregnanolone. Allopregnanolone in the brain is produced by cortical and hippocampus pyramidal neurons and pyramidal-like neurons of the basolateral amygdala.

In plants, it is also involved in the biosynthesis of various aromatic compounds, and in carbon fixation; in bacteria, it is also used as the source of energy for the phosphotransferase system.Nelson, D. L.; Cox, M. M. "Lehninger, Principles of Biochemistry" 3rd Ed. Worth Publishing: New York, 2000. .

Without frataxin, the energy in the mitochondria falls, and excess iron creates extra ROS, leading to further cell damage. Low frataxin levels lead to insufficient biosynthesis of iron–sulfur clusters that are required for mitochondrial electron transport and assembly of functional aconitase and iron dysmetabolism of the entire cell.

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.

Lethal synthesis, or suicide metabolism, is the biosynthesis of a toxin from a precursor which is not itself toxic, such as the synthesis of fluorocitrate from fluoroacetate or the synthesis of methylglyoxal from glycerol. The term was first publicised by Rudolph Peters in his Croonian Lecture of 1951.

Conversion of ribose 5-phosphate open chain form to furanose form. R5P is produced in the pentose phosphate pathway in all organisms. The pentose phosphate pathway (PPP) is a metabolic pathway that runs parallel to glycolysis. It is a crucial source for NADPH generation for reductive biosynthesis (e.g.

Nucleotides serve as the building blocks for nucleic acids, DNA and RNA. They are composed of a nitrogenous base, a pentose sugar, and at least one phosphate group. Nucleotides contain either a purine or a pyrimidine nitrogenous base. All intermediates in purine biosynthesis are constructed on a R5P "scaffold".

It is the one- carbon donor for thymidylate synthase, for methylation of 2-deoxy- uridine-5-monophosphate (dUMP) to 2-deoxy-thymidine-5-monophosphate (dTMP). The coenzyme is necessary for the biosynthesis of thymidine and is the C1-donor in the reactions catalyzed by TS and thymidylate synthase (FAD).

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.

The important exceptions are the foods cocoa butter (34%) and shea butter, where the stearic acid content (as a triglyceride) is 28–45%. In terms of its biosynthesis, stearic acid is produced from carbohydrates via the fatty acid synthesis machinery wherein acetyl-CoA contributes two-carbon building blocks.

In 1964 he married Helke Mosner (two children). From 1968–1971 he was a teaching and research assistant at the Physiological Chemistry Institute of the Ludwig-Maximilians-Universität München. In 1971 he was qualified for lecturing at the Universität Konstanz (habilitation). The thesis was entitled: “Biosynthesis of cytochrome c”.

This is supported by the poor water solubility of an inhibitor to ecFabH. It is also hoped that, by being small molecules, their synthesis or biosynthesis will be simple and cheap, thereby enhancing affordability of subsequent drugs to developing countries. Techniques for screening efficacy of inhibitors are available.

Umbarger was a leading expert on biosynthesis of amino acids in bacteria. He is perhaps best known as the co-discoverer, with Edward A. Adelberg in 1953, of feedback inhibition in enzymology. While he was still a student, Umbarger married Merle Gladys Abele (1922–1993). They had three daughters.

The enzyme cystathionine gamma-lyase converts the cystathionine into cysteine and alpha-ketobutyrate. In plants and bacteria, cysteine biosynthesis also starts from serine, which is converted to O-acetylserine by the enzyme serine transacetylase. The enzyme cysteine synthase, using sulfide sources, converts this ester into cysteine, releasing acetate.

Water is not a co- product. The direct biosynthesis of PLA similar to the poly(hydroxyalkanoate)s has been reported as well. Another method devised is by contacting lactic acid with a zeolite. This condensation reaction is a one-step process, and runs about 100 °C lower in temperature.

Glycogenin-1 is an enzyme that is involved in the biosynthesis of glycogen. It is capable of self-glucosylation, forming an oligosaccharide primer that serves as a substrate for glycogen synthase. This is done through an inter- subunit mechanism. It also plays a role in glycogen metabolism regulation.

Group C are disorders of structure and function of myomatrix. Group D disorders are those that affect glycosaminoglycan biosynthesis. Group E disorders are characterized by defects in the complement pathway. Group F are disorders of intracellular processes, and Group G is considered to be unresolved forms of EDS.

The TCA cycle is a hub of metabolism, with central importance in both energy production and biosynthesis. Therefore, it is crucial for the cell to regulate concentrations of TCA cycle metabolites in the mitochondria. Anaplerotic flux must balance cataplerotic flux in order to retain homeostasis of cellular metabolism.

17α-Hydroxyprogesterone (17α-OHP), also known as 17-OH progesterone (17-OHP), or hydroxyprogesterone (OHP), is an endogenous progestogen steroid hormone related to progesterone. It is also a chemical intermediate in the biosynthesis of many other endogenous steroids, including androgens, estrogens, glucocorticoids, and mineralocorticoids, as well as neurosteroids.

Christian Rudolf Hubert Raetz (1946 – August 16, 2011) was the George Barth Geller Professor of Biochemistry at Duke University. He was elected to the National Academy of Sciences in 2006. His laboratory's research focused on lipid biochemistry and has contributed significantly to the understanding of Lipid A biosynthesis.

Journal of Chemical Ecology. (15) 1: 317-28 ISSN 0098-0331/89/0100-0317506.00/0The Pherobase (Database pf pheromones and semiochemicals). 5-Pentylresorcinol. Retrieved 18 January 2014 The cannabis plant internally produces the related substance olivetolic acid (OLA), which may be involved in the biosynthesis of tetrahydrocannabinol (THC).

It is classified as an alkylpyrazine. Its biosynthesis involves amination of acetoin, the latter derived from pyruvate.Takuo Kosuge, Tahei Adachi & Hiroko Kamiya "Isolation Of Tetramethylpyrazine From Culture Of Bacillus Natto, And Biosynthetic Pathways Of Tetramethylpyrazine" Nature 1962, volume 195, 1103 . It exhibits potential nootropic and antiinflammatory activities in rats.

Pederin and its derivatives are being researched as anticancer drugs. This family of compounds is able to inhibit protein and DNA biosynthesis, making it useful to slow the division of cancer cells. One derivative of pederin, psymberin, has been found to be highly selective in targeting solid tumor cells.

N-Methylethanolamine is an alkanolamine with the formula CH3NHCH2CH2OH. It is flammable, corrosive, colorless, viscous liquid.Matthias Frauenkron, Johann- Peter Melder, Günther Ruider, Roland Rossbacher, Hartmut Höke "Ethanolamines and Propanolamines" in Ullmann's Encyclopedia of Industrial Chemistry, 2002, Wiley-VCH, Weinheim. It is an intermediate in the biosynthesis of choline.

Apart from this, studies also suggest that when TM7x is associated with XH001, the gene encoding the lsrB ortholog which functions as a receptor for the AI-2 signalling molecule is highly upregulated. Comparatively, the genes encoding potassium uptake, putative membrane proteins, and ompA expression, known to encode an immunogenic protein were down-regulated. The TM7x cells are capable of several common metabolic processes, such as glycolysis, the TCA cycle, nucleotide biosynthesis and some amino acid biosynthesis and salvage pathways. Genes coding for glycosyl hydrolase family enzymes have been observed, suggesting that these cells may use oligosaccharides as growth substrates, as well as Arginine, which is another potential growth substrate (arginine deiminase pathway).

Ethylene's role in this developmental scenario is to move the plant away from a state of attracting pollinators, so it also aids in decreasing the production of these volatiles. Ethylene production in corolla tissue does not directly cause the senescence of corolla tissue, but acts by releasing secondary products that are consistent with tissue ageing. While the mechanism of ethylene-mediated senescence are unclear, its role as a senescence-directing hormone can be confirmed by ethylene-sensitive petunia response to ethylene knockdown. Knockdown of ethylene biosynthesis genes was consistent with increased corolla longevity; inversely, up-regulation of ethylene biosynthesis gene transcription factors were consistent with a more rapid senescence of the corolla.

Lee et al. showed that the same source of enzymes efficiently make both mevalonate and its 3-ethyl homolog, homomevalonate. Bergot showed that the mevalonate and homomevalonate produced by these enzymes has the same 3S optical isomer configuration as the vertebrate enzymes. Baker showed that isopentenyl diphosphate, and its homolog, 3-ethyl-butenyl diphosphate (homoisopentenyl diphosphate) are metabolized to their corresponding allyic diphosphates, DMAPP and homoDMAPP (3-ethyl-3-methylallyl diphosphate). The latter is required for biosynthesis of JH I, JH II, and 4-methylJH I. 2 units of homoDMAPP are required for JH I and 4methyl JH I biosynthesis, and one for JH II biosynthesis.Baker, F.C., Lee, E., Bergot, B.J., Schooley, D.A., 1981.

Since WTAs are required for host infection and play important role in biofilm formation, it has been suggested that they are important virulence factors required for the establishment and spread of infection in a host. Therefore, the enzymes involved in WTAs biosynthesis can be considered as good targets for novel antivirulence agents that interfere with Gram-positive pathogenic process. One possible target is the WTA biosynthetic pathway because strains of S.aureus and Bacillus subtilis mutants in WTAs are not able to colonize the host tissue and show a greatly diminished ability to establish infection in animal models.Swoboda JG, Campbell J, Meredith TC, Walker S (2010) Wall teichoic acid function, biosynthesis, and inhibition.

3-Hydroxy-16-methoxy-2,3-dihydrotabersonine is a terpene indole alkaloid produced by Catharanthus roseus. The metabolite is a substrate for 3-hydroxy-16-methoxy-2,3-dihydrotabersonine N-methyltransferase (NMT) which transfers a methyl group to the nitrogen of the indole ring forming desacetoxyvindoline.Dethier and De Luca (1993) Partial purification of an N-methyltransferase involved in vindoline biosynthesis in Catharanthus roseus. Phytochemistry. 32(3). 673-678 The enzyme catalyzing the formation of 3-hydroxy-16-methoxy-2,3-dihydrotabersonine from 16-methoxytabersonine is currently unknown, but is a result of hydration of the double bond connecting the 6 and 13 position carbons.Liscombe, Usera and O’connor (2010) Homolog of tocopherol C methyltransferases catalyzes N methylation in anticancer alkaloid biosynthesis.

In some creatures, such as bdelloid rotifers, no trehalose has been found, which has led scientists to propose other mechanisms of anhydrobiosis, possibly involving intrinsically disordered proteins. In 2011, Caenorhabditis elegans, a nematode that is also one of the best-studied model organisms, was shown to undergo anhydrobiosis in the dauer larva stage. Further research taking advantage of genetic and biochemical tools available for this organism revealed that in addition to trehalose biosynthesis, a set of other functional pathways is involved in anhydrobiosis at the molecular level. These are mainly defense mechanisms against reactive oxygen species and xenobiotics, expression of heat shock proteins and intrinsically disordered proteins as well as biosynthesis of polyunsaturated fatty acids and polyamines.

Cuticular wax is known to be largely composed of compounds which derive from very-long-chain fatty acids (VLCFAs), such as aldehydes, alcohols, alkanes, ketones, and esters. Also present are other compounds in cuticular wax which are not VLCFA derivatives, such as terpenoids, flavonoids, and sterols, and thus have different synthetic pathways than those VLCFAs. The first step of the biosynthesis pathway for the formation of cuticular VLCFAs, occurs with the de novo biosynthesis of C16 acyl chains (palmitate) by chloroplasts in the mesophyll, and concludes with the extension of these chains in the endoplasmic reticulum of epidermal cells. An important catalyzer thought to be in this process is the fatty acid elongase (FAE) complex.

Flutamide and hydroxyflutamide have been found in vitro to inhibit CYP17A1 (17α-hydroxylase/17,20-lyase), an enzyme which is required for the biosynthesis of androgens. In accordance, flutamide has been found to slightly but significantly lower androgen levels in GnRH analogue-treated male prostate cancer patients and women with polycystic ovary syndrome. As such, flutamide is a weak inhibitor of androgen biosynthesis. However, the clinical significance of this action may be limited when flutamide is given without a GnRH analogue to non-castrated men, as the medication markedly elevates testosterone levels into the high normal male range via prevention of AR activation-mediated negative feedback on the hypothalamic–pituitary–gonadal axis in this context.

Biosynthesis pathway of N-linked glycoproteins: The synthesis of N-linked glycan starts in the endoplasmic reticulum, continues in the Golgi and ends at the plasma membrane, where the N-linked glycoproteins are either secreted or becomes embedded in the plasma membrane. The biosynthesis of N-linked glycans occurs via 3 major steps: #Synthesis of dolichol-linked precursor oligosaccharide #En bloc transfer of precursor oligosaccharide to protein #Processing of the oligosaccharide Synthesis, en bloc transfer and initial trimming of precursor oligosaccharide occurs in the endoplasmic reticulum (ER). Subsequent processing and modification of the oligosaccharide chain is carried out in the Golgi apparatus. The synthesis of glycoproteins is thus spatially separated in different cellular compartments.

From the viewpoint of chemical synthesis, living organisms are remarkable chemical factories that can easily produce structurally-complex chemical compounds by biosynthesis. In contrast, engineered chemical synthesis is necessarily simpler, with a lower chemical diversity in each reaction, than the incredibly-diverse biosynthesis pathways that are crucial to life. As a result, certain functional groups are much easier to prepare by engineered synthesis than others, such as acetylation, in which certain biosynthetic pathways can generate groups and structures with minimal economic input that would be prohibitive via total synthesis. Plants, animals, fungi, and bacteria are all used as sources for those tricky precursor molecules, including the use of bioreactors at the meeting point between engineered and biological chemical synthesis.

The biosynthesis of xenortides A-D consists of two non-ribosomal peptide synthases (NRPS) coded by genes XndA and XndB, as well as upstream NADH flavin reductase, and a D-aminopeptidase. The first NRPS (XndA) consists of a condensation, adenylation, methylation, and thiolation domain, and has been implicated for the loading of N-methylleucine (xenortides A-B) or N-methylvaline (xenortides C-D). The second NRPS (XndB) consists of a condensation, adenylation, methylation, thiolation, and terminal condensation domains. XndB has been implicated in elongation with N-methylphenylalanine, as well as the final condensation of the enzyme-bound peptide with either decarboxylated phenylalanine (xenortides A and C) or decarboxylated tryptophan (xenortides B and D), ending the biosynthesis.

One or two genes encode the enzymes responsible for the first steps of GA biosynthesis in Arabidopsis and rice. The null alleles of the genes encoding CPS, KS, and KO result in GA-deficient Arabidopsis dwarves. Multigene families encode the 2ODDs that catalyze the formation of GA12 to bioactive GA4.

Ornithine decarboxylase (ODC), is a labile protein that is the first rate-limiting enzyme in polyamine biosynthesis. Its degradation is regulated by antizyme that is induced by polyamine production. NQO1 has been shown to stabilize the degradation of ODC by binding to it and protecting it from 20S proteasomal degradation.

Plant FMO's play a role in defending against pathogens and catalyze specific steps in the biosynthesis of auxin, a plant hormone. Plant FMO's also play a role in the metabolism of glucosinolates. These non-xenobiotic roles of plant FMO's suggest that other FMO functions could be identified in non-plant organisms.

In molecular biology, Yce-I protein domain is a putative periplasmic protein. This entry represents the lipid-binding protein YceI from Escherichia coli and the polyisoprenoid-binding protein TTHA0802 from Thermus thermophilus. Its role is to help aid the biosynthesis of isoprenoid, an important molecule found in all living organisms.

3,5-Dihydroxyphenylglycine can be isolated from the latex of Euphorbia helioscopia. DHGP is also found in vancomycin and related glycopeptides. Although the (S) stereoisomer is synthesized by the DpgA-D enzymes,Yim, G., Thaker, M. N., Koteva, K., Wright, G. "Glycopeptide antibiotic biosynthesis." The Journal of Antibiotics, 2017, 67, 31-41.

Phenethyl isothiocyanate (PEITC) is a naturally occurring isothiocyanate whose precursor, gluconasturtiin is found in some cruciferous vegetables, especially watercress. PEITC has been studied for its potential for chemoprevention of cancers, such as prostate cancer. In terms of biosynthesis, PEITC is produced from gluconasturtiin by the action of the enzyme myrosinase.

The protein encoded by this gene is an isoform of xylosyltransferase, which belongs to a family of glycosyltransferases. This enzyme transfers xylose from UDP-xylose to specific serine residues of the core protein and initiates the biosynthesis of glycosaminoglycan chains in proteoglycans including chondroitin sulfate, heparan sulfate, heparin and dermatan sulfate.

Among the many metabolic processes in which it participates, glutathione is required for the biosynthesis of leukotrienes and prostaglandins. It plays a role in the storage of cysteine. Glutathione enhances the function of citrulline as part of the nitric oxide cycle. It is a cofactor and acts on glutathione peroxidase.

In Bacillus cereus, cereulide biosynthesis occurs by the non-ribosomal peptide synthetase of the heterodimer proteins CesA and CesB. In non-ribosomal peptide synthetase, individual amino acids are added, modified, and linked. Addition is facilitated by the adenylation (A) domain. Modification is accomplished by the ketoreductase (KR) and epimerization (E) domains.

This enzyme participates in d-alanine metabolism and peptidoglycan biosynthesis. Phosphinate and D-cycloserine are known to inhibit this enzyme. The N-terminal region of the D-alanine—D-alanine ligase is thought to be involved in substrate binding, while the C-terminus is thought to be a catalytic domain.

Biosynthesis of spermidine and spermine from putrescine. Ado = 5'-adenosyl Spermidine is synthesized from putrescine, using an aminopropyl group from decarboxylated S-adenosyl-L-methionine (SAM). The reaction is catalyzed by spermidine synthase. Spermine is synthesized from the reaction of spermidine with SAM in the presence of the enzyme spermine synthase.

If rifamycin binds the polymerase after the chain extension process has started, no inhibition is observed on the biosynthesis, consistent with a steric-occlusion mechanism. Single step high level resistance to the rifamycins occurs as the result of a single amino acid change in the bacterial DNA dependent RNA polymerase.

At the turn of the millennium it was apparent that progesterone activity was not mediated only via transcription factor, but also by a membrane-bound G protein-coupled receptor designated as 7TMPR. When the receptor is activated it blocks adenylyl cyclase, leading to decreased biosynthesis of the intracellular second-messenger cAMP.

Coniferyl alcohol is an intermediate in biosynthesis of eugenol and of stilbenoids and coumarin. Gum benzoin contains significant amount of coniferyl alcohol and its esters. It is found in both gymnosperm and angiosperm plants. Sinapyl alcohol and paracoumaryl alcohol, the other two lignin monomers, are found in angiosperm plants and grasses.

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.

The oxygen atoms attached to carbons in positions that do not correspond to polyketides—carbons 8 and 13 (the ether bridge), carbon 2 (the methoxy substituent), and carbon 18 (on the hydroxyethyl chain attached to the lactone ring) are derived from molecular oxygen. Last steps of the biosynthesis of Nargenicin.

This the first step in the biosynthesis of gallotannins. The molecule is then used by enzymes in the gallotannins synthetis pathway like beta-glucogallin O-galloyltransferase or beta-glucogallin-tetrakisgalloylglucose O-galloyltransferase. β-Glucogallin is aldose reductase inhibitor. Half-life of β-Glucogallin in human body seems to be unknown.

Plants in the genus Humulus and Cannabis produce terpenophenolic metabolites, compounds that are meroterpenes.Chapter eight: "Biosynthesis of terpenophenolic metabolites in hop and cannabis". Jonathan E. Page and Jana Nagel, Recent Advances in Phytochemistry, 2006, Volume 40, pp. 179–210, Phenolic lipids are long aliphatic chains bonded to a phenolic moiety.

The immediate precursor is 6-methylsalicylic acid. Isoepoxydon dehydrogenase (IDH) is an important enzyme in the multi-step biosynthesis of patulin. Its gene is present in other fungi that may potentially produce the toxin. It is reactive with sulfur dioxide, so antioxidant and antimicrobial agents may be useful to destroy it.

Stilbenoids are hydroxylated derivatives of stilbene and have a C6–C2–C6 structure. They belong to the family of phenylpropanoids and share most of their biosynthesis pathway with chalcones. Under UV irradiation, stilbene and its derivatives undergo intramolecular cyclization, called Stilbene photocyclization to form dihydrophenanthrenes. Oligomeric forms are known as oligostilbenoids.

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.

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.

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.

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.

Bergamottin is derived from components originating in the shikimate pathway.Dewick, P. Medicinal Natural Products:A Biosynthetic Approach, 2nd ed., Wiley&Sons;: West Sussex, England, 2001, p 145. The biosynthesis of this compound starts with the formation of the demethylsuberosin (3) product, which is formed via the alkylation of the umbelliferone (2) compound.

Plants synthesise isoprenoid precursors using the mevalonate pathway in the cytoplasm and using the MEP pathway in their chloroplasts. Bacteria that use the pathway include important pathogens such Mycobacterium tuberculosis. Non- mevalonate pathway reactions in the biosynthesis of isoprenoids. Redrawn verbatim from the scheme of Qidwai and coworkers [Fig. 2.].

5-Dehydroepisterol is a sterol and an intermediate in steroid biosynthesis, particularly synthesis of brassinosteroids. It is formed from episterol through action of ERG3, the C-5 sterol desaturase in the yeast and is then converted into 24-methylenecholesterol by 7-dehydrocholesterol reductase. Episterol and 5-dehydroepisterol are found in Leishmania.

Methionine is an intermediate in the biosynthesis of cysteine, carnitine, taurine, lecithin, phosphatidylcholine, and other phospholipids. Improper conversion of methionine can lead to atherosclerosis due to accumulation of homocysteine. Methionine might also be essential to reversing damaging methylation of glucocorticoid receptors caused by repeated stress exposures, with implications for depression.

Androstenedione, or 4-androstenedione (abbreviated as A4 or Δ4-dione), also known as androst-4-ene-3,17-dione, is an endogenous weak androgen steroid hormone and intermediate in the biosynthesis of estrone and of testosterone from dehydroepiandrosterone (DHEA). It is closely related to androstenediol (androst-5-ene-3β,17β-diol).

Gooday served as a lecturer at Aberdeen University from 1972 and was promoted to Professor in 1986. His research focused on the fungal cell wall, in particular to the biochemistry and physiology of chitin biosynthesis and degradation. He also contributed to pheromone signalling in zygomycetes and yeast-hypha dimorphism in Candida.

Among his many students was Nobelist K. Barry Sharpless. He led a team who were the first persons to achieve the total synthesis of yohimbine. He pioneered in what is today called biomimetic synthesis. He was the first to identify squalene oxide as a precursor in the biosynthesis of cholesterol.

The category of EC 2.10 includes enzymes that transfer molybdenum or tungsten-containing groups. However, as of 2011, only one enzyme has been added: molybdopterin molybdotransferase. This enzyme is a component of MoCo biosynthesis in Escherichia coli. The reaction it catalyzes is as follows: adenylyl-molybdopterin + molybdate \rightarrow molybdenum cofactor + AMP.

The importance of the AT to the stringent incorporation of specific extender unit in the synthesis of polyketide building blocks makes it vital that the mechanism and structure of these domains be well-elucidated in order to develop efficient strategies for the regiospecific engineering of extender unit incorporation in polyketide biosynthesis.

Here, she focused on enantioselective catalysis of alkyl nucleophiles to ketone and ketoimine substrates. She was awarded a National Institutes of Health Postdoctoral Fellowship which led to her doing postdoctoral work at Harvard Medical School under Professor Jon Clardy. Her postdoctoral research was largely focused on natural product discovery and biosynthesis.

The oxidized, disulfide form of mycothiol (MSSM) is called mycothione, and is reduced to mycothiol by the flavoprotein mycothione reductase. Mycothiol biosynthesis and mycothiol-dependent enzymes such as mycothiol-dependent formaldehyde dehydrogenase and mycothione reductase have been proposed to be good drug targets for the development of treatments for tuberculosis.

The biosynthesis in Lyngbya aestuarii was recently explored by Balskus, Case, and Walsh. It proceeds by the conversion of L-tryptophan to 3-indole pyruvic acid, followed by coupling to p-hydroxyphenylpyruvic acid. Cyclization of the resultant β-ketoacid yields a tricyclic ketone. Oxidation and dimerization yields the completed natural product.

Secologanin biosynthesis begins from geranyl pyrophosphate (GPP) taken from the mevalonate pathway used to make terpenoids. Recent efforts have characterized the entire secologanin biosynthetic pathway. Secologanin is formed from loganin through the action of the enzyme secologanin synthase. Secologanin is then able to proceed onto produce ipecac and terpene indole alkaloids.

After absorption, sultamicillin releases ampicillin and sulbactam into the system, so all the antibacterial efficacy of sultamicillin is due to ampicillin and sulbactam. Ampicillin exerts antibacterial activity against sensitive organisms by inhibiting biosynthesis of cell wall mucopeptide where as sulbactam irreversibly inhibits most important beta-lactamases that occur in resistant strains.

Arenobufagin is a cardiotoxic bufanolide steroid secreted by the Argentine toad Bufo arenarum.Garraffo HM, Gros EG. Biosynthesis of bufadienolides in toads. VI. Experiments with [1,2-3H]cholesterol, [21-14C]coprostanol, and 5 beta-[21-14 °C]pregnanolone in the toad Bufo arenarum. Steroids. 1986 Sep- Oct;48(3-4):251-7.

A hormone produced in the brain of the female moths controls sex pheromones. The hormone is released into the hemolymph to stimulate pheromone production. Pheromone biosynthesis-activating neuropeptide (PBAN) is a peptide that regulates pheromone production in moths. It acts on the pheromone gland cells using calcium and cyclic AMP.

In enzymology, a shikimate dehydrogenase () is an enzyme that catalyzes the chemical reaction :shikimate + NADP+ \rightleftharpoons 3-dehydroshikimate + NADPH + H+ Thus, the two substrates of this enzyme are shikimate and NADP+, whereas its 3 products are 3-dehydroshikimate, NADPH, and H+. This enzyme participates in phenylalanine, tyrosine and tryptophan biosynthesis.

Golden rice differs from its parental strain by the addition of three beta-carotene biosynthesis genes. The parental strain can naturally produce beta-carotene in its leaves, where it is involved in photosynthesis. However, the plant does not normally produce the pigment in the endosperm, where photosynthesis does not occur.

Biosynthesis of indole-3-acetic acid by the gall-inducing fungus Ustilago esculenta. Journal of Biological Sciences 4(6) 744–50. (also, gau sun and kah peh sung)Terrell, E. E. and L. R. Batra. (1982). Zizania latifolia and Ustilago esculenta, a grass-fungus association. Economic Botany 36(3) 274–85.

4-Diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (or CDP-MEP, 4-diphosphocytidyl-2C methylerythritol 2-phosphate) is an intermediate in the MEP pathway of isoprenoid precursor biosynthesis. It is formed by CDP-ME kinase (IspE) and is a substrate for 2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase (IspF).

MPT synthase is involved in the biosynthesis of MoCo, which is essential for the activity of enzymes like xanthine dehydrogenase, aldehyde oxidase, and sulfite oxidase in humans. MoCo containing enzymes typically catalyze the net transfer of an oxygen atom to and from their substrates in a two electron redox reaction.

However, together with other data on neuroendocrine properties of zona glomerulosa cells, NCAM expression may reflect a neuroendocrine differentiation of these cells. Voltage-dependent calcium channels have been detected in the zona glomerulosa of the human adrenal, which suggests that calcium-channel blockers may directly influence the adrenocortical biosynthesis of aldosterone in vivo.

Caffeic acid is an organic compound that is classified as a hydroxycinnamic acid. This yellow solid consists of both phenolic and acrylic functional groups. It is found in all plants because it is a key intermediate in the biosynthesis of lignin, one of the principal components of woody plant biomass and its residues.

Cysteine synthesis from serine. Cystathionine beta synthase catalyzes the upper reaction and cystathionine gamma-lyase catalyzes the lower reaction. Serine is important in metabolism in that it participates in the biosynthesis of purines and pyrimidines. It is the precursor to several amino acids including glycine and cysteine, as well as tryptophan in bacteria.

Biosynthesis of Phosphatidylglycerol Phosphatidic acid reacts with CTP, producing CDP-diacylglycerol, with loss of pyrophosphate. Glycerol-3-phosphate reacts with CDP-diacylglycerol to form phosphatidylglycerol phosphate, while CMP is released. The phosphate group is hydrolysed forming phosphatidylglycerol. Phosphatidylglycerol combines with CDP-DAG forming cardiolipin releasing CMP by the action of cardiolipin synthase.

This mechanism is supported by findings reported in Widboom et al in 2007.Widboom, P. F., Fielding, E. N., Liu, Y., Bruner, S. D. "Structural basis for cofactor-independent dioxygenation in vancomycin biosynthesis." Nature, 2007, 447, 342-345. Finally, the molecule is transaminated by 4-hydroxyphenylglycine transferase using tyrosine to become DHPG.

Final steps of the biosynthesis of DHPG. The mechanism of DpgC on the intermediate substrate has been proposed by Chen et al is included. 4-Hydroxyphenylglycine transferase synthesizes the (S) stereoisomer of DHPG, however, an epimerase switches the stereocenter to the (R) configuration after DHPG is incorporated into the vancomycin non-ribosomal polypeptide.

One of the most interesting things about this biosynthetic pathway is the presence of the Z stereochemistry in the C4/C5 double bond. This feature is not very commonly seen in polyketides. More over module 5 contains a dehydratase (DH) domain that is not functional. Biosynthesis of annimycin proposed by Kalan et al.

Because both galactose and glucose sugars can be added to the ceramide lipid, we have two groups of glycosphingolipids. Galactosphingolipids are generally very simple in structure and the core galactose is not usually modified. Glucosphingolipids, however, are often modified and can become a lot more complex. Biosynthesis of galacto- and glucosphingolipids occurs differently.

The biosynthesis of lipid-linked oligosaccharides is highly conserved among eukaryotes and is catalyzed by 14 glycosyltransferases in an ordered stepwise manner. The Alg1 mannosyltransferase I (MT I) catalyzes the first mannosylation step in this process. Clinically, the deficiency of ALG1 in humans results in ALG1-CDG, a congenital disorder of glycosylation.

In enzymology, a polyneuridine-aldehyde esterase () is an enzyme that catalyzes the chemical reaction: :polyneuridine aldehyde + H2O \rightleftharpoons 16-epivellosimine + CO2 \+ methanol Thus, the two substrates of this enzyme are polyneuridine aldehyde and H2O, whereas its three products are 16-epivellosimine, CO2, and methanol. This enzyme participates in indole and ipecac alkaloid biosynthesis.

Onslow later worked within Bateson's genetic group and then Frederick Gowland Hopkins biochemical group in Cambridge, providing her with expertise in biochemical genetics for investigating the inheritance and biosynthesis of petal colour in Antirrhinum. She was one of the first women appointed as a lecturer at Cambridge, after moving to the Biochemistry department.

1-acyl-sn-glycerol-3-phosphate acyltransferase epsilon is an enzyme that in humans is encoded by the AGPAT5 gene. This gene encodes a member of the 1-acylglycerol-3-phosphate O-acyltransferase family. This integral membrane protein converts lysophosphatidic acid to phosphatidic acid, the second step in de novo phospholipid biosynthesis.

Adenylyltransferase and sulfurtransferase MOCS3 is an enzyme that in humans is encoded by the MOCS3 gene. Molybdenum cofactor (MoCo) is necessary for the function of all molybdoenzymes. One of the enzymes required for the biosynthesis of MoCo is molybdopterin synthase (MPT synthase). The protein encoded by this gene adenylates and activates MPT synthase.

Some organisms, like plants, are autotrophs, meaning that they can fix carbon dioxide for biosynthesis. Plants are photoautotrophs, in that they use the energy of light to fix carbon. Microorganisms employ oxygenic and anoxygenic photoautotrophy, as well as chemoautotrophy. Microbial communities can coordinate in syntrophic metabolisms to shift reaction kinetics in their favor.

This enzyme participates in arginine and proline metabolism and aminoacyl-trna biosynthesis. It contains a conserved domain at the N terminus called arginyl tRNA synthetase N terminal domain or additional domain 1 (Add-1). This domain is about 140 residues long and it has been suggested that it is involved in tRNA recognition.

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.

Sources for β-alanine includes pyrimidine catabolism of cytosine and uracil. β-Alanine can undergo a transamination reaction with pyruvate to form malonate-semialdehyde and L-alanine. The malonate semialdehyde can then be converted into malonate via malonate-semialdehyde dehydrogenase. Malonate is then converted into malonyl-CoA and enter fatty acid biosynthesis.

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.

Biosynthesis of sulfoquinovosyl diacylglycerol (SQDG) from UDP-glucose. In cyanobacteria and plants, SQDG is synthesized in two steps. First, UDP-glucose and sulfite are combined by UDP- sulfoquinovose synthase (SQD1) to produce UDP-sulfoquinovose. Second, the sulfoquinovose portion of UDP-sulfoquinovose is transferred to diacylglycerol by the glycosyltransferase SQDG synthase, to form SQDG .

4-Hydroxymellein is also produced by Aspergillus ochraceus. 6-Hydroxymellein, together with S-adenosyl methionine, is a substrate of the enzyme 6-hydroxymellein O-methyltransferase to form 6-methoxymellein and S-adenosylhomocysteine in Apiaceae.6-methoxymellein biosynthesis pathway on www.biocyc.org 6-Methoxymellein is one of the compounds responsible for bitterness in carrots.

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.

Most lyngbyabellins also contain DHIV in their structure, as well as dolabellin. Figure 2 compares the structures of deacetylhectochlorin, hectochlorin, lyngbyabellin B and dolabellin. This figure illustrates the similarities (black) and differences (red) between those compounds compared to deacetylhectochlorin. All of those compounds (but hectochlorin) do not have a proposed biosynthesis published.

The MR1 protein is capable of binding to molecules derived from bacterial riboflavin biosynthesis, and then present them to MAIT for activation. MR1 is almost undetectable under physiological conditions, surface expression increase in cells infected by microbes. Due to the antigen necessity for MR1 stabilization. MR1 binds the intermediates of riboflavine synthesis.

5-Fluoro-5-deoxy--ribose 1-phosphate is metabolite formed during the biosynthesis of organofluorides. It is formed by the purine nucleoside phosphorylase mediated phosphorolytic cleavage of 5'-deoxy-5'-fluoroadenosine. It is isomerized to 5-fluoro-5-deoxy-ribulose-1-phosphate which is then cleaved by an aldolase to release fluoroacetaldehyde.

Anthocyanin 3-O-glucoside 6″-O-hydroxycinnamoyltransferase is an enzyme forming delphinidin 3-(6-p-coumaroyl)glucoside from delphinidin 3-O-glucoside (myrtillin) and p-coumaroyl-CoA. It is an enzyme in the anthocyanin biosynthesis pathway.Delphinidin 3-(6-p-coumaroyl)glucoside synthesis reaction on www.kegg.jp It can be isolated from Perilla frutescens.

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.

GPAT4 is involved in the biosynthesis of triglycerides. The majority of triglycerides are synthesised from glycerol 3-phosphate (G3P) via the addition of three fatty acyl-CoA substrates, which are made from fatty acids. The first of these additions is catalysed by G3P acyltransferases (GPATs: EC 2.3.1.15), including GPAT4, yielding lysophosphatidic acid.

Thiocyanate is known to be an important part in the biosynthesis of hypothiocyanite by a lactoperoxidase. Thus the complete absence of thiocyanate or reduced thiocyanate in the human body, (e.g., cystic fibrosis) is damaging to the human host defense system. Thiocyanate is a potent competitive inhibitor of the thyroid sodium-iodide symporter.

A cytochrome P450 enzyme is proposed to metabolize diethyl ether.109\. Aspergillus flavus mutant strain 241, blocked in aflatoxin biosynthesis, does not accumulate aflR transcript. Matthew P. Brown and Gary A. Payne, North Carolina State University, Raleigh, NC 27695 fgsc.net Diethyl ether inhibits alcohol dehydrogenase, and thus slows the metabolism of ethanol.

Biosynthesis of cis-3-hexenal from linolenic acid via the hydroperoxide by the action of a lipoxygenase followed by a hydroperoxide lyase. cis-3-Hexenal is an aldehyde. It is relatively unstable and isomerizes into the conjugated trans-2-hexenal. The related alcohol cis-3-hexen-1-ol is much more stable.

EPSP synthase participates in the biosynthesis of the aromatic amino acids phenylalanine, tyrosine, and tryptophan via the shikimate pathway in bacteria, fungi, and plants. EPSP synthase is produced only by plants and micro-organisms; the gene coding for it is not in the mammalian genome. Gut flora of some animals contain EPSPS.

The systematic name of this enzyme class is stearoyl-CoA,ferrocytochrome-b5:oxygen oxidoreductase (9,10-dehydrogenating). Other names in common use include Delta9-desaturase, acyl-CoA desaturase, fatty acid desaturase, and stearoyl- CoA, hydrogen-donor:oxygen oxidoreductase. This enzyme participates in polyunsaturated fatty acid biosynthesis and ppar signaling pathway. It employs one cofactor, iron.

This enzyme is also called leucoanthocyanidin dioxygenase (LDOX) or anthocyanidin synthase (ANS). This enzyme participates in flavonoid biosynthesis. In a broader way, leucocyanidin oxygenase uses flavan-3,4-diols (leucoanthocyanidins) to produce 3-hydroxyanthocyanidins. The gene encoding the enzyme (PpLDOX) has been identified in peach and expression has been studied in Vitis vinifera.

The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is 6-oxocineole,NADPH:oxygen oxidoreductase. This enzyme is also called 6-oxocineole oxygenase. This enzyme participates in terpenoid biosynthesis.

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.

The biosynthesis of oleic acid involves the action of the enzyme stearoyl-CoA 9-desaturase acting on stearoyl-CoA. In effect, stearic acid is dehydrogenated to give the monounsaturated derivative, oleic acid. Oleic acid undergoes the reactions of carboxylic acids and alkenes. It is soluble in aqueous base to give soaps called oleates.

This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-arogenate:2-oxoglutarate aminotransferase. Other names in common use include prephenate transaminase (ambiguous), PAT (ambiguous), and L-glutamate:prephenate aminotransferase. It operates in the phenylalanine and tyrosine biosynthesis pathway.

Fisetin is a flavonoid, which is a polyphenol subgroup. Flavonoid synthesis begins with the phenylpropanoid pathway, in which phenylalanine, an amino acid, is transformed into 4-coumaroyl-CoA. This is the compound that enters the flavonoid biosynthesis pathway. Chalcone synthase, the first enzyme of this pathway, produces chalcone from 4-coumaroyl-CoA.

In enzymology, a chrysanthemyl diphosphate synthase () is an enzyme involved in the biosynthesis of terpenoids. This enzyme is also known as CPPase. It catalyzes the chemical reaction shown below (color-coded to show how precursors link): :320px The substrate of CPPase is dimethylallyl diphosphate. The two products are diphosphate and chrysanthemyl diphosphate.

PLP is an essential component of enzymes that facilitate the biosynthesis of sphingolipids. Particularly, the synthesis of ceramide requires PLP. In this reaction, serine is decarboxylated and combined with palmitoyl-CoA to form sphinganine, which is combined with a fatty acyl- CoA to form dihydroceramide. Dihydroceramide is then further desaturated to form ceramide.

Cytochalasin B has an effect on thyroid hormone and growth hormone secretion. Phosphatidylcholine and phosphatidylethanolamine biosynthesis is inhibited by cytochalasin B, as shown by George et al. It does so by inhibiting the conversion of phosphoethanolamine to cytidinediphosphate-ethanolamine. It was proposed that the mechanism is associated with alterations of intracellular calcium ions.

Arginine synthesis also utilizes negative feedback as well as repression through a repressor encoded by the gene argR. The gene product of argR, ArgR an aporepressor, and arginine as a corepressor affect the operon of arginine biosynthesis. The degree of repression is determined by the concentrations of the repressor protein and corepressor level.

The third step is the dehydration of α, β-dihydroxyisovalerate catalyzed by dihydroxy acid dehydrase. In the fourth and final step, the resulting α-ketoisovalerate undergoes transamination catalyzed either by an alanine- valine transaminase or a glutamate-valine transaminase. Valine biosynthesis is subject to feedback inhibition in the production of acetohydroxy acid synthase.

Homoisocitric acid is an isomer of homocitric acid in which the hydroxyl is on the 2 position. It is an intermediate in the α-aminoadipate pathway of lysine biosynthesis where it is produced by homocitrate synthase and is a substrate for homoaconitase. Homoisocitrate is an anion, salt, or ester of homoisocitric acid.

Dr. Luis Leloir deduced the role of GALE in galactose metabolism during his tenure at the Instituto de Investigaciones Bioquímicas del Fundación Campomar, initially terming the enzyme waldenase. Dr. Leloir was awarded the 1970 Nobel Prize in Chemistry for his discovery of sugar nucleotides and their role in the biosynthesis of carbohydrates.

April 4, 2005 Plant gene replacement results in the world's only blue rose Dihydroflavonol 4-reductase is an enzyme part of the lignin biosynthesis pathway. In Arabidopsis thaliana, the enzyme uses sinapaldehyde or coniferyl aldehyde or coumaraldehyde and NADPH to produce sinapyl alcohol or coniferyl alcohol or coumaryl alcohol respectively and NADP+.

Gaston, Marsha A.; Jiang, Ruisheng; Krzycki, Joseph A. "Functional Context, Biosynthesis, and Genetic Encoding of Pyrrolysine" Current Opinion in Microbiology 2011, vol. 14, pp. 342-349. Quitterer, F.; Beck, P.; Bacher, A.; Groll, M., "Structure and Reaction Mechanism of Pyrrolysine Synthase (PylD)", Angew. Chem. Int. Ed. 2013, volume 52, pp. 7033-7037.

Studies on Arabidopsis mutants revealed that several Glycosyltransferases are involved in the biosynthesis of xylans. Glycosyltransferases (GTs) catalyze the formation of glycosidic bonds between sugar molecules using nucleotide sugar as donor molecule. In eukaryotes, GTs represent about 1% to 2% of gene products. GTs are assembled into complexes existing in the Golgi apparatus.

Within a normal yeast cell, lanosterol is demethylated using 14α-demethylation. This process creates zymosterol: a major constituent in the ergosterol biosynthesis pathway for the creation of cell membrane constituents in yeast. This structure provides the membrane with fluidity. This occurs by transforming lanosterol into 4,4'-dimethyl cholesta-8,14,24-triene-3-β-ol.

Aminoshikimic acid is an unnatural carbohydrate, although aminoshikimic acid is the namesake of the aminoshikimate pathway, which generates the 3-amino-5-hydroxybenzoic acid (AHBA) starter unit required for the biosynthesis of the ansamycins and mitomycins. The first microbe- catalyzed syntheses of aminoshikimic acid were described by Guo and Frost in 2004.

An alternative theory involving endogenous non-peptidyl biosynthesis was also proposed, based on evidence gathered from a study involving feeding normal and undernourished human subjects with the amino acid lysine.Khan- Siddiqui, L.; Bamji, M. S. Lysine-carnitine conversion in normal and undernourished adult man – suggestion of a nonpeptidyl pathway. Am. J. Clin. Nutr.

6-deoxyerythronolide B hydroxylase is an Actinobacteria Cytochrome P450 enzyme originally from Saccharopolyspora erythraea, catalyzes the 6S-hydroxylate of 6-deoxyerythronolide B (6-DEB) to erythronolide B (EB) which is the first step of biosynthesis of the macrolide antibiotic erythromycin. This bacterial enzyme belongs to CYP family CYP107, with the CYP Symbol CYP107A1.

Together with norvaline, norleucine is found in small amounts in some bacterial strains where its concentration can approach millimolar. Its biosynthesis has been examined. It arises via the action of 2-isopropylmalate synthase on α-ketobutyrate. The incorporation of Nle into peptides reflects the imperfect selectivity of the associated aminoacyl-tRNA synthetase.

In animals, the peripheral benzodiazepine receptor is a mitochondrial protein (located in the outer mitochondrial membrane) characterised by its ability to bind with nanomolar affinity to a variety of benzodiazepine-like drugs, as well as to dicarboxylic tetrapyrrole intermediates of the haem biosynthetic pathway. Depending upon the tissue, it was shown to be involved in steroidogenesis, haem biosynthesis, apoptosis, cell growth and differentiation, mitochondrial respiratory control, and immune and stress response, but the precise function of the PBR remains unclear. The role of PBR in the regulation of cholesterol transport from the outer to the inner mitochondrial membrane, the rate- determining step in steroid biosynthesis, has been studied in detail. PBR is required for the binding, uptake and release, upon ligand activation, of the substrate cholesterol.

David Gottlieb (1911–1982), a professor of plant pathology at the University of Illinois at Urbana-Champaign (1946–1982), was a pioneer in the field of fungal physiology and antibiotics for plants. Gottlieb is best known for isolation in the 1940s of the strain of Streptomyces from which chloramphenicol was developed, for his mentoring in the field, and for his editorial work.Editor for the Annual Review of Phytopathology, 1969-1974 He used plant-pathogenic fungi in studies of sterol biosynthesis, respiration, aging, spore germination, and the mechanism of action of antifungal antibiotics. Gottlieb discovered or co-discovered several new antibiotics in addition to chloramphenicol, including filipin, levomycin, and tetrin, and he described the mechanism of action and biosynthesis of several of these and other antibiotics.

Proposed scheme for the biosynthesis of trabecteden The biosynthesis of trabectedin in Candidatus Endoecteinascidia frumentensis starts with a fatty acid loading onto the acyl-ligase domain of the EtuA3 module. A cysteine and glycine are then loaded as canonical NRPS amino acids. A tyrosine residue is modified by the enzymes EtuH, EtuM1, and EtuM2 to add a hydroxyl at the meta position of the phenol, and adding two methyl groups at the para-hydroxyl and the meta carbon position. This modified tyrosine reacts with the original substrate via a Pictet-Spengler reaction, where the amine group is converted to an imine by deprotonation, then attacks the free aldehyde to form a carbocation that is quenched by electrons from the methyl-phenol ring.

Although either can dictate colour, the VvMYBA1 gene, which activates the anthocyanin biosynthesis necessary to produce red grapes, was shown not to be transcribed in white grape berries. The white berry allele of VvMYBA2 was inactivated by two mutations, one leading to an amino acid substitution and the other to a frameshift mutation. Tests showed that either mutation removes the ability of the regulator to switch on anthocyanin biosynthesis, and when both are switched off it results in a white cultivar. Sequence analyses of the VvMYBA2 gene confirmed that all of the 55 white cultivars tested contained the white berry allele, but not red berry alleles – and all displayed exactly the same double mutation, pointing to a single, common ancestor.

In recent research that builds on his work in polymerisation, Gilbert has developed a new way of understanding the biochemistry of the enzymatic processes involved in starch biosynthesis, in collaboration with Dr Melissa Fitzgerald, International Rice Research Institute, Manilla. In this new field, he applied the methods he had developed for understanding molecular-weight distributions in synthetic polymers to understanding those of natural ones. He has thus created a powerful new technique for probing the enzymatic processes in starch biosynthesis in grains, again, creating a methodology to obtain reliable mechanistic knowledge by isolating steps in highly complex systems. Each enzymatic step that creates individual chains—analysed by debranching the starch—can now be associated with particular regions in the molecular-weight distribution of a starch.

Cyanobacteria blooms on a lake Nitrogen-fixing marine cyanobacteria are known to support oxygen production in oceans by fixing inorganic nitrogen using the enzyme nitrogenase. A special subset of these bacteria, UCYN-A, was found to lack the photosystem II complex usually used in photosynthesis and that it lacks a number of major metabolic pathways but is still capable of using the electron transport chain to generate energy from a light source. Furthermore, anabolic enzymes needed for creating amino acids such as valine, leucine and isoleucine are missing, as well as some which lead to phenylalanine, tyrosine and tryptophan biosynthesis. This organism seems to be an obligate photoheterotroph that uses carbon substrates for energy production and some biosynthetic materials for biosynthesis.