Tetrahydrofolate synthase

The 3 substrates of this enzyme are ATP, [[tetrahydropteroyl-[gamma-Glu]n]], and L-glutamate, whereas its 3 products are ADP, phosphate, and [[tetrahydropteroyl-[gamma-Glu]n+1]].

This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases (peptide synthases). The systematic name of this enzyme class is tetrahydropteroyl-gamma-polyglutamate:L-glutamate gamma-ligase (ADP-forming). Other names in common use include folylpolyglutamate synthase, folate polyglutamate synthetase, formyltetrahydropteroyldiglutamate synthetase, N10-formyltetrahydropteroyldiglutamate synthetase, folylpoly-gamma-glutamate synthase, folylpolyglutamyl synthetase, folylpoly(gamma-glutamate) synthase, folylpolyglutamate synthetase, folylpoly-gamma-glutamate synthetase-dihydrofolate synthetase, FPGS, tetrahydrofolylpolyglutamate synthase, tetrahydrofolate:L-glutamate gamma-ligase (ADP-forming), tetrahydropteroyl-[gamma-Glu]n:L-glutamate gamma-ligase, and (ADP-forming). This enzyme participates in folate biosynthesis.

Structural studies

As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes 1FGS, 1JBV, 1JBW, 2GC5, 2GC6, 2GCA, and 2GCB.

References

Cichowicz DJ, Foo SK, Shane B (1981). "Folylpoly-gamma-glutamate synthesis by bacteria and mammalian cells". Mol. Cell. Biochem. 39: 209–28. doi:10.1007/BF00232575. PMID 6458762.
McGuire JJ, Bertino JR (1981). "Enzymatic synthesis and function of folylpolyglutamates". Mol. Cell. Biochem. 38 Spec No (Pt 1): 19–48. PMID 7027025.
Bognar AL, Osborne C, Shane B, Singer SC, Ferone R (1985). "Folylpoly-gamma-glutamate synthetase-dihydrofolate synthetase Cloning and high expression of the Escherichia coli folC gene and purification and properties of the gene product". J. Biol. Chem. 260 (9): 5625–30. PMID 2985605.
R, Rebeille F; Cherest, H; Jabrin, S; Grunwald, D; Surdin-Kerjan, Y; Douce, R; Rébeillé, F (2001). "Tetrahydrofolate biosynthesis in plants: molecular and functional characterization of dihydrofolate synthetase and three isoforms of folylpolyglutamate synthetase in Arabidopsis thaliana". Proc. Natl. Acad. Sci. U.S.A. 98 (26): 15360–5. doi:10.1073/pnas.261585098. PMC 65034. PMID 11752472.
Cossins EA, Chen L (1997). "Folates and one-carbon metabolism in plants and fungi". Phytochemistry. 45 (3): 437–52. doi:10.1016/S0031-9422(96)00833-3. PMID 9190084.
Cherest H, Thomas D, Surdin-Kerjan Y (2000). "Polyglutamylation of folate coenzymes is necessary for methionine biosynthesis and maintenance of intact mitochondrial genome in Saccharomyces cerevisiae". J. Biol. Chem. 275 (19): 14056–63. doi:10.1074/jbc.275.19.14056. PMID 10799479.

Enzymes: CO CS and CN ligases (EC 6.1-6.3)

6.1: Carbon-Oxygen	Aminoacyl tRNA synthetase Alanine Arginine Asparagine Aspartate Cysteine D-alanine—poly(phosphoribitol) ligase Glutamate Glutamine Glycine Histidine Isoleucine Leucine Lysine Methionine Phenylalanine Proline Serine Threonine Tryptophan Tyrosine Valine

6.2: Carbon-Sulfur	Succinyl coenzyme A synthetase Acetyl—CoA synthetase Long-chain-fatty-acid—CoA ligase

6.3: Carbon-Nitrogen	Glutamine synthetase Ubiquitin ligase Cullin Von Hippel–Lindau tumor suppressor UBE3A Mdm2 Anaphase-promoting complex UBR1 Glutathione synthetase CTP synthetase Adenylosuccinate synthase Argininosuccinate synthase Holocarboxylase synthetase GMP synthase Asparagine synthetase Carbamoyl phosphate synthetase I II Glutamate–cysteine ligase

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases(list) EC2 Transferases(list) EC3 Hydrolases(list) EC4 Lyases(list) EC5 Isomerases(list) EC6 Ligases(list)

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