Tetrahydrofolate synthase
In enzymology, a tetrahydrofolate synthase (EC 6.3.2.17) is an enzyme that catalyzes the chemical reaction
- ATP + tetrahydropteroyl-[gamma-Glu]n + L-glutamate ADP + phosphate + tetrahydropteroyl-[gamma-Glu]n+1
| tetrahydrofolylpolyglutamate synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 6.3.2.17 | ||||||||
| CAS number | 63363-84-8 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
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. S2CID 43985411.
- McGuire JJ, Bertino JR (1981). "Enzymatic synthesis and function of folylpolyglutamates". Mol. Cell. Biochem. 38 Spec. No (Pt 1): 19–48. doi:10.1007/BF00235686. PMID 7027025. S2CID 9149947.
- 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. Bibcode:2001PNAS...9815360R. 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.