Biology:Dihydrofolate synthase
| Dihydrofolate synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Dihydrofolate synthase monomer, E.Coli | |||||||||
| Identifiers | |||||||||
| EC number | 6.3.2.12 | ||||||||
| CAS number | 37318-62-0 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, a dihydrofolate synthase (EC 6.3.2.12) is an enzyme that catalyzes the chemical reaction
- ATP + 7,8-dihydropteroate + L-glutamate [math]\displaystyle{ \rightleftharpoons }[/math] ADP + phosphate + 7,8-dihydropteroylglutamate
The 3 substrates of this enzyme are ATP, 7,8-dihydropteroate, and L-glutamate, whereas its 3 products are ADP, phosphate, and 7,8-dihydropteroylglutamate.
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 7,8-dihydropteroate:L-glutamate ligase (ADP-forming). Other names in common use include dihydrofolate synthetase, 7,8-dihydrofolate synthetase, H2-folate synthetase, 7,8-dihydropteroate:L-glutamate ligase (ADP), dihydrofolate synthetase-folylpolyglutamate synthetase, folylpoly-(gamma-glutamate) synthetase-dihydrofolate synthase, FHFS, FHFS/FPGS, dihydropteroate:L-glutamate ligase (ADP-forming), and DHFS. This enzyme participates in folate biosynthesis.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1W78, 1W7K, and 2BMB.
References
- "The Biosynthesis of Folic Acid. III. Enzymatic Formation of Dihydrofolic Acid from Dihydropteroic Acid and of Tetrahydropteroylpolyglutamic Acid Compounds from Tetrahydrofolic Acid". J. Biol. Chem. 239: 310–6. 1964. doi:10.1016/S0021-9258(18)51783-X. PMID 14114858.
- "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. 1985. doi:10.1016/S0021-9258(18)89069-X. 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. PMID 11752472. Bibcode: 2001PNAS...9815360R.
- "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. 2000. doi:10.1074/jbc.275.19.14056. PMID 10799479.
- "Folates and one-carbon metabolism in plants and fungi". Phytochemistry 45 (3): 437–52. 1997. doi:10.1016/S0031-9422(96)00833-3. PMID 9190084.
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