Dihydrofolate synthase

Dihydrofolate synthase
Dihydrofolate synthase monomer, E.Coli
Identifiers
EC no.	6.3.2.12
CAS no.	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
Search PMC articles PubMed articles NCBI proteins

In enzymology, a dihydrofolate synthase (EC 6.3.2.12) is an enzyme that catalyzes the chemical reaction

ATP + 7,8-dihydropteroate + L-glutamate ${\displaystyle \rightleftharpoons }$ 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.

As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1W78, 1W7K, and 2BMB.

• GRIFFIN MJ, BROWN GM (1964). "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. doi:10.1016/S0021-9258(18)51783-X. PMID 14114858.
• 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. 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. Bibcode:2001PNAS...9815360R. doi:10.1073/pnas.261585098. PMC 65034. PMID 11752472.
• 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.
• Cossins EA, Chen L (1997). "Folates and one-carbon metabolism in plants and fungi". Phytochemistry. 45 (3): 437–52. Bibcode:1997PChem..45..437C. doi:10.1016/S0031-9422(96)00833-3. PMID 9190084.

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