ExplorEnz: EC 6.3.2.17

Your query returned 1 entry. Printable version

6.3.2.17

Accepted name:

tetrahydrofolate synthase

Reaction:

ATP + tetrahydropteroyl-[γ-Glu]_n + L-glutamate = ADP + phosphate + tetrahydropteroyl-[γ-Glu]_n+1

For diagram of folate biosynthesis (late stages), click here

Other name(s):

folylpolyglutamate synthase; folate polyglutamate synthetase; formyltetrahydropteroyldiglutamate synthetase; N¹⁰-formyltetrahydropteroyldiglutamate synthetase; folylpoly-γ-glutamate synthase; folylpolyglutamyl synthetase; folylpoly(γ-glutamate) synthase; folylpolyglutamate synthetase; FPGS; tetrahydrofolylpolyglutamate synthase; tetrahydrofolate:L-glutamate γ-ligase (ADP-forming); tetrahydropteroyl-[γ-Glu]_n:L-glutamate γ-ligase (ADP-forming)

Systematic name:

tetrahydropteroyl-γ-polyglutamate:L-glutamate γ-ligase (ADP-forming)

Comments:

In some bacteria, a single protein catalyses both this activity and that of EC 6.3.2.12, dihydrofolate synthase [3], the combined activity of which leads to the formation of the cofactor polyglutamated tetrahydropteroate (H₄PteGlu_n), i.e. various tetrahydrofolates (H₄folate). In contrast, the activities are located on separate proteins in most eukaryotes studied to date [4]. In Arabidopsis thaliana, this enzyme is present as distinct isoforms in the mitochondria, the cytosol and the chloroplast. Each isoform is encoded by a separate gene, a situation that is unique among eukaryotes [4]. As the affinity of folate-dependent enzymes increases markedly with the number of glutamic residues, the tetrahydropteroyl polyglutamates are the preferred cofactors of C₁ metabolism. (reviewed in [5]). The enzymes from different sources (particularly eukaryotes versus prokaryotes) have different substrate specificities with regard to one-carbon substituents and the number of glutamate residues present on the tetrahydrofolates.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 63363-84-8

References:

1.	Cichowicz, D., Foo, S.K. and Shane, B. Folylpoly-γ-glutamate synthesis by bacteria and mammalian cells. Mol. Cell. Biochem. 39 (1981) 209–228. [DOI] [PMID: 6458762]
2.	McGuire, J.J. and Bertino, J.R. Enzymatic synthesis and function of folylpolyglutamates. Mol. Cell. Biochem. 38 (1981) 19–48. [DOI] [PMID: 7027025]
3.	Bognar, A.L., Osborne, C., Shane, B., Singer, S.C. and Ferone, R. Folylpoly-γ-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 (1985) 5625–5630. [DOI] [PMID: 2985605]
4.	Ravanel, S., Cherest, H., Jabrin, S., Grunwald, D., Surdin-Kerjan, Y., Douce, R. and Rébeillé, F. Tetrahydrofolate biosynthesis in plants: molecular and functional characterization of dihydrofolate synthetase and three isoforms of folylpolyglutamate synthetase in Arabidopsis thaliana. Proc. Natl. Acad. Sci. USA 98 (2001) 15360–15365. [DOI] [PMID: 11752472]
5.	Cossins, E.A. and Chen, L. Folates and one-carbon metabolism in plants and fungi. Phytochemistry 45 (1997) 437–452. [DOI] [PMID: 9190084]
6.	Cherest, H., Thomas, D. and Surdin-Kerjan, Y. Polyglutamylation of folate coenzymes is necessary for methionine biosynthesis and maintenance of intact mitochondrial genome in Saccharomyces cerevisiae. J. Biol. Chem. 275 (2000) 14056–14063. [DOI] [PMID: 10799479]

[EC 6.3.2.17 created 1984, modified 2003, modified 2005]