The Enzyme Database

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Accepted name: phosphoribosylglycinamide formyltransferase 1
Reaction: 10-formyltetrahydrofolate + N1-(5-phospho-D-ribosyl)glycinamide = tetrahydrofolate + N2-formyl-N1-(5-phospho-D-ribosyl)glycinamide
For diagram of purine biosynthesis (early stages), click here
Other name(s): 2-amino-N-ribosylacetamide 5′-phosphate transformylase; GAR formyltransferase; GAR transformylase; glycinamide ribonucleotide transformylase; GAR TFase; 5,10-methenyltetrahydrofolate:2-amino-N-ribosylacetamide ribonucleotide transformylase; purN (gene name); ADE8 (gene name); GART (gene name); 5′-phosphoribosylglycinamide transformylase; phosphoribosylglycinamide formyltransferase (ambiguous)
Systematic name: 10-formyltetrahydrofolate:5′-phosphoribosylglycinamide N-formyltransferase
Comments: Two enzymes are known to catalyse the third step in de novo purine biosynthesis. This enzyme utilizes 10-formyltetrahydrofolate as the formyl donor, while the other enzyme, EC, phosphoribosylglycinamide formyltransferase 2, utilizes formate. In vertebrates this activity is catalysed by a trifunctional enzyme that also catalyses the activities of EC, phosphoribosylamine—glycine ligase and EC, phosphoribosylformylglycinamidine cyclo-ligase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9032-02-4
1.  Hartman, S.C. and Buchanan, J.M. Biosynthesis of the purines. XXVI. The identification of the formyl donors of the transformylation reaction. J. Biol. Chem. 234 (1959) 1812–1816. [PMID: 13672969]
2.  Smith, G.K., Benkovic, P.A. and Benkovic, S.J. L(–)-10-Formyltetrahydrofolate is the cofactor for glycinamide ribonucleotide transformylase from chicken liver. Biochemistry 20 (1981) 4034–4036. [PMID: 7284307]
3.  Warren, L. and Buchanan, J.M. Biosynthesis of the purines. XIX. 2-Amino-N-ribosylacetamide 5′-phosphate (glycinamide ribotide) transformylase. J. Biol. Chem. 229 (1957) 613–626. [PMID: 13502326]
4.  Schild, D., Brake, A.J., Kiefer, M.C., Young, D. and Barr, P.J. Cloning of three human multifunctional de novo purine biosynthetic genes by functional complementation of yeast mutations. Proc. Natl. Acad. Sci. USA 87 (1990) 2916–2920. [DOI] [PMID: 2183217]
5.  Zhang, Y., Desharnais, J., Greasley, S.E., Beardsley, G.P., Boger, D.L. and Wilson, I.A. Crystal structures of human GAR Tfase at low and high pH and with substrate β-GAR. Biochemistry 41 (2002) 14206–14215. [DOI] [PMID: 12450384]
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