The Enzyme Database

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EC 2.1.2.5     
Accepted name: glutamate formimidoyltransferase
Reaction: 5-formimidoyltetrahydrofolate + L-glutamate = tetrahydrofolate + N-formimidoyl-L-glutamate
Other name(s): FTCD (gene name); glutamate formyltransferase; formiminoglutamic acid transferase; formiminoglutamic formiminotransferase; glutamate formiminotransferase
Systematic name: 5-formimidoyltetrahydrofolate:L-glutamate N-formimidoyltransferase
Comments: The enzyme also catalyses formyl transfer from 5-formyltetrahydrofolate to L-glutamate. In eukaryotes, it occurs as a bifunctional enzyme that also has formimidoyltetrahydrofolate cyclodeaminase (EC 4.3.1.4) activity.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9032-83-1
References:
1.  Miller, A. and Waelsch, H. Formimino transfer from formamidinoglutaric acid to tetrahydrofolic acid. J. Biol. Chem. 228 (1957) 397–417. [PMID: 13475327]
2.  Silverman, M., Keresztesy, J.C., Koval, G.J. and Gardiner, R.C. Citrovorium factor and the synthesis of formylglutamic acid. J. Biol. Chem. 226 (1957) 83–94. [PMID: 13428739]
3.  Tabor, H. and Wyngarden, L. The enzymatic formation of formiminotetrahydrofolic acid, 5,10-methenyltetrahydrofolic acid, and 10-formyltetrahydrofolic acid in the metabolism of formiminoglutamic acid. J. Biol. Chem. 234 (1959) 1830–1849. [PMID: 13672973]
4.  Kohls, D., Sulea, T., Purisima, E.O., MacKenzie, R.E. and Vrielink, A. The crystal structure of the formiminotransferase domain of formiminotransferase-cyclodeaminase: implications for substrate channeling in a bifunctional enzyme. Structure 8 (2000) 35–46. [PMID: 10673422]
5.  Mao, Y., Vyas, N.K., Vyas, M.N., Chen, D.H., Ludtke, S.J., Chiu, W. and Quiocho, F.A. Structure of the bifunctional and Golgi-associated formiminotransferase cyclodeaminase octamer. EMBO J. 23 (2004) 2963–2971. [PMID: 15272307]
6.  Jeanguenin, L., Lara-Nunez, A., Pribat, A., Mageroy, M.H., Gregory, J.F., 3rd, Rice, K.C., de Crecy-Lagard, V. and Hanson, A.D. Moonlighting glutamate formiminotransferases can functionally replace 5-formyltetrahydrofolate cycloligase. J. Biol. Chem. 285 (2010) 41557–41566. [PMID: 20952389]
[EC 2.1.2.5 created 1961, modified 2000 (EC 2.1.2.6 created 1965, incorporated 1984)]
 
 


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