The Enzyme Database

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EC 2.1.2.1     
Accepted name: glycine hydroxymethyltransferase
Reaction: 5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
For diagram of folate cofactors, click here and for diagram of C1 metabolism, click here
Other name(s): serine aldolase; threonine aldolase; serine hydroxymethylase; serine hydroxymethyltransferase; allothreonine aldolase; L-serine hydroxymethyltransferase; L-threonine aldolase; serine transhydroxymethylase
Systematic name: 5,10-methylenetetrahydrofolate:glycine hydroxymethyltransferase
Comments: A pyridoxal-phosphate protein. Also catalyses the reaction of glycine with acetaldehyde to form L-threonine, and with 4-trimethylammoniobutanal to form 3-hydroxy-N6,N6,N6-trimethyl-L-lysine.
Links to other databases: BRENDA, EXPASY, Gene, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9029-83-8
References:
1.  Akhtar, M. and El-Obeid, H.A. Inactivation of serine transhydroxymethylase and threonine aldolase activities. Biochim. Biophys. Acta 258 (1972) 791–799. [DOI] [PMID: 5017703]
2.  Blakley, R.L. A spectrophotometric study of the reaction catalysed by serine transhydroxymethylase. Biochem. J. 77 (1960) 459–465. [PMID: 16748851]
3.  Fujioka, M. Purification and properties of serine hydroxymethylase from soluble and mitochondrial fractions of rabbit liver. Biochim. Biophys. Acta 185 (1969) 338–349. [DOI] [PMID: 5808700]
4.  Kumagai, H., Nagate, T., Yoshida, H. and Yamada, H. Threonine aldolase from Candida humicola. II. Purification, crystallization and properties. Biochim. Biophys. Acta 258 (1972) 779–790. [DOI] [PMID: 5017702]
5.  Schirch, L.V. and Gross, T. Serine transhydroxymethylase. Identification as the threonine and allothreonine aldolases. J. Biol. Chem. 243 (1968) 5651–5655. [PMID: 5699057]
[EC 2.1.2.1 created 1961, modified 1983]
 
 
EC 2.1.2.2     
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 6.3.1.21, phosphoribosylglycinamide formyltransferase 2, utilizes formate. In vertebrates this activity is catalysed by a trifunctional enzyme that also catalyses the activities of EC 6.3.4.13, phosphoribosylamine—glycine ligase and EC 6.3.3.1, phosphoribosylformylglycinamidine cyclo-ligase.
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9032-02-4
References:
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]
[EC 2.1.2.2 created 1961, modified 2000, modified 2021]
 
 
EC 2.1.2.3     
Accepted name: phosphoribosylaminoimidazolecarboxamide formyltransferase
Reaction: 10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide = tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
For diagram of the late stages of purine biosynthesis, click here
Other name(s): 5-amino-4-imidazolecarboxamide ribonucleotide transformylase; AICAR transformylase; 10-formyltetrahydrofolate:5′-phosphoribosyl-5-amino-4-imidazolecarboxamide formyltransferase; 5′-phosphoribosyl-5-amino-4-imidazolecarboxamide formyltransferase; 5-amino-1-ribosyl-4-imidazolecarboxamide 5′-phosphate transformylase; 5-amino-4-imidazolecarboxamide ribotide transformylase; AICAR formyltransferase; aminoimidazolecarboxamide ribonucleotide transformylase
Systematic name: 10-formyltetrahydrofolate:5′-phosphoribosyl-5-amino-4-imidazole-carboxamide N-formyltransferase
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9032-03-5
References:
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]
[EC 2.1.2.3 created 1961, modified 2000]
 
 
EC 2.1.2.4     
Accepted name: glycine formimidoyltransferase
Reaction: 5-formimidoyltetrahydrofolate + glycine = tetrahydrofolate + N-formimidoylglycine
For diagram of reaction, click here
Other name(s): formiminoglycine formiminotransferase; FIG formiminotransferase; glycine formiminotransferase
Systematic name: 5-formimidoyltetrahydrofolate:glycine N-formimidoyltransferase
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, CAS registry number: 9029-84-9
References:
1.  Rabinowitz, J.C. and Pricer, W.E. Formiminotetrahydrofolic acid and methenyltetrahydrofolic acid as intermediates in the formation of N10-formyltetrahydrofolic acid. J. Am. Chem. Soc. 78 (1956) 5702–5704.
2.  Rabinowitz, J.C. and Pricer, W.E. Formation, isolation and properties of 5-formiminotetrahydrofolic acid. Fed. Proc. 16 (1957) 236.
3.  Sagers, R.D., Beck, J.V., Gruber, W. and Gunsalus, I.C. A tetrahydrofolic acid linked formimino transfer enzyme. J. Am. Chem. Soc. 78 (1956) 694–695.
[EC 2.1.2.4 created 1961, modified 2000]
 
 
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, Gene, 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)]
 
 
EC 2.1.2.6      
Deleted entry:  glutamate formyltransferase. Now included with EC 2.1.2.5, glutamate formimidoyltransferase
[EC 2.1.2.6 created 1965, deleted 1984]
 
 
EC 2.1.2.7     
Accepted name: D-alanine 2-hydroxymethyltransferase
Reaction: 5,10-methylenetetrahydrofolate + D-alanine + H2O = tetrahydrofolate + 2-methylserine
Other name(s): 2-methylserine hydroxymethyltransferase
Systematic name: 5,10-methylenetetrahydrofolate:D-alanine 2-hydroxymethyltransferase
Comments: Also acts on 2-hydroxymethylserine.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number: 9075-76-7
References:
1.  Wilson, E.M. and Snell, E.E. Metabolism of α-methylserine. I. α-Methylserine hydroxymethyltransferase. J. Biol. Chem. 237 (1962) 3171–3179. [PMID: 14001018]
[EC 2.1.2.7 created 1972]
 
 
EC 2.1.2.8     
Accepted name: deoxycytidylate 5-hydroxymethyltransferase
Reaction: 5,10-methylenetetrahydrofolate + H2O + deoxycytidylate = tetrahydrofolate + 5-hydroxymethyldeoxycytidylate
Other name(s): dCMP hydroxymethylase; d-cytidine 5′-monophosphate hydroxymethylase; deoxyCMP hydroxymethylase; deoxycytidylate hydroxymethylase; deoxycytidylic hydroxymethylase
Systematic name: 5,10-methylenetetrahydrofolate:deoxycytidylate 5-hydroxymethyltransferase
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9012-68-4
References:
1.  Mathews, C.K., Brown, F. and Cohen, S.S. Virus-induced acquisition of metabolic function. VII. Biosynthesis de novo of deoxycytidylate hydroxymethylase. J. Biol. Chem. 239 (1964) 2957–2963. [PMID: 14217882]
[EC 2.1.2.8 created 1972]
 
 
EC 2.1.2.9     
Accepted name: methionyl-tRNA formyltransferase
Reaction: 10-formyltetrahydrofolate + L-methionyl-tRNAfMet = tetrahydrofolate + N-formylmethionyl-tRNAfMet
For diagram of C1 metabolism, click here
Other name(s): N10-formyltetrahydrofolic-methionyl-transfer ribonucleic transformylase; formylmethionyl-transfer ribonucleic synthetase; methionyl ribonucleic formyltransferase; methionyl-tRNA Met formyltransferase; methionyl-tRNA transformylase; methionyl-transfer RNA transformylase; methionyl-transfer ribonucleate methyltransferase; methionyl-transfer ribonucleic transformylase
Systematic name: 10-formyltetrahydrofolate:L-methionyl-tRNA N-formyltransferase
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9015-76-3
References:
1.  Dickerman, H.W., Steers, E., Jr., Redfield, B.G. and Weissbach, H. Methionyl soluble ribonucleic acid transformylase. I. Purification and partial characterization. J. Biol. Chem. 242 (1967) 1522–1525. [PMID: 5337045]
[EC 2.1.2.9 created 1972, modified 2002, modified 2012]
 
 
EC 2.1.2.10     
Accepted name: aminomethyltransferase
Reaction: [protein]-S8-aminomethyldihydrolipoyllysine + tetrahydrofolate = [protein]-dihydrolipoyllysine + 5,10-methylenetetrahydrofolate + NH3
For diagram of the glycine-cleavage system, click here
Glossary: dihydrolipoyl group
Other name(s): S-aminomethyldihydrolipoylprotein:(6S)-tetrahydrofolate aminomethyltransferase (ammonia-forming); T-protein; glycine synthase; tetrahydrofolate aminomethyltransferase; [protein]-8-S-aminomethyldihydrolipoyllysine:tetrahydrofolate aminomethyltransferase (ammonia-forming)
Systematic name: [protein]-S8-aminomethyldihydrolipoyllysine:tetrahydrofolate aminomethyltransferase (ammonia-forming)
Comments: A component, with EC 1.4.4.2 glycine dehydrogenase (decarboxylating) and EC 1.8.1.4, dihydrolipoyl dehydrogenanse, of the glycine cleavage system, formerly known as glycine synthase. The glycine cleavage system is composed of four components that only loosely associate: the P protein (EC 1.4.4.2), the T protein (EC 2.1.2.10), the L protein (EC 1.8.1.4) and the lipoyl-bearing H protein [3].
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 37257-08-2
References:
1.  Okamura-Ikeda, K., Fujiwara, K. and Motokawa, Y. Purification and characterization of chicken liver T-protein, a component of the glycine cleavage system. J. Biol. Chem. 257 (1982) 135–139. [PMID: 7053363]
2.  Perham, R.N. Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions. Annu. Rev. Biochem. 69 (2000) 961–1004. [DOI] [PMID: 10966480]
3.  Nesbitt, N.M., Baleanu-Gogonea, C., Cicchillo, R.M., Goodson, K., Iwig, D.F., Broadwater, J.A., Haas, J.A., Fox, B.G. and Booker, S.J. Expression, purification, and physical characterization of Escherichia coli lipoyl(octanoyl)transferase. Protein Expr. Purif. 39 (2005) 269–282. [DOI] [PMID: 15642479]
[EC 2.1.2.10 created 1972, modified 2003, modified 2006]
 
 
EC 2.1.2.11     
Accepted name: 3-methyl-2-oxobutanoate hydroxymethyltransferase
Reaction: 5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = tetrahydrofolate + 2-dehydropantoate
For diagram of the early stages of CoA biosynthesis, click here
Other name(s): α-ketoisovalerate hydroxymethyltransferase; dehydropantoate hydroxymethyltransferase; ketopantoate hydroxymethyltransferase; oxopantoate hydroxymethyltransferase; 5,10-methylene tetrahydrofolate:α-ketoisovalerate hydroxymethyltransferase
Systematic name: 5,10-methylenetetrahydrofolate:3-methyl-2-oxobutanoate hydroxymethyltransferase
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 56093-17-5
References:
1.  Powers, S.G. and Snell, E.E. Ketopantoate hydroxymethyltransferase. II. Physical, catalytic, and regulatory properties. J. Biol. Chem. 251 (1976) 3786–3793. [PMID: 6463]
2.  Teller, J.H., Powers, S.G. and Snell, E.E. Ketopantoate hydroxymethyltransferase. I. Purification and role in pantothenate biosynthesis. J. Biol. Chem. 251 (1976) 3780–3785. [PMID: 776976]
[EC 2.1.2.11 created 1982]
 
 
EC 2.1.2.12      
Deleted entry:  now EC 2.1.1.74 methylenetetrahydrofolate-tRNA-(uracil-5-)-methyltransferase (FADH2-oxidizing)
[EC 2.1.2.12 created 1983, deleted 1984]
 
 
EC 2.1.2.13     
Accepted name: UDP-4-amino-4-deoxy-L-arabinose formyltransferase
Reaction: 10-formyltetrahydrofolate + UDP-4-amino-4-deoxy-β-L-arabinopyranose = 5,6,7,8-tetrahydrofolate + UDP-4-deoxy-4-formamido-β-L-arabinopyranose
For diagram of UDP-4-amino-4-deoxy-β-L-arabinose biosynthesis, click here
Other name(s): UDP-L-Ara4N formyltransferase; ArnAFT
Systematic name: 10-formyltetrahydrofolate:UDP-4-amino-4-deoxy-β-L-arabinose N-formyltransferase
Comments: The activity is part of a bifunctional enzyme also performing the reaction of EC 1.1.1.305 [UDP-glucuronic acid dehydrogenase (UDP-4-keto-hexauronic acid decarboxylating)].
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB
References:
1.  Breazeale, S.D., Ribeiro, A.A., McClerren, A.L. and Raetz, C.R.H. A formyltransferase required for polymyxin resistance in Escherichia coli and the modification of lipid A with 4-amino-4-deoxy-L-arabinose. Identification and function of UDP-4-deoxy-4-formamido-L-arabinose. J. Biol. Chem. 280 (2005) 14154–14167. [DOI] [PMID: 15695810]
2.  Gatzeva-Topalova, P.Z., May, A.P. and Sousa, M.C. Crystal structure and mechanism of the Escherichia coli ArnA (PmrI) transformylase domain. An enzyme for lipid A modification with 4-amino-4-deoxy-L-arabinose and polymyxin resistance. Biochemistry 44 (2005) 5328–5338. [DOI] [PMID: 15807526]
3.  Williams, G.J., Breazeale, S.D., Raetz, C.R.H. and Naismith, J.H. Structure and function of both domains of ArnA, a dual function decarboxylase and a formyltransferase, involved in 4-amino-4-deoxy-L-arabinose biosynthesis. J. Biol. Chem. 280 (2005) 23000–23008. [DOI] [PMID: 15809294]
4.  Gatzeva-Topalova, P.Z., May, A.P. and Sousa, M.C. Structure and mechanism of ArnA: conformational change implies ordered dehydrogenase mechanism in key enzyme for polymyxin resistance. Structure 13 (2005) 929–942. [DOI] [PMID: 15939024]
5.  Yan, A., Guan, Z. and Raetz, C.R.H. An undecaprenyl phosphate-aminoarabinose flippase required for polymyxin resistance in Escherichia coli. J. Biol. Chem. 282 (2007) 36077–36089. [DOI] [PMID: 17928292]
[EC 2.1.2.13 created 2010]
 
 
EC 2.1.2.14     
Accepted name: GDP-perosamine N-formyltransferase
Reaction: 10-formyltetrahydrofolate + GDP-α-D-perosamine = tetrahydrofolate + GDP-N-formyl-α-D-perosamine
Glossary: GDP-α-D-perosamine = GDP-4-amino-4,6-dideoxy-α-D-mannose
Other name(s): wbkC (gene name)
Systematic name: 10-formyltetrahydrofolate:GDP-α-D-perosamine N-formyltransferase
Comments: The enzyme, characterized from the bacterium Brucella melitensis, synthesizes a building block of the O antigen produced by Brucella species.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Godfroid, F., Cloeckaert, A., Taminiau, B., Danese, I., Tibor, A., de Bolle, X., Mertens, P. and Letesson, J.J. Genetic organisation of the lipopolysaccharide O-antigen biosynthesis region of Brucella melitensis 16M (wbk). Res. Microbiol. 151 (2000) 655–668. [DOI] [PMID: 11081580]
2.  Riegert, A.S., Chantigian, D.P., Thoden, J.B., Tipton, P.A. and Holden, H.M. Biochemical characterization of WbkC, an N-formyltransferase from Brucella melitensis. Biochemistry 56 (2017) 3657–3668. [DOI] [PMID: 28636341]
[EC 2.1.2.14 created 2021]
 
 


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