The Enzyme Database

Your query returned 5 entries.    printer_iconPrintable version



EC 2.1.2.1     
Accepted name: glycine hydroxymethyltransferase
Reaction: 5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
For diagram of folate-coenzyme interconversions, click here
Other name(s): serine aldolase; threonine aldolase; serine hydroxymethylase; serine hydroxymethyltransferase; allothreonine aldolase; L-serine hydroxymethyltransferase; L-threonine aldolase; serine hydroxymethyltransferase; 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, 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 2.1.2.10     
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, KEGG, MetaCyc, PDB, CAS registry number: 37257-08-2
References:
1.  Okamura-Ikeda, J., 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, 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, KEGG, MetaCyc
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]
 
 


Data © 2001–2018 IUBMB
Web site © 2005–2018 Andrew McDonald