The Enzyme Database

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EC 2.3.1.4     
Accepted name: glucosamine-phosphate N-acetyltransferase
Reaction: acetyl-CoA + D-glucosamine 6-phosphate = CoA + N-acetyl-D-glucosamine 6-phosphate
For diagram of the biosynthesis of UDP-N-acetylglucosamine, click here
Other name(s): phosphoglucosamine transacetylase; phosphoglucosamine acetylase; glucosamine-6-phosphate acetylase; D-glucosamine-6-P N-acetyltransferase; aminodeoxyglucosephosphate acetyltransferase; glucosamine 6-phosphate acetylase; glucosamine 6-phosphate N-acetyltransferase; N-acetylglucosamine-6-phosphate synthase; phosphoglucosamine N-acetylase; glucosamine-6-phosphate N-acetyltransferase
Systematic name: acetyl-CoA:D-glucosamine-6-phosphate N-acetyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9031-91-8
References:
1.  Davidson, E.A. Glucosamine 6-phosphate N-acetylase. Methods Enzymol. 9 (1966) 704–707.
2.  Davidson, E.A., Blumenthal, H.J. and Roseman, F. Glucosamine metabolism. II. Studies of glucosamine 6-phosphate N-acetylase. J. Biol. Chem. 226 (1957) 125–133. [PMID: 13428743]
3.  Pattabiraman, T.N. and Bachhawat, B.K. Purification of glucosamine-6-phosphate N-acetylase from sheep brain. Biochim. Biophys. Acta 59 (1962) 681–689. [DOI] [PMID: 14484387]
4.  Boehmelt, G., Fialka, I., Brothers, G., McGinley, M.D., Patterson, S.D., Mo, R., Hui, C.C., Chung, S., Huber, L.A., Mak, T.W. and Iscove, N.N. Cloning and characterization of the murine glucosamine-6-phosphate acetyltransferase EMeg32. Differential expression and intracellular membrane association. J. Biol. Chem. 275 (2000) 12821–12832. [DOI] [PMID: 10777580]
[EC 2.3.1.4 created 1961, modified 2002]
 
 
EC 2.3.1.40     
Accepted name: acyl-[acyl-carrier-protein]—phospholipid O-acyltransferase
Reaction: an acyl-[acyl-carrier protein] + O-(2-acyl-sn-glycero-3-phospho)ethanolamine = an [acyl-carrier protein] + O-(1,2-diacyl-sn-glycero-3-phospho)ethanolamine
Other name(s): acyl-[acyl-carrier protein]:O-(2-acyl-sn-glycero-3-phospho)-ethanolamine O-acyltransferase
Systematic name: acyl-[acyl-carrier protein]:O-(2-acyl-sn-glycero-3-phospho)ethanolamine O-acyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37257-18-4
References:
1.  Taylor, S.S. and Heath, E.C. The incorporation of β-hydroxy fatty acids into a phospholipid of Escherichia coli B. J. Biol. Chem. 244 (1969) 6605–6616. [PMID: 4902888]
[EC 2.3.1.40 created 1972]
 
 
EC 2.3.1.41     
Accepted name: β-ketoacyl-[acyl-carrier-protein] synthase I
Reaction: an acyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein] = a 3-oxoacyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein]
Glossary: acyl-[acyl-carrier protein] = R-CO-[acyl-carrier protein]
malonyl-[acyl-carrier protein] = HOOC-CH2-CO-[acyl-carrier protein]
3-oxoacyl-[acyl-carrier protein] = R-CO-CH2-CO-[acyl-carrier protein]
Other name(s): β-ketoacyl-ACP synthase I; β-ketoacyl synthetase; β-ketoacyl-ACP synthetase; β-ketoacyl-acyl carrier protein synthetase; β-ketoacyl-[acyl carrier protein] synthase; β-ketoacylsynthase; condensing enzyme (ambiguous); 3-ketoacyl-acyl carrier protein synthase; fatty acid condensing enzyme; acyl-malonyl(acyl-carrier-protein)-condensing enzyme; acyl-malonyl acyl carrier protein-condensing enzyme; β-ketoacyl acyl carrier protein synthase; 3-oxoacyl-[acyl-carrier-protein] synthase; 3-oxoacyl:ACP synthase I; KASI; KAS I; FabF1; FabB; acyl-[acyl-carrier-protein]:malonyl-[acyl-carrier-protein] C-acyltransferase (decarboxylating)
Systematic name: acyl-[acyl-carrier protein]:malonyl-[acyl-carrier protein] C-acyltransferase (decarboxylating)
Comments: This enzyme is responsible for the chain-elongation step of dissociated (type II) fatty-acid biosynthesis, i.e. the addition of two C atoms to the fatty-acid chain. Escherichia coli mutants that lack this enzyme are deficient in unsaturated fatty acids. The enzyme can use fatty acyl thioesters of ACP (C2 to C16) as substrates, as well as fatty acyl thioesters of Co-A (C4 to C16) [4]. The substrate specificity is very similar to that of EC 2.3.1.179, β-ketoacyl-ACP synthase II, with the exception that the latter enzyme is far more active with palmitoleoyl-ACP (C16Δ9) as substrate, allowing the organism to regulate its fatty-acid composition with changes in temperature [4,5].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9077-10-5
References:
1.  Alberts, A.W., Majerus, P.W. and Vagelos, P.R. Acetyl-CoA acyl carrier protein transacylase. Methods Enzymol. 14 (1969) 50–53.
2.  Prescott, D.J. and Vagelos, P.R. Acyl carrier protein. Adv. Enzymol. Relat. Areas Mol. Biol. 36 (1972) 269–311. [PMID: 4561013]
3.  Toomey, R.E. and Wakil, S.J. Studies on the mechanism of fatty acid synthesis. XVI. Preparation and general properties of acyl-malonyl acyl carrier protein-condensing enzyme from Escherichia coli. J. Biol. Chem. 241 (1966) 1159–1165. [PMID: 5327099]
4.  D'Agnolo, G., Rosenfeld, I.S. and Vagelos, P.R. Multiple forms of β-ketoacyl-acyl carrier protein synthetase in Escherichia coli. J. Biol. Chem. 250 (1975) 5289–5294. [PMID: 237914]
5.  Garwin, J.L., Klages, A.L. and Cronan, J.E., Jr.. Structural, enzymatic, and genetic studies of β-ketoacyl-acyl carrier protein synthases I and II of Escherichia coli. J. Biol. Chem. 255 (1980) 11949–11956. [PMID: 7002930]
6.  Wang, H. and Cronan, J.E. Functional replacement of the FabA and FabB proteins of Escherichia coli fatty acid synthesis by Enterococcus faecalis FabZ and FabF homologues. J. Biol. Chem. 279 (2004) 34489–34495. [DOI] [PMID: 15194690]
7.  Cronan, J.E., Jr. and Rock, C.O. Biosynthesis of membrane lipids. In: Neidhardt, F.C. (Ed.), Escherichia coli and Salmonella: Cellular and Molecular Biology, 2nd edn, vol. 1, ASM Press, Washington, DC, 1996, pp. 612–636.
[EC 2.3.1.41 created 1972, modified 2006]
 
 
EC 2.3.1.42     
Accepted name: glycerone-phosphate O-acyltransferase
Reaction: acyl-CoA + glycerone phosphate = CoA + acylglycerone phosphate
Glossary: glycerone phosphate = dihydroxyacetone phosphate = 3-hydroxy-2-oxopropyl phosphate
Other name(s): dihydroxyacetone phosphate acyltransferase
Systematic name: acyl-CoA:glycerone-phosphate O-acyltransferase
Comments: A membrane protein. Uses CoA derivatives of palmitate, stearate and oleate, with highest activity on palmitoyl-CoA.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37257-19-5
References:
1.  Ballas, L.M. and Bell, R.M. Topography of glycerolipid synthetic enzymes. Synthesis of phosphatidylserine, phosphatidylinositol and glycerolipid intermediates occurs on the cytoplasmic surface of rat liver microsomal vesicles. Biochim. Biophys. Acta 665 (1981) 586–595. [DOI] [PMID: 6271231]
2.  Declercq, P.E., Haagsman, H.P., Van Veldhoven, P., Debeer, L.J., Van Golde, L.M.G. and Mannaerts, G.P. Rat liver dihydroxyacetone-phosphate acyltransferases and their contribution to glycerolipid synthesis. J. Biol. Chem. 259 (1984) 9064–9075. [PMID: 6746639]
3.  Hajra, A.K. Biosynthesis of acyl dihydroxyacetone phosphate in guinea pig liver mitochondria. J. Biol. Chem. 243 (1968) 3458–3465. [PMID: 5656381]
[EC 2.3.1.42 created 1972]
 
 
EC 2.3.1.43     
Accepted name: phosphatidylcholine—sterol O-acyltransferase
Reaction: phosphatidylcholine + a sterol = 1-acylglycerophosphocholine + a sterol ester
Other name(s): lecithin—cholesterol acyltransferase; phospholipid—cholesterol acyltransferase; LCAT (lecithin-cholesterol acyltransferase); lecithin:cholesterol acyltransferase; lysolecithin acyltransferase
Systematic name: phosphatidylcholine:sterol O-acyltransferase
Comments: Palmitoyl, oleoyl and linoleoyl residues can be transferred; a number of sterols, including cholesterol, can act as acceptors. The bacterial enzyme also catalyses the reactions of EC 3.1.1.4 phospholipase A2 and EC 3.1.1.5 lysophospholipase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9031-14-5
References:
1.  Bartlett, K., Keat, M.J. and Mercer, E.I. Biosynthesis of sterol esters in Phycomyces blakesleeanus. Phytochemistry 13 (1974) 1107–1113.
2.  Buckley, J.T., Halasa, L.N. and Macintyre, S. Purification and partial characterization of a bacterial phospholipid: cholesterol acyltransferase. J. Biol. Chem. 257 (1982) 3320–3325. [PMID: 7061477]
3.  Glomset, J.A.J. The plasma lecithins:cholesterol acyltransferase reaction. Lipid Res. 9 (1968) 155–167. [PMID: 4868699]
4.  Vahouny, G.V. and Tradwell, C.R. Enzymatic synthesis and hydrolysis of cholesterol esters. Methods Biochem. Anal. 16 (1968) 219–272. [PMID: 4877146]
[EC 2.3.1.43 created 1972, modified 1976]
 
 
EC 2.3.1.44     
Accepted name: N-acetylneuraminate 4-O-acetyltransferase
Reaction: acetyl-CoA + N-acetylneuraminate = CoA + N-acetyl-4-O-acetylneuraminate
Other name(s): sialate O-acetyltransferase
Systematic name: acetyl-CoA:N-acetylneuraminate 4-O-acetyltransferase
Comments: Both free and glycosidically bound N-acetyl- and N-glycolyl- neuraminates can act as O-acetyl acceptors.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 51004-25-2
References:
1.  Schauer, R. Biosynthese von N-Acetyl-O-acetylneuraminsaüren. I. Inkorporation von [14C]Acetate in Schnitte der Unterkieferspeicheldrüse von Rind und Pferd. Hoppe-Seyler's Z. Physiol. Chem. 351 (1970) 595–602. [PMID: 5446640]
2.  Schauer, R. Biosynthese von N-Acetyl-O-acetylneuraminsaüren. II. Untersuchungen über Substrat und intracelluläre Lokalisation der Acetyl-coenzym A: N-acetylneuraminat-7- and 8-O-acetyltransferase von Rind. Hoppe-Seyler's Z. Physiol. Chem. 351 (1970) 749–758. [PMID: 5425947]
[EC 2.3.1.44 created 1972]
 
 
EC 2.3.1.45     
Accepted name: N-acetylneuraminate 7-O(or 9-O)-acetyltransferase
Reaction: acetyl-CoA + N-acetylneuraminate = CoA + N-acetyl-7-O(or 9-O)-acetylneuraminate
Other name(s): N-acetylneuraminate 7(8)-O-acetyltransferase; sialate O-acetyltransferase; N-acetylneuraminate 7,8-O-acetyltransferase; acetyl-CoA:N-acetylneuraminate-7- or 8-O-acetyltransferase; acetyl-CoA:N-acetylneuraminate-7- and/or 8-O-acetyltransferase; glycoprotein 7(9)-O-acetyltransferase; acetyl-CoA:N-acetylneuraminate-9(7)-O-acetyltransferase; N-acetylneuraminate O7-(or O9-)acetyltransferase; acetyl-CoA:N-acetylneuraminate-9(or 7)-O-acetyltransferase
Systematic name: acetyl-CoA:N-acetylneuraminate 7-O(or 9-O)-acetyltransferase
Comments: Both free and glycosidically bound N-acetyl- and N-glycolylneuraminates can act as O-acetyl acceptors.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9054-50-6
References:
1.  Schauer, R. Biosynthese von N-Acetyl-O-acetylneuraminsaüren. I. Inkorporation von [14C]Acetate in Schnitte der Unterkieferspeicheldrüse von Rind und Pferd. Hoppe-Seyler's Z. Physiol. Chem. 351 (1970) 595–602. [PMID: 5446640]
2.  Schauer, R. Biosynthese von N-Acetyl-O-acetylneuraminsaüren. II. Untersuchungen über Substrat und intracelluläre Lokalisation der Acetyl-coenzym A: N-acetylneuraminat-7- and 8-O-acetyltransferase von Rind. Hoppe-Seyler's Z. Physiol. Chem. 351 (1970) 749–758. [PMID: 5425947]
[EC 2.3.1.45 created 1972]
 
 
EC 2.3.1.46     
Accepted name: homoserine O-succinyltransferase
Reaction: succinyl-CoA + L-homoserine = CoA + O-succinyl-L-homoserine
For diagram of L-Methionine biosynthesis, click here
Other name(s): homoserine O-transsuccinylase; homoserine succinyltransferase
Systematic name: succinyl-CoA:L-homoserine O-succinyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 62213-51-8
References:
1.  Rowbury, R.J. and Woods, D.D. O-Succinylhomoserine as an intermediate in the synthesis of cystathionine by Escherichia coli. J. Gen. Microbiol. 36 (1964) 341–358. [PMID: 14217349]
[EC 2.3.1.46 created 1976]
 
 
EC 2.3.1.47     
Accepted name: 8-amino-7-oxononanoate synthase
Reaction: pimeloyl-[acyl-carrier protein] + L-alanine = 8-amino-7-oxononanoate + CO2 + holo-[acyl-carrier protein]
Glossary: pimeloyl-[acyl-carrier protein] = 6-carboxyhexanoyl-[acyl-carrier protein]
Other name(s): 7-keto-8-aminopelargonic acid synthetase; 7-keto-8-aminopelargonic synthetase; 8-amino-7-oxopelargonate synthase; bioF (gene name)
Systematic name: 6-carboxyhexanoyl-[acyl-carrier protein]:L-alanine C-carboxyhexanoyltransferase (decarboxylating)
Comments: A pyridoxal-phosphate protein. The enzyme catalyses the decarboxylative condensation of L-alanine and pimeloyl-[acyl-carrier protein], a key step in the pathway for biotin biosynthesis. Pimeloyl-CoA can be used with lower efficiency [5].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9075-61-0
References:
1.  Eisenberg, M.A. and Star, C. Synthesis of 7-oxo-8-aminopelargonic acid, a biotin vitamer, in cell-free extracts of Escherichia coli biotin auxotrophs. J. Bacteriol. 96 (1968) 1291–1297. [PMID: 4879561]
2.  Alexeev, D., Alexeeva, M., Baxter, R.L., Campopiano, D.J., Webster, S.P. and Sawyer, L. The crystal structure of 8-amino-7-oxononanoate synthase: a bacterial PLP-dependent, acyl-CoA-condensing enzyme. J. Mol. Biol. 284 (1998) 401–419. [DOI] [PMID: 9813126]
3.  Ploux, O., Breyne, O., Carillon, S. and Marquet, A. Slow-binding and competitive inhibition of 8-amino-7-oxopelargonate synthase, a pyridoxal-5′-phosphate-dependent enzyme involved in biotin biosynthesis, by substrate and intermediate analogs. Kinetic and binding studies. Eur. J. Biochem. 259 (1999) 63–70. [PMID: 9914476]
4.  Webster, S.P. , Alexeev. D., Campopiano, D.J., Watt, R.M., Alexeeva, M., Sawyer, L. and Baxter, R. Mechanism of 8-amino-7-oxononanoate synthase: spectroscopic, kinetic, and crystallographic studies. Biochemistry 39 (2000) 516–528. [DOI] [PMID: 10642176]
5.  Lin, S., Hanson, R.E. and Cronan, J.E. Biotin synthesis begins by hijacking the fatty acid synthetic pathway. Nat. Chem. Biol. 6 (2010) 682–688. [DOI] [PMID: 20693992]
[EC 2.3.1.47 created 1976, modified 2013]
 
 
EC 2.3.1.48     
Accepted name: histone acetyltransferase
Reaction: acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N6-acetyl-L-lysine
Other name(s): nucleosome-histone acetyltransferase; histone acetokinase; histone acetylase; histone transacetylase; lysine acetyltransferase; protein lysine acetyltransferase; acetyl-CoA:histone acetyltransferase
Systematic name: acetyl-CoA:[protein]-L-lysine acetyltransferase
Comments: A group of enzymes acetylating histones. Several of the enzymes can also acetylate lysines in other proteins [3,4].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9054-51-7
References:
1.  Gallwitz, D. and Sures, I. Histone acetylation. Purification and properties of three histone-specific acetyltransferases from rat thymus nuclei. Biochim. Biophys. Acta 263 (1972) 315–328. [DOI] [PMID: 5031160]
2.  Makowski, A.M., Dutnall, R.N. and Annunziato, A.T. Effects of acetylation of histone H4 at lysines 8 and 16 on activity of the Hat1 histone acetyltransferase. J. Biol. Chem. 276 (2001) 43499–43502. [DOI] [PMID: 11585814]
3.  Lee, K.K. and Workman, J.L. Histone acetyltransferase complexes: one size doesn’t fit all. Nat. Rev. Mol. Cell. Biol. 8 (2007) 284–295. [DOI] [PMID: 17380162]
4.  Thao, S. and Escalante-Semerena, J.C. Biochemical and thermodynamic analyses of Salmonella enterica Pat, a multidomain, multimeric Nε-lysine acetyltransferase involved in carbon and energy metabolism. MBio 2 (2011) E216. [DOI] [PMID: 22010215]
5.  Wu, H., Moshkina, N., Min, J., Zeng, H., Joshua, J., Zhou, M.M. and Plotnikov, A.N. Structural basis for substrate specificity and catalysis of human histone acetyltransferase 1. Proc. Natl. Acad. Sci. USA 109 (2012) 8925–8930. [DOI] [PMID: 22615379]
6.  Das, C., Roy, S., Namjoshi, S., Malarkey, C.S., Jones, D.N., Kutateladze, T.G., Churchill, M.E. and Tyler, J.K. Binding of the histone chaperone ASF1 to the CBP bromodomain promotes histone acetylation. Proc. Natl. Acad. Sci. USA 111 (2014) E1072–E1081. [DOI] [PMID: 24616510]
[EC 2.3.1.48 created 1976, modified 2017]
 
 
EC 2.3.1.49     
Accepted name: deacetyl-[citrate-(pro-3S)-lyase] S-acetyltransferase
Reaction: S-acetylphosphopantetheine + holo-[citrate (pro-3S)-lyase] = phosphopantetheine + acetyl-[citrate (pro-3S)-lyase]
Other name(s): S-acetyl phosphopantetheine:deacetyl citrate lyase S-acetyltransferase; deacetyl-[citrate-(pro-3S)-lyase] acetyltransferase; S-acetylphosphopantetheine:deacetyl-[citrate-oxaloacetate-lyase((pro-3S)-CH2COO-→acetate)] S-acetyltransferase
Systematic name: S-acetylphosphopantetheine:holo-[citrate (pro-3S)-lyase] S-acetyltransferase
Comments: Both this enzyme and EC 6.2.1.22, [citrate (pro-3S)-lyase] ligase, acetylate and activate EC 4.1.3.6, citrate (pro-3S)-lyase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 42616-18-2
References:
1.  Singh, M., Böttger, B., Brooks, G.C. and Srere, P.A. S-Acetyl phosphopantetheine: deacetyl citrate lyase S-acetyl transferase from Klebsiella aerogenes. Biochem. Biophys. Res. Commun. 53 (1973) 1–9. [DOI] [PMID: 4741546]
[EC 2.3.1.49 created 1976]
 
 


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