EC 2.3.1 Transferring groups other than amino-acyl groups
EC 2.3.2 Aminoacyltransferases
('Acetyltransferase', etc. may be replaced by 'transacetylase' etc.)
See separate file for EC 2.3.1.51 to EC 2.3.1.100, EC 2.3.1.101 to EC 2.3.1.150, EC 2.3.1.151 to EC 2.3.1.200 and EC 2.3.1.201 to EC 2.3.1.328
EC 2.3.1.51 to EC 2.3.1.100
EC 2.3.1.101 to EC 2.3.1.150
EC 2.3.1.151 to EC 2.3.1.200
EC 2.3.1.200 to EC 2.3.1.328
Accepted name: amino-acid N-acetyltransferase
Reaction: acetyl-CoA + L-glutamate = CoA + N-acetyl-L-glutamate
For diagram click here.
Other name(s): N-acetylglutamate synthase; AGAS; acetylglutamate acetylglutamate synthetase; acetylglutamic synthetase; amino acid acetyltransferase; N-acetyl-L-glutamate synthetase; N-acetylglutamate synthetase
Systematic name: acetyl-CoA:L-glutamate N-acetyltransferase
Comments: Also acts with L-aspartate and, more slowly, with some other amino acids.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9029-88-3
References:
1. Maas, W.K., Novelli, G.D. and Lipmann, F. Acetylation of glutamic acid by extracts of Escherichia coli. Proc. Natl. Acad. Sci. USA 39 (1953) 1004-1008.
Accepted name: imidazole N-acetyltransferase
Reaction: acetyl-CoA + imidazole = CoA + N-acetylimidazole
Other name(s): imidazole acetylase; imidazole acetyltransferase
Systematic name: acetyl-CoA:imidazole N-acetyltransferase
Comments: Also acts with propanoyl-CoA.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, CAS registry number: 9029-89-4
References:
1. Kinsky, S.C. Assay, purification, and properties of imidazole acetylase. J. Biol. Chem. 235 (1960) 94-98.
Accepted name: glucosamine N-acetyltransferase
Reaction: acetyl-CoA + D-glucosamine = CoA + N-acetyl-D-glucosamine
Other name(s): glucosamine acetylase; glucosamine acetyltransferase
Systematic name: acetyl-CoA:D-glucosamine N-acetyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9032-94-4
References:
1. Chou, T.C. and Soodak, M. The acetylation of D-glucosamine by pigeon liver extracts. J. Biol. Chem. 196 (1952) 105-109.
Accepted name: glucosamine-phosphate N-acetyltransferase
Reaction: acetyl-CoA + D-glucosamine 6-phosphate = CoA + N-acetyl-D-glucosamine 6-phosphate
For diagram 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.
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.
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. [PMID: 10777580]
Accepted name: arylamine N-acetyltransferase
Reaction: acetyl-CoA + an arylamine = CoA + an N-acetylarylamine
Other name(s): arylamine acetylase; β-naphthylamine N-acetyltransferase; 4-aminobiphenyl N-acetyltransferase; acetyl CoA-arylamine N-acetyltransferase; 2-naphthylamine N-acetyltransferase; arylamine acetyltransferase; indoleamine N-acetyltransferase; N-acetyltransferase (ambiguous); p-aminosalicylate N-acetyltransferase; serotonin acetyltransferase; serotonin N-acetyltransferase
Systematic name: acetyl-CoA:arylamine N-acetyltransferase
Comments: Wide specificity for aromatic amines, including serotonin; also catalyses acetyl-transfer between arylamines without CoA.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9027-33-2
References:
1. Chou, T.C. and Lipmann, F. Separation of acetyl transfer enzymes in pigeon liver extract. J. Biol. Chem. 196 (1952) 89-103.
2. Paul, R.C. and Ratledge, C. Further studies on anthranilate N-acetylanthranilic acid in Aerobacter aerogenes. Biochim. Biophys. Acta 320 (1973) 9-15.
3. Tabor, H., Mehler, A.H. and Stadtman, E.R. The enzymatic acetylation of amines. J. Biol. Chem. 204 (1953) 127-138.
4. Weissbach, H., Redfield, B.G. and Axelrod, J. The enzymic acetylation of serotonin and other naturally occurring amines. Biochim. Biophys. Acta 54 (1961) 190-192.
Accepted name: choline O-acetyltransferase
Reaction: acetyl-CoA + choline = CoA + O-acetylcholine
Other name(s): choline acetylase; choline acetyltransferase
Systematic name: acetyl-CoA:choline O-acetyltransferase
Comments: Propanoyl-CoA can act, more slowly, in place of acetyl-CoA.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9012-78-6
References:
1. Berman, R., Wilson, I.B. and Nachmansohn, D. Choline acetylase specificity in relation to biological function. Biochim. Biophys. Acta 12 (1953) 315-324.
2. Berry, J.F. and Whittaker, V.P. The acyl-group specificity of choline acetylase. Biochem. J. 73 (1959) 447-458.
3. Fritz, I.B. and Schultz, S.K. Carnitine acetyltransferase. II. Inhibition by carnitine analogues and by sulfhydryl reagents. J. Biol. Chem. 240 (1965) 2188-2192.
4. Schuberth, J. Choline acetyltransferase. Purification and effect of salts on the mechanism of the enzyme-catalysed reaction. Biochim. Biophys. Acta 122 (1966) 470-481.
Accepted name: carnitine O-acetyltransferase
Reaction: acetyl-CoA + carnitine = CoA + O-acetylcarnitine
Other name(s): acetyl-CoA-carnitine O-acetyltransferase; acetylcarnitine transferase; carnitine acetyl coenzyme A transferase; carnitine acetylase; carnitine acetyltransferase; carnitine-acetyl-CoA transferase; CATC
Systematic name: acetyl-CoA:carnitine O-acetyltransferase
Comments: Also acts on propanoyl-CoA and butanoyl-CoA (cf. EC 2.3.1.21 carnitine O-palmitoyltransferase and EC 2.3.1.137 carnitine O-octanoyltransferase).
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9029-90-7
References:
1. Chase, J.F.A., Pearson, D.J. and Tubbs, P.K. The preparation of crystalline carnitine acetyltransferase. Biochim. Biophys. Acta 96 (1965) 162-165.
2. Friedman, S. and Fraenkel, G. Reversible enzymatic acetylation of carnitine. Arch. Biochem. Biophys. 59 (1955) 491-501.
3. Miyazawa, S., Ozasa, H., Furuta, S., Osumi, T. and Hashimoto, T. Purification and properties of carnitine acetyl transferase from rat liver. J. Biochem. (Tokyo) 93 (1983) 439-451.
Accepted name: phosphate acetyltransferase
Reaction: acetyl-CoA + phosphate = CoA + acetyl phosphate
Other name(s): phosphotransacetylase; phosphoacylase; PTA
Systematic name: acetyl-CoA:phosphate acetyltransferase
Comments: Also acts with other short-chain acyl-CoAs.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9029-91-8
References:
1. Bergmeyer, H.U., Holz, G., Klotzsch, H. and Lang, G. Phosphotransacetylase aus Clostridium kluyveri. Züchtung des Bacteriums, Isolierung, Krystallisation und Eigenschaften des Enzyms. Biochem. Z. 338 (1963) 114-121.
2. Stadtman, E.R. The purification and properties of phosphotransacetylase. J. Biol. Chem. 196 (1952) 527-534.
3. Stadtman, E.R. Phosphotransacetylase from Clostridium kluyveri. Methods Enzymol. 1 (1955) 596-599.
Accepted name: acetyl-CoA C-acetyltransferase
Reaction: 2 acetyl-CoA = CoA + acetoacetyl-CoA (overall reaction)
(1a) acetyl-CoA + [acetyl-CoA C-acetyltransferase]-L-cysteine = [acetyl-CoA C-acetyltransferase]-S-acetyl-L-cysteine + CoA
(1b) [acetyl-CoA C-acetyltransferase]-S-acetyl-L-cysteine + acetyl-CoA = acetoacetyl-CoA + [acetyl-CoA C-acetyltransferase]-L-cysteine
For diagram of the reaction click here or click here
Other name(s): acetoacetyl-CoA thiolase; β-acetoacetyl coenzyme A thiolase; 2-methylacetoacetyl-CoA thiolase [misleading]; 3-oxothiolase; acetyl coenzyme A thiolase; acetyl-CoA acetyltransferase; acetyl-CoA:N-acetyltransferase; thiolase II; type II thiolase
Systematic name: acetyl-CoA:acetyl-CoA C-acetyltransferase
Comments: The enzyme, found in both eukaryotes and prokaryotes, catalyses the Claisen condensation of an acetyl-CoA and an acyl-CoA (often another acetyl-CoA), leading to the formation of an acyl-CoA that is longer by two carbon atoms. The reaction starts with the acylation of a nucleophilic cysteine at the active site, usually by acetyl-CoA but potentially by a different acyl-CoA, with concomitant release of CoA. In the second step the acyl group is transferred to an acetyl-CoA molecule. cf. EC 2.3.1.16, acetyl-CoA C-acyltransferase.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9027-46-7
References:
1. Lynen, F. and Ochoa, S. Enzymes of fatty acid metabolism. Biochim. Biophys. Acta 12 (1953) 299-314. [PMID: 13115439]
2. Stern, J.R., Drummond, G.I., Coon, M.J. and del Campillo, A. Enzymes of ketone body metabolism. I. Purification of an acetoacetate-synthesizing enzyme from ox liver. J. Biol. Chem. 235 (1960) 313-317. [PMID: 13834445]
Accepted name: hydrogen-sulfide S-acetyltransferase
Reaction: acetyl-CoA + hydrogen sulfide = CoA + thioacetate
Other name(s): hydrogen-sulfide acetyltransferase
Systematic name: acetyl-CoA:hydrogen-sulfide S-acetyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9029-92-9
References:
1. Brady, R.O. and Stadtman, E.R. Enzymatic thioltransacetylation. J. Biol. Chem. 211 (1954) 621-629.
Accepted name: thioethanolamine S-acetyltransferase
Reaction: acetyl-CoA + 2-aminoethanethiol = CoA + S-(2-aminoethyl)thioacetate
Other name(s): thioltransacetylase B; thioethanolamine acetyltransferase; acetyl-CoA:thioethanolamine S-acetyltransferase
Systematic name: acetyl-CoA:2-aminoethanethiol S-acetyltransferase
Comments: 2-Sulfanylethanol (2-mercaptoethanol) can act as a substrate [1].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9029-93-0
References:
1. Brady, R.O. and Stadtman, E.R. Enzymatic thioltransacetylation. J. Biol. Chem. 211 (1954) 621-629. [PMID: 13221570]
2. Gunsalus, I.C. Group transfer and acyl-generating functions of lipoic acid derivatives. In: McElroy, W.D. and Glass, B. (Ed.), A Symposium on the Mechanism of Enzyme Action, vol. , Johns Hopkins Press, Baltimore, 1954, pp. 545-580.
Accepted name: dihydrolipoyllysine-residue acetyltransferase
Reaction: acetyl-CoA + enzyme N6-(dihydrolipoyl)lysine = CoA + enzyme N6-(S-acetyldihydrolipoyl)lysine
For diagram of reaction click here.
Glossary: dihydrolipoyl group
Other name(s): acetyl-CoA:dihydrolipoamide S-acetyltransferase; dihydrolipoamide S-acetyltransferase; dihydrolipoate acetyltransferase; dihydrolipoic transacetylase; dihydrolipoyl acetyltransferase; lipoate acetyltransferase; lipoate transacetylase; lipoic acetyltransferase; lipoic acid acetyltransferase; lipoic transacetylase; lipoylacetyltransferase; thioltransacetylase A; transacetylase X
Systematic name: acetyl-CoA:enzyme-N6-(dihydrolipoyl)lysine S-acetyltransferase
Comments: A multimer (24-mer or 60-mer, depending on the source) of this enzyme forms the core of the pyruvate dehydrogenase multienzyme complex, and binds tightly both EC 1.2.4.1, pyruvate dehydrogenase (acetyl-transferring) and EC 1.8.1.4, dihydrolipoyl dehydrogenase. The lipoyl group of this enzyme is reductively acetylated by EC 1.2.4.1, and the only observed direction catalysed by EC 2.3.1.12 is that where the acetyl group is passed to coenzyme A.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9032-29-5
References:
1. Brady, R.O. and Stadtman, E.R. Enzymatic thioltransacetylation. J. Biol. Chem. 211 (1954) 621-629.
2. Gunsalus, I.C. Group transfer and acyl-generating functions of lipoic acid derivatives. In: McElroy, W.D. and Glass, B. (Eds.), A Symposium on the Mechanism of Enzyme Action Johns Hopkins Press, Baltimore, 1954, pp. 545-480.
3. Gunsalus, I.C., Barton, L.S. and Gruber, W. Biosynthesis and structure of lipoic acid derivatives. J. Am. Chem. Soc. 78 (1956) 1763-1766.
4. Perham, R.N. Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions. Annu. Rev. Biochem. 69 (2000) 961-1004. [PMID: 10966480]
Accepted name: ATP carbamoyltransferase
Accepted name: glycine N-acyltransferase
Reaction: acyl-CoA + glycine = CoA + N-acylglycine
Other name(s): glycine acyltransferase; glycine-N-acylase
Systematic name: acyl-CoA:glycine N-acyltransferase
Comments: The CoA derivatives of a number of aliphatic and aromatic acids, but not phenylacetyl-CoA or (indol-3-yl)acetyl-CoA, can act as donor. Not identical with EC 2.3.1.68 glutamine N-acyltransferase or EC 2.3.1.71 glycine N-benzoyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9029-95-2
References:
1. Nandi, D.L., Lucas, S.V. and Webster, L.T. Benzoyl-coenzyme A:glycine N-acyltransferase and phenylacetyl-coenzyme A:glycine N-acyltransferase from bovine liver mitochondria. Purification and characterization. J. Biol. Chem. 254 (1979) 7230-7237. [PMID: 457678]
2. Schachter, D. and Taggart, J.V. Glycine N-acylase: purification and properties. J. Biol. Chem. 208 (1954) 263-275. [PMID: 13174534]
3. Webster, L.T., Jr., Siddiqui, U.A., Lucas, S.V., Strong, J.M. and Mieyal, J.J. Identification of N-acyltransferase activities in mitochondrial fractions from liver of rhesus monkey and man. J. Biol. Chem. 251 (1976) 3352-3358. [PMID: 931988]
Accepted name: glutamine N-phenylacetyltransferase
Reaction: phenylacetyl-CoA + L-glutamine = CoA + α-N-phenylacetyl-L-glutamine
Other name(s): glutamine phenylacetyltransferase; phenylacetyl-CoA:L-glutamine N-acetyltransferase
Systematic name: phenylacetyl-CoA:L-glutamine α-N-phenylacetyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9030-00-6
References:
1. Moldave, K. and Meister, A. Synthesis of phenylacetylglutamine by human tissue. J. Biol. Chem. 229 (1957) 463-476.
Accepted name: glycerol-3-phosphate 1-O-acyltransferase
Reaction: acyl-CoA + sn-glycerol 3-phosphate = CoA + 1-acyl-sn-glycerol 3-phosphate
Other name(s): α-glycerophosphate acyltransferase; 3-glycerophosphate acyltransferase; ACP:sn-glycerol-3-phosphate acyltransferase; glycerol 3-phosphate acyltransferase; glycerol phosphate acyltransferase; glycerol phosphate transacylase; glycerophosphate acyltransferase; glycerophosphate transacylase; sn-glycerol 3-phosphate acyltransferase; sn-glycerol-3-phosphate acyltransferase; glycerol-3-phosphate O-acyltransferase (ambiguous)
Systematic name: Acyl-CoA:sn-glycerol-3-phosphate 1-O-acyltransferase
Comments: acyl-[acyl-carrier protein] can also act as acyl donor. The enzyme acts only on derivatives of fatty acids of chain length above C10
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9029-96-3
References:
1. Bertrams, M. and Heinz, E. Positional specificity and fatty-acid selectivity of purified sn-glycerol 3-phosphate acyltransferases from chloroplasts. Plant Physiol. 68 (1981) 653-657.
2. Frentzen, M., Heinz, E., McKeon, T.A. and Stumpf, P.K. Specificities and selectivities of glycerol-3-phosphate acyltransferase and monoacylglycerol-3-phosphate acyltransferase from pea and spinach chloroplasts. Eur. J. Biochem. 129 (1983) 629-636. [PMID: 6825679]
3. Green, P.R., Merrill, A.H. and Bell, R.M. Membrane phospholipid synthesis in Escherichia coli. Purification, reconstitution, and characterization of sn-glycerol-3-phosphate acyltransferase. J. Biol. Chem. 256 (1981) 11151-11159. [PMID: 6350296]
4. Yamashita, S. and Numa, N. Partial purification and properties of glycerophosphate acyltransferase from rat liver. Formation of 1-acylglycerol 3-phosphate from sn-glycerol 3-phosphate and palmityl coenzyme A. Eur. J. Biochem. 31 (1972) 565-573. [PMID: 4650158]
Accepted name: acetyl-CoA C-acyltransferase
Reaction: acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA (overall reaction)
(1a) [acetyl-CoA C-acyltransferase]-S-acyl-L-cysteine + acetyl-CoA = 3-oxoacyl-CoA + [acetyl-CoA C-acyltransferase]-L-cysteine
(1b) acyl-CoA + [acetyl-CoA C-acyltransferase]-L-cysteine = [acetyl-CoA C-acyltransferase]-S-acyl-L-cysteine + CoA
For diagram of reaction click here or click here
Other name(s): β-ketothiolase; 3-ketoacyl-CoA thiolase; KAT; β-ketoacyl coenzyme A thiolase; β-ketoacyl-CoA thiolase; β-ketoadipyl coenzyme A thiolase; β-ketoadipyl-CoA thiolase; 3-ketoacyl CoA thiolase; 3-ketoacyl coenzyme A thiolase; 3-ketoacyl thiolase; 3-ketothiolase; 3-oxoacyl-CoA thiolase; 3-oxoacyl-coenzyme A thiolase; 6-oxoacyl-CoA thiolase; acetoacetyl-CoA β-ketothiolase; acetyl-CoA acyltransferase; ketoacyl-CoA acyltransferase; ketoacyl-coenzyme A thiolase; long-chain 3-oxoacyl-CoA thiolase; oxoacyl-coenzyme A thiolase; pro-3-ketoacyl-CoA thiolase; thiolase I; type I thiolase; 2-methylacetoacetyl-CoA thiolase [misleading]
Systematic name: acyl-CoA:acetyl-CoA C-acyltransferase
Comments: The enzyme, found in both eukaryotes and in prokaryotes, is involved in degradation pathways such as fatty acid β-oxidation. The enzyme acts on 3-oxoacyl-CoAs to produce acetyl-CoA and an acyl-CoA shortened by two carbon atoms. The reaction starts with the acylation of a nucleophilic cysteine at the active site by a 3-oxoacyl-CoA, with the concomitant release of acetyl-CoA. In the second step the acyl group is transferred to CoA. Most enzymes have a broad substrate range for the 3-oxoacyl-CoA. cf. EC 2.3.1.9, acetyl-CoA C-acetyltransferase.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9029-97-4
References:
1. Beinert, H., Bock, R.M., Goldman, D.S., Green, D.E., Mahler, H.R., Mii, S., Stansly, P.G. and Wakil, S.J. A synthesis of dl-cortisone acetate. J. Am. Chem. Soc. 75 (1953) 4111-4112.
2. Goldman, D.S. Studies on the fatty acid oxidizing system of animal tissue. VII. The β-ketoacyl coenzyme A cleavage enzyme. J. Biol. Chem. 208 (1954) 345-357. [PMID: 13174544]
3. Stern, J.R., Coon, M.J. and del Campillo, A. Enzymatic breakdown and synthesis of acetoacetate. Nature 171 (1953) 28-30. [PMID: 13025466]
Accepted name: aspartate N-acetyltransferase
Reaction: acetyl-CoA + L-aspartate = CoA + N-acetyl-L-aspartate
Other name(s): aspartate acetyltransferase; L-aspartate N-acetyltransferase
Systematic name: acetyl-CoA:L-aspartate N-acetyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9029-99-6
References:
1. Goldstein, F.B. Biosynthesis of N-acetyl-L-aspartic acid. J. Biol. Chem. 234 (1959) 2702-2706.
2. Knizley, H., Jr. The enzymatic synthesis of N-acetyl-L-aspartic acid by a water-insoluble preparation of a cat brain acetone powder. J. Biol. Chem. 242 (1967) 4619-4622. [PMID: 6061408]
Accepted name: galactoside O-acetyltransferase
Reaction: acetyl-CoA + a β-D-galactoside = CoA + a 6-acetyl-β-D-galactoside
Other name(s): thiogalactoside acetyltransferase; galactoside acetyltransferase; thiogalactoside transacetylase
Systematic name: acetyl-CoA:β-D-galactoside 6-acetyltransferase
Comments: Acts on thiogalactosides and phenylgalactoside.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9029-94-1
References:
1. Zabin, I. Crystalline thiogalactoside transacetylase. J. Biol. Chem. 238 (1963) 3300-3306.
2. Zabin, I., Kepes, A. and Monod, J. Thiogalactoside transacetylase. J. Biol. Chem. 237 (1962) 253-257.
Accepted name: phosphate butyryltransferase
Reaction: butanoyl-CoA + phosphate = CoA + butanoyl phosphate
Other name(s): phosphotransbutyrylase
Systematic name: butanoyl-CoA:phosphate butanoyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9030-01-7
References:
1. Valentine, R.C. and Wolfe, R.S. Purification and role of phosphotransbutyrylase. J. Biol. Chem. 235 (1960) 1948-1952.
Accepted name: diacylglycerol O-acyltransferase
Reaction: acyl-CoA + 1,2-diacyl-sn-glycerol = CoA + triacylglycerol
Other name(s): diglyceride acyltransferase; 1,2-diacylglycerol acyltransferase; diacylglycerol acyltransferase; diglyceride O-acyltransferase; palmitoyl-CoA-sn-1,2-diacylglycerol acyltransferase; acyl-CoA:1,2-diacylglycerol O-acyltransferase
Systematic name: acyl-CoA:1,2-diacyl-sn-glycerol O-acyltransferase
Comments: Palmitoyl-CoA and other long-chain acyl-CoAs can act as donors.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9029-98-5
References:
1. Coleman, R. and Bell, R.M. Triacylglycerol synthesis in isolated fat cells. Studies on the microsomal diacylglycerol acyltransferase activity using ethanol-dispersed diacylglycerols. J. Biol. Chem. 251 (1976) 4537-4543. [PMID: 947894]
2. Grigor, M.R. and Bell, R.M. Separate monoacylglycerol and diacylglycerol acyltransferases function in intestinal triacylglycerol synthesis. Biochim. Biophys. Acta 712 (1982) 464-472. [PMID: 6289909]
3. Kawasaki, T. and Snyder, F. Synthesis of a novel acetylated neutral lipid related to platelet-activating factor by acyl-CoA:1-O-alkyl-2-acetyl-sn-glycerol acyltransferase in HL-60 cells. J. Biol. Chem. 263 (1988) 2593-2596. [PMID: 3422635]
4. Weiss, S.B., Kennedy, E.P. and Kiyasu, J.Y. The enzymatic synthesis of triglycerides. J. Biol. Chem. 235 (1960) 40-44.
Accepted name: carnitine O-palmitoyltransferase
Reaction: palmitoyl-CoA + L-carnitine = CoA + L-palmitoylcarnitine
Other name(s): CPT (ambiguous); CPTo; outer malonyl-CoA inhibitable carnitine palmitoyltransferase; CPTi; CPT I (outer membrane carnitine palmitoyl transferase); carnitine palmitoyltransferase I; carnitine palmitoyltransferase II; CPT-A; CPT-B; acylcarnitine transferase; carnitine palmitoyltransferase; carnitine palmitoyltransferase-A; L-carnitine palmitoyltransferase; palmitoylcarnitine transferase
Systematic name: palmitoyl-CoA:L-carnitine O-palmitoyltransferase
Comments: Broad specificity to acyl group, over the range C8 to C18; optimal activity with palmitoyl-CoA. cf. EC 2.3.1.7 carnitine O-acetyltransferase and EC 2.3.1.137 carnitine O-octanoyltransferase.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9068-41-1
References:
1. Derrick, J.P., Tubbs, P.K. and Ramsay, R.R. Purification and properties of an easily solubilized L-carnitine palmitoyltransferase from beef-liver mitochondria. Biochem. Soc. Trans. 14 (1986) 698.
2. Healy, M.J., Kerner, J. and Bieber, L.L. Enzymes of carnitine acylation. Is overt carnitine palmitoyltransferase of liver peroxisomal carnitine octanoyltransferase? Biochem. J. 249 (1988) 231-237. [PMID: 3342008]
3. Miyazawa, S., Ozasa, H., Osumi, T. and Hashimoto, T. Purification and properties of carnitine octanoyltransferase and carnitine palmitoyltransferase from rat liver. J. Biochem. (Tokyo) 94 (1983) 529-542. [PMID: 6630173]
Accepted name: 2-acylglycerol O-acyltransferase
Reaction: acyl-CoA + 2-acylglycerol = CoA + diacylglycerol
Other name(s): acylglycerol palmitoyltransferase; monoglyceride acyltransferase; acyl coenzyme A-monoglyceride acyltransferase; monoacylglycerol acyltransferase
Systematic name: acyl-CoA:2-acylglycerol O-acyltransferase
Comments: Various 2-acylglycerols can act as acceptor; palmitoyl-CoA and other long-chain acyl-CoAs can act as donors. The sn-1 position and the sn-3 position are both acylated, at about the same rate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9055-17-8
References:
1. Manganaro, F. and Kuksis, A. Purification and preliminary characterization of 2-monoacylglycerol acyltransferase from rat intestinal villus cells. Can. J. Biochem. Cell Biol. 63 (1985) 341-347. [PMID: 4016575]
Accepted name: 1-acylglycerophosphocholine O-acyltransferase
Reaction: acyl-CoA + 1-acyl-sn-glycero-3-phosphocholine = CoA + 1,2-diacyl-sn-glycero-3-phosphocholine
Other name(s): lysolecithin acyltransferase; 1-acyl-sn-glycero-3-phosphocholine acyltransferase; acyl coenzyme A-monoacylphosphatidylcholine acyltransferase; acyl-CoA:1-acyl-glycero-3-phosphocholine transacylase; lysophosphatide acyltransferase; lysophosphatidylcholine acyltransferase
Systematic name: acyl-CoA:1-acyl-sn-glycero-3-phosphocholine O-acyltransferase
Comments: Acts preferentially with unsaturated acyl-CoA derivatives. 1-Acyl-sn-glycero-3-phosphoinositol can also act as acceptor.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9027-64-9
References:
1. Bell, R.M. and Coleman, R.A. Enzymes of glycerolipid synthesis in eukaryotes. Annu. Rev. Biochem. 49 (1980) 459-487. [PMID: 6250446]
2. Hill, E.E. and Lands, W.E.M. Incorporation of long-chain and polyunsaturated acids into phosphatidate and phosphatidylcholine. Biochim. Biophys. Acta 152 (1968) 645-648. [PMID: 5661029]
3. Miki, Y., Hosaka, K., Yamashita, S., Handa, H. and Numa, S. Acyl-acceptor specificities of 1-acylglycerolphosphate acyltransferase and 1-acylglycerophosphorylcholine acyltransferase resolved from rat liver microsomes. Eur. J. Biochem. 81 (1977) 433-441. [PMID: 598375]
4. van den Bosch, H., van Golde, L.M.G., Eibl, H. and van Deenen, L.L.M. The acylation of 1-acylglycero-3-phosphorylcholines by rat-liver microsomes. Biochim. Biophys. Acta 144 (1967) 613-623. [PMID: 6078124]
Accepted name: sphingosine N-acyltransferase
Reaction: an acyl-CoA + sphingosine = CoA + an N-acylsphingosine
Other name(s): ceramide synthetase; sphingosine acyltransferase
Systematic name: acyl-CoA:sphingosine N-acyltransferase
Comments: Acts on sphingosine or its 2-epimer.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37257-09-3
References:
1. Sribney, M. Enzymatic synthesis of ceramide. Biochim. Biophys. Acta 125 (1966) 542-547. [PMID: 5973195]
Accepted name: plasmalogen synthase
Reaction: acyl-CoA + 1-O-(alk-1-enyl)glycero-3-phosphocholine = CoA + plasmenylcholine
Glossary: 1-O-(alk-1-enyl)glycero-3-phosphocholine = 1-alkenylglycerophosphocholine,
plasmenylcholine = 1-alkenyl-2-acylglycerophosphocholine
Other name(s): lysoplasmenylcholine acyltransferase; O-1-alkenylglycero-3-phosphorylcholine acyltransferase; 1-alkenyl-glycero-3-phosphorylcholine:acyl-CoA acyltransferase; 1-alkenylglycerophosphocholine O-acyltransferase
Systematic name: acyl-CoA:1-O-(alk-1-enyl)-glycero-3-phosphocholine 2-O-acyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37257-10-6
References:
1. Waku, K. and Lands, W.E.M. Acyl coenzyme A:1-alkenyl-glycero-3-phosphorylcholine acyltransferase action in plasmalogen biosynthesis. J. Biol. Chem. 243 (1968) 2654-2659. [PMID: 5689955]
2. Arthur, G. and Choy, P.C. Acylation of 1-alkenyl-glycerophosphocholine and 1-acyl-glycerophosphocholine in guinea pig heart. Biochem. J. 236 (1986) 481-487. [PMID: 3753462]
Accepted name: sterol O-acyltransferase
Reaction: a long-chain acyl-CoA + a sterol = CoA + a long-chain 3-hydroxysterol ester
Other name(s): cholesterol acyltransferase; sterol-ester synthase; acyl coenzyme A-cholesterol-O-acyltransferase; acyl-CoA:cholesterol acyltransferase; ACAT; acylcoenzyme A:cholesterol O-acyltransferase; cholesterol ester synthase; cholesterol ester synthetase; cholesteryl ester synthetase; SOAT1 (gene name); SOAT2 (gene name); ARE1 (gene name); ARE2 (gene name); acyl-CoA:cholesterol O-acyltransferase
Systematic name: long-chain acyl-CoA:sterol O-acyltransferase
Comments: The enzyme catalyses the formation of sterol esters from a sterol and long-chain fatty acyl-coenzyme A. The enzyme from yeast, but not from mammals, prefers monounsaturated acyl-CoA. In mammals the enzyme acts mainly on cholesterol and forms cholesterol esters that are stored in cytosolic droplets, which may serve to protect cells from the toxicity of free cholesterol. In macrophages, the accumulation of cytosolic droplets of cholesterol esters results in the formation of `foam cells', a hallmark of early atherosclerotic lesions. In hepatocytes and enterocytes, cholesterol esters can be incorporated into apolipoprotein B-containing lipoproteins for secretion from the cell.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9027-63-8
References:
1. Spector, A.A., Mathur, S.N. and Kaduce, T.L. Role of acylcoenzyme A: cholesterol O-acyltransferase in cholesterol metabolism. Prog. Lipid Res. 18 (1979) 31-53. [PMID: 42927]
2. Taketani, S., Nishino, T. and Katsuki, H. Characterization of sterol-ester synthetase in Saccharomyces cerevisiae. Biochim. Biophys. Acta 575 (1979) 148-155. [PMID: 389289]
3. Lee, O., Chang, C.C., Lee, W. and Chang, T.Y. Immunodepletion experiments suggest that acyl-coenzyme A:cholesterol acyltransferase-1 (ACAT-1) protein plays a major catalytic role in adult human liver, adrenal gland, macrophages, and kidney, but not in intestines. J. Lipid Res. 39 (1998) 1722-1727. [PMID: 9717734]
4. Yang, H., Cromley, D., Wang, H., Billheimer, J.T. and Sturley, S.L. Functional expression of a cDNA to human acyl-coenzyme A:cholesterol acyltransferase in yeast. Species-dependent substrate specificity and inhibitor sensitivity. J. Biol. Chem 272 (1997) 3980-3985. [PMID: 9020103]
5. Chang, C.C., Lee, C.Y., Chang, E.T., Cruz, J.C., Levesque, M.C. and Chang, T.Y. Recombinant acyl-CoA:cholesterol acyltransferase-1 (ACAT-1) purified to essential homogeneity utilizes cholesterol in mixed micelles or in vesicles in a highly cooperative manner. J. Biol. Chem 273 (1998) 35132-35141. [PMID: 9857049]
6. Das, A., Davis, M.A. and Rudel, L.L. Identification of putative active site residues of ACAT enzymes. J. Lipid Res. 49 (2008) 1770-1781. [PMID: 18480028]
Accepted name: cortisol O-acetyltransferase
Reaction: acetyl-CoA + cortisol = CoA + cortisol 21-acetate
Other name(s): cortisol acetyltransferase; corticosteroid acetyltransferase; corticosteroid-21-O-acetyltransferase
Systematic name: acetyl-CoA:cortisol O-acetyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9076-48-6
References:
1. Thomas, P.J. Cortisol acetyltransferase from baboon brain. Biochem. J. 109 (1968) 695-696. [PMID: 4971640]
Accepted name: chloramphenicol O-acetyltransferase
Reaction: acetyl-CoA + chloramphenicol = CoA + chloramphenicol 3-acetate
Other name(s): chloramphenicol acetyltransferase; chloramphenicol acetylase; chloramphenicol transacetylase; CAT I; CAT II; CAT III
Systematic name: acetyl-CoA:chloramphenicol 3-O-acetyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9040-07-7
References:
1. Shaw, W.V. The enzymatic acetylation of chloramphenicol by extracts of R factor-resistant Escherichia coli. J. Biol. Chem. 242 (1967) 687-693. [PMID: 5335032]
2. Shaw, W.V. and Brodsky, R.F. Characterization of chloramphenicol acetyltransferase from chloramphenicol-resistant Staphylococcus aureus. J. Bacteriol. 95 (1968) 28-36. [PMID: 4965980]
Accepted name: glycine C-acetyltransferase
Reaction: acetyl-CoA + glycine = CoA + 2-amino-3-oxobutanoate
Other name(s): 2-amino-3-ketobutyrate CoA ligase; 2-amino-3-ketobutyrate coenzyme A ligase; 2-amino-3-ketobutyrate-CoA ligase; glycine acetyltransferase; aminoacetone synthase; aminoacetone synthetase; KBL; AKB ligase
Systematic name: acetyl-CoA:glycine C-acetyltransferase
Comments: This is a pyridoxal-phosphate-dependent enzyme that acts in concert with EC 1.1.1.103, L-threonine 3-dehydrogenase, in the degradation of threonine to form glycine [3]. This threonine degradation pathway is common to prokaryotic and eukaryotic cells and the two enzymes involved form a complex [4].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37257-11-7
References:
1. McGilvray, D. and Morris, J.G. Utilization of L-threonine by a species of Arthrobacter. A novel catabolic role for "aminoacetone synthase". Biochem. J. 112 (1969) 657-671. [PMID: 5821726]
2. Mukherjee, J.J. and Dekker, E.E. Purification, properties, and N-terminal amino acid sequence of homogeneous Escherichia coli 2-amino-3-ketobutyrate CoA ligase, a pyridoxal phosphate-dependent enzyme. J. Biol. Chem. 262 (1987) 14441-14447. [PMID: 3117785]
3. Edgar, A.J. and Polak, J.M. Molecular cloning of the human and murine 2-amino-3-ketobutyrate coenzyme A ligase cDNAs. Eur. J. Biochem. 267 (2000) 1805-1812. [PMID: 10712613]
4. Schmidt, A., Sivaraman, J., Li, Y., Larocque, R., Barbosa, J.A., Smith, C., Matte, A., Schrag, J.D. and Cygler, M. Three-dimensional structure of 2-amino-3-ketobutyrate CoA ligase from Escherichia coli complexed with a PLP-substrate intermediate: inferred reaction mechanism. Biochemistry 40 (2001) 5151-5160. [PMID: 11318637]
Accepted name: serine O-acetyltransferase
Reaction: acetyl-CoA + L-serine = CoA + O-acetyl-L-serine
For diagram of reaction click here.
Glossary: O-acetyl-L-serine = (2S)-3-acetyloxy-2-aminopropanoic acid
Other name(s): SATase; L-serine acetyltransferase; serine acetyltransferase; serine transacetylase
Systematic name: acetyl-CoA:L-serine O-acetyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9023-16-9
References:
1. Kredich, N.M. and Tomkins, G.M. The enzymic synthesis of L-cysteine in Escherichia coli and Salmonella typhimurium. J. Biol. Chem. 241 (1966) 4955-4965.
2. Smith, I.K. and Thompson, J.F. Purification and characterization of L-serine transacetylase and O-acetyl-L-serine sulfhydrylase from kidney bean seedlings (Phaseolus vulgaris). Biochim. Biophys. Acta 227 (1971) 288-295. [PMID: 5550822]
Accepted name: homoserine O-acetyltransferase
Reaction: acetyl-CoA + L-homoserine = CoA + O-acetyl-L-homoserine
Other name(s): homoserine acetyltransferase; homoserine transacetylase; homoserine-O-transacetylase; L-homoserine O-acetyltransferase
Systematic name: acetyl-CoA:L-homoserine O-acetyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9030-72-2
References:
1. Nagai, S. and Flavin, M. Acetylhomoserine. An intermediate in the fungal biosynthesis of methionine. J. Biol. Chem. 242 (1967) 3884-3895. [PMID: 6037552]
Accepted name: lysine N-acetyltransferase
Reaction: acetyl phosphate + L-lysine = phosphate + N6-acetyl-L-lysine
Other name(s): lysine acetyltransferase
Systematic name: acetyl-phosphate:L-lysine N6-acetyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37257-12-8
References:
1. Paik, W.K. and Kim, S. Enzymic synthesis of ε-N-acetyl-L-lysine. Arch. Biochem. Biophys. 108 (1964) 221-229.
Accepted name: histidine N-acetyltransferase
Reaction: acetyl-CoA + L-histidine = CoA + N-acetyl-L-histidine
Other name(s): acetylhistidine synthetase; histidine acetyltransferase
Systematic name: acetyl-CoA:L-histidine N-acetyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9027-59-2
References:
1. Baslow, M.H. N-acetyl-L-histidine synthetase activity from the brain of the killifish. Brain Res. 3 (1966) 210-213. [PMID: 5971525]
Accepted name: D-tryptophan N-acetyltransferase
Reaction: acetyl-CoA + D-tryptophan = CoA + N-acetyl-D-tryptophan
Other name(s): D-tryptophan acetyltransferase; acetyl-CoA-D-tryptophan-α-N-acetyltransferase
Systematic name: acetyl-CoA:D-tryptophan N-acetyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37257-13-9
References:
1. Zenk, M.H. and Schmitt, J. Enzymatische Acetylierung von D-Tryptophan. Naturwissenschaften 51 (1964) 510-511.
Accepted name: glutamate N-acetyltransferase
Reaction: N2-acetyl-L-ornithine + L-glutamate = L-ornithine + N-acetyl-L-glutamate
Other name(s): ornithine transacetylase; α-N-acetyl-L-ornithine:L-glutamate N-acetyltransferase; acetylglutamate synthetase; acetylglutamate-acetylornithine transacetylase; acetylglutamic synthetase; acetylglutamic-acetylornithine transacetylase; acetylornithine glutamate acetyltransferase; glutamate acetyltransferase; N-acetyl-L-glutamate synthetase; N-acetylglutamate synthase; N-acetylglutamate synthetase; ornithine acetyltransferase; 2-N-acetyl-L-ornithine:L-glutamate N-acetyltransferase; acetylornithinase (ambiguous)
Systematic name: N2-acetyl-L-ornithine:L-glutamate N-acetyltransferase
Comments: Also has some hydrolytic activity on acetyl-L-ornithine, but the rate is 1% of that of transferase activity.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 37257-14-0
References:
1. Staub, M. and Dénes, G. Mechanism of arginine biosynthesis in Chlamydomonas reinhardti. I. Purification and properties of ornithine acetyltransferase. Biochim. Biophys. Acta 128 (1966) 82-91. [PMID: 5972370]
Accepted name: D-amino-acid N-acetyltransferase
Reaction: acetyl-CoA + a D-amino acid = CoA + an N-acetyl-D-amino acid
Other name(s): D-amino acid acetyltransferase; D-amino acid-α-N-acetyltransferase
Systematic name: acetyl-CoA:D-amino-acid N-acetyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37257-15-1
References:
1. Zenk, M.H. and Schmitt, J. Reinigung und Eigenschaften von Acetyl-CoA:D-Aminosäure-α-N -Acetyltransferase aus Hefe. Biochem. Z. 342 (1965) 54-65.
Accepted name: 5-aminolevulinate synthase
Reaction: succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2
For diagram of reaction click here.
Other name(s): ALAS; ALA synthase; α-aminolevulinic acid synthase; δ-aminolevulinate synthase; δ-aminolevulinate synthetase; δ-aminolevulinic acid synthase; δ-aminolevulinic acid synthetase; δ-aminolevulinic synthetase; 5-aminolevulinate synthetase; 5-aminolevulinic acid synthetase; ALA synthetase; aminolevulinate synthase; aminolevulinate synthetase; aminolevulinic acid synthase; aminolevulinic acid synthetase; aminolevulinic synthetase
Systematic name: succinyl-CoA:glycine C-succinyltransferase (decarboxylating)
Comments: A pyridoxal-phosphate protein. The enzyme in erythrocytes is genetically distinct from that in other tissues.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9037-14-3
References:
1. Bishop, D.F., Henderson, A.S. and Astrin, K.H. Human δ-aminolevulinate synthase - assignment of the housekeeping gene to 3p21 and the erythroid-specific gene to the X-chromosome. Genomics 7 (1990) 207-214.
2. Kikuchi, G., Kumar, A., Talmage, P. and Shemin, D. The enzymatic synthesis of δ-aminolevulinic acid. J. Biol. Chem. 233 (1958) 1214-1219.
3. Ramaswamy, N.K. and Nair, P.M. δ-Aminolevulinic acid synthetase from cold-stored potatoes. Biochim. Biophys. Acta 293 (1973) 269-277. [PMID: 4685279]
4. Scholnick, P.L., Hammaker, L.E. and Marver, H.S. Soluble δ-aminolevulinic acid synthetase of rat liver. I. Some properties of the partially purified enzyme. J. Biol. Chem. 247 (1972) 4126-4131. [PMID: 4624703]
5. Scholnick, P.L., Hammaker, L.E. and Marver, H.S. Soluble δ-aminolevulinic acid synthetase of rat liver. II. Studies related to the mechanism of enzyme action and hemin inhibition. J. Biol. Chem. 247 (1972) 4132-4137. [PMID: 5035685]
6. Tait, G.H. Aminolaevulinate synthetase of Micrococcus denitrificans. Purification and properties of the enzyme, and the effect of growth conditions on the enzyme activity in cells. Biochem. J. 131 (1973) 389-403. [PMID: 4722442]
7. Warnick, G.R. and Burnham, B.F. Regulation of porphyrin biosynthesis. Purification and characterization of δ-aminolevulinic acid synthase. J. Biol. Chem. 246 (1971) 6880-6885. [PMID: 5315997]
Accepted name: [acyl-carrier-protein] S-acetyltransferase
Reaction: acetyl-CoA + an [acyl-carrier protein] = CoA + an acetyl-[acyl-carrier protein]
For diagram click here.
Other name(s): acetyl coenzyme A-acyl-carrier-protein transacylase; [acyl-carrier-protein]-acetyltransferase; [ACP]-acetyltransferase; acetyl-CoA:[acyl-carrier-protein] S-acetyltransferase
Systematic name: acetyl-CoA:[acyl-carrier protein] S-acetyltransferase
Comments: This enzyme, along with EC 2.3.1.39, [acyl-carrier-protein] S-malonyltransferase, is essential for the initiation of fatty-acid biosynthesis in bacteria. The substrate acetyl-CoA protects the enzyme against inhibition by N-ethylmaleimide or iodoacetamide [4]. This is one of the activities associated with β-ketoacyl-ACP synthase III (EC 2.3.1.180) [5].
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 37257-16-2
References:
1. Prescott, D.J. and Vagelos, P.R. Acyl carrier protein. Adv. Enzymol. Relat. Areas Mol. Biol. 36 (1972) 269-311. [PMID: 4561013]
2. Vance, D.E., Mituhashi, O. and Bloch, K. Purification and properties of the fatty acid synthetase from Mycobacterium phlei. J. Biol. Chem. 248 (1973) 2303-2309. [PMID: 4698221]
3. Williamson, I.P. and Wakil, S.J. Studies on the mechanism of fatty acid synthesis. XVII. Preparation and general properties of acetyl coenzyme A and malonyl coenzyme A-acyl carrier protein transacylases. J. Biol. Chem. 241 (1966) 2326-2332. [PMID: 5330116]
4. Lowe, P.N. and Rhodes, S. Purification and characterization of [acyl-carrier-protein] acetyltransferase from Escherichia coli. Biochem. J. 250 (1988) 789-796. [PMID: 3291856]
5. Tsay, J.T., Oh, W., Larson, T.J., Jackowski, S. and Rock, C.O. Isolation and characterization of the β-ketoacyl-acyl carrier protein synthase III gene (fabH) from Escherichia coli K-12. J. Biol. Chem. 267 (1992) 6807-6814. [PMID: 1551888]
6. Rangan, V.S. and Smith, S. Alteration of the substrate specificity of the malonyl-CoA/acetyl-CoA:acyl carrier protein S-acyltransferase domain of the multifunctional fatty acid synthase by mutation of a single arginine residue. J. Biol. Chem. 272 (1997) 11975-11978. [PMID: 9115261]
Accepted name: [acyl-carrier-protein] S-malonyltransferase
Reaction: malonyl-CoA + an [acyl-carrier protein] = CoA + a malonyl-[acyl-carrier protein]
Other name(s): [acyl carrier protein]malonyltransferase; FabD; malonyl coenzyme A-acyl carrier protein transacylase; malonyl transacylase; malonyl transferase; malonyl-CoA-acyl carrier protein transacylase; malonyl-CoA:[acyl-carrier-protein] S-malonyltransferase; malonyl-CoA:ACP transacylase; malonyl-CoA:ACP-SH transacylase; malonyl-CoA:AcpM transacylase; malonyl-CoA:acyl carrier protein transacylase; malonyl-CoA:acyl-carrier-protein transacylase; malonyl-CoA/dephospho-CoA acyltransferase; MAT; MCAT; MdcH
Systematic name: malonyl-CoA:[acyl-carrier protein] S-malonyltransferase
Comments: This enzyme, along with EC 2.3.1.38, [acyl-carrier-protein] S-acetyltransferase, is essential for the initiation of fatty-acid biosynthesis in bacteria. This enzyme also provides the malonyl groups for polyketide biosynthesis [7]. The product of the reaction, malonyl-ACP, is an elongation substrate in fatty-acid biosynthesis. In Mycobacterium tuberculosis, holo-ACP (the product of EC 2.7.8.7, holo-[acyl-carrier-protein] synthase) is the preferred substrate [5]. This enzyme also forms part of the multienzyme complexes EC 4.1.1.88 (biotin-independent malonate decarboxylase) and EC 7.2.4.4, biotin-dependent malonate decarboxylase. Malonylation of ACP is immediately followed by decarboxylation within the malonate-decarboxylase complex to yield acetyl-ACP, the catalytically active species of the decarboxylase [12]. In the enzyme from Klebsiella pneumoniae, methylmalonyl-CoA can also act as a substrate but acetyl-CoA cannot [10] whereas the enzyme from Pseudomonas putida can use both as substrates [11]. The ACP subunit found in fatty-acid biosynthesis contains a pantetheine-4'-phosphate prosthetic group; that from malonate decarboxylase also contains pantetheine-4'-phosphate but in the form of a 2'-(5-triphosphoribosyl)-3'-dephospho-CoA prosthetic group.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 37257-17-3
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. Williamson, I.P. and Wakil, S.J. Studies on the mechanism of fatty acid synthesis. XVII. Preparation and general properties of acetyl coenzyme A and malonyl coenzyme A-acyl carrier protein transacylases. J. Biol. Chem. 241 (1966) 2326-2332. [PMID: 5330116]
4. Joshi, V.C. and Wakil, S.J. Studies on the mechanism of fatty acid synthesis. XXVI. Purification and properties of malonyl-coenzyme A--acyl carrier protein transacylase of Escherichia coli. Arch. Biochem. Biophys. 143 (1971) 493-505. [PMID: 4934182]
5. Kremer, L., Nampoothiri, K.M., Lesjean, S., Dover, L.G., Graham, S., Betts, J., Brennan, P.J., Minnikin, D.E., Locht, C. and Besra, G.S. Biochemical characterization of acyl carrier protein (AcpM) and malonyl-CoA:AcpM transacylase (mtFabD), two major components of Mycobacterium tuberculosis fatty acid synthase II. J. Biol. Chem. 276 (2001) 27967-27974. [PMID: 11373295]
6. Keatinge-Clay, A.T., Shelat, A.A., Savage, D.F., Tsai, S.C., Miercke, L.J., O'Connell, J.D., 3rd, Khosla, C. and Stroud, R.M. Catalysis, specificity, and ACP docking site of Streptomyces coelicolor malonyl-CoA:ACP transacylase. Structure 11 (2003) 147-154. [PMID: 12575934]
7. Szafranska, A.E., Hitchman, T.S., Cox, R.J., Crosby, J. and Simpson, T.J. Kinetic and mechanistic analysis of the malonyl CoA:ACP transacylase from Streptomyces coelicolor indicates a single catalytically competent serine nucleophile at the active site. Biochemistry 41 (2002) 1421-1427. [PMID: 11814333]
8. Hoenke, S., Schmid, M. and Dimroth, P. Sequence of a gene cluster from Klebsiella pneumoniae encoding malonate decarboxylase and expression of the enzyme in Escherichia coli. Eur. J. Biochem. 246 (1997) 530-538. [PMID: 9208947]
9. Koo, J.H. and Kim, Y.S. Functional evaluation of the genes involved in malonate decarboxylation by Acinetobacter calcoaceticus. Eur. J. Biochem. 266 (1999) 683-690. [PMID: 10561613]
10. Hoenke, S. and Dimroth, P. Formation of catalytically active acetyl-S-malonate decarboxylase requires malonyl-coenzyme A:acyl carrier protein transacylase as auxiliary enzyme. Eur. J. Biochem. 259 (1999) 181-187. [PMID: 9914491]
11. Chohnan, S., Fujio, T., Takaki, T., Yonekura, M., Nishihara, H. and Takamura, Y. Malonate decarboxylase of Pseudomonas putida is composed of five subunits. FEMS Microbiol. Lett. 169 (1998) 37-43. [PMID: 9851033]
12. Dimroth, P. and Hilbi, H. Enzymic and genetic basis for bacterial growth on malonate. Mol. Microbiol. 25 (1997) 3-10. [PMID: 11902724]
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
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]
Accepted name: β-ketoacyl-acyl-carrier-protein synthase I
Reaction: an acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein] = a 3-oxoacyl-[acyl-carrier protein] + CO2 + [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. 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, PDB, Metacyc, 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. [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.
Accepted name: glycerone-phosphate O-acyltransferase
Reaction: acyl-CoA + glycerone phosphate = CoA + acylglycerone phosphate
Other name(s): dihydroxyacetone phosphate acyltransferase (ambiguous)
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. [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.
3. Hajra, A.K. Biosynthesis of acyl dihydroxyacetone phosphate in guinea pig liver mitochondria. J. Biol. Chem. 243 (1968) 3458-3465. [PMID: 5656381]
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, PDB, 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]
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]
Accepted name: N-acetylneuraminate 9-O-acetyltransferase
Reaction: acetyl-CoA + CMP-N-acetyl-β-neuraminate = CoA + CMP-N-acetyl-9-O-acetyl-β-neuraminate
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; CASD1; acetyl-CoA:N-acetylneuraminate 7-O(or 9-O)-acetyltransferase; N-acetylneuraminate 7-O(or 9-O)-acetyltransferase
Systematic name: acetyl-CoA:CMP-N-acetyl-β-neuraminate 9-O-acetyltransferase
Comments: The enzyme, found in animals, is essential for the formation of acetylated sialoglycans. The acetyl group has been shown to spontaneously move between the 9-O, 8-O, and 7-O positions of the neuraminate, with 9-O acetylation being most favoured.
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]
3. Baumann, A.M., Bakkers, M.J., Buettner, F.F., Hartmann, M., Grove, M., Langereis, M.A., de Groot, R.J. and Muhlenhoff, M. 9-O-Acetylation of sialic acids is catalysed by CASD1 via a covalent acetyl-enzyme intermediate. Nat. Commun. 6 (2015) 7673. [PMID: 26169044]
Accepted name: homoserine O-succinyltransferase
Reaction: succinyl-CoA + L-homoserine = CoA + O-succinyl-L-homoserine
For diagram of reaction click here.
Other name(s): homoserine O-transsuccinylase (ambiguous); 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.
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. [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. [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. (2010) . [PMID: 20693992]
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. [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. [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. [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. [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. [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. [PMID: 24616510]
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. [PMID: 4741546]
Accepted name: serine C-palmitoyltransferase
Reaction: palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2
Other name(s): serine palmitoyltransferase; SPT; 3-oxosphinganine synthetase; acyl-CoA:serine C-2 acyltransferase decarboxylating
Systematic name: palmitoyl-CoA:L-serine C-palmitoyltransferase (decarboxylating)
Comments: A pyridoxal-phosphate protein.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 62213-50-7
References:
1. Brady, R.N., DiMari, S.J. and Snell, E.E. Biosynthesis of sphingolipid bases. 3. Isolation and characterization of ketonic intermediates in the synthesis of sphingosine and dihydrosphingosine by cell-free extracts of Hansenula ciferri. J. Biol. Chem. 244 (1969) 491-496. [PMID: 4388074]
2. Stoffel, W., Le Kim, D. and Sticht, G. Biosynthesis of dihydrosphingosine in vitro. Hoppe-Seyler's Z. Physiol. Chem. 349 (1968) 664-670. [PMID: 4386961]