Enzyme Nomenclature Continued from EC 2.2.1.1 - EC 2.2.1.4

EC 2.3

Acyltransferases

Sections

EC 2.3.1 Transferring groups other than amino-acyl groups
EC 2.3.2 Aminoacyltransferases


EC 2.3.1 Transferring groups other than amino-acyl groups

('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 2.3.1.264

Contents

EC 2.3.1.1 amino-acid N-acetyltransferase
EC 2.3.1.2 imidazole N-acetyltransferase
EC 2.3.1.3 glucosamine N-acetyltransferase
EC 2.3.1.4 glucosamine-phosphate N-acetyltransferase
EC 2.3.1.5 arylamine N-acetyltransferase
EC 2.3.1.6 choline O-acetyltransferase
EC 2.3.1.7 carnitine O-acetyltransferase
EC 2.3.1.8 phosphate acetyltransferase
EC 2.3.1.9 acetyl-CoA C-acetyltransferase
EC 2.3.1.10 hydrogen-sulfide S-acetyltransferase
EC 2.3.1.11 thioethanolamine S-acetyltransferase
EC 2.3.1.12 dihydrolipoyllysine-residue acetyltransferase
EC 2.3.1.13 glycine N-acyltransferase
EC 2.3.1.14 glutamine N-phenylacetyltransferase
EC 2.3.1.15 glycerol-3-phosphate 1-O-acyltransferase
EC 2.3.1.16 acetyl-CoA C-acyltransferase
EC 2.3.1.17 aspartate N-acetyltransferase
EC 2.3.1.18 galactoside O-acetyltransferase
EC 2.3.1.19 phosphate butyryltransferase
EC 2.3.1.20 diacylglycerol O-acyltransferase
EC 2.3.1.21 carnitine O-palmitoyltransferase
EC 2.3.1.22 2-acylglycerol O-acyltransferase
EC 2.3.1.23 1-acylglycerophosphocholine O-acyltransferase
EC 2.3.1.24 sphingosine N-acyltransferase
EC 2.3.1.25 plasmalogen synthase
EC 2.3.1.26 sterol O-acyltransferase
EC 2.3.1.27 cortisol O-acetyltransferase
EC 2.3.1.28 chloramphenicol O-acetyltransferase
EC 2.3.1.29 glycine C-acetyltransferase
EC 2.3.1.30 serine O-acetyltransferase
EC 2.3.1.31 homoserine O-acetyltransferase
EC 2.3.1.32 lysine N-acetyltransferase
EC 2.3.1.33 histidine N-acetyltransferase
EC 2.3.1.34 D-tryptophan N-acetyltransferase
EC 2.3.1.35 glutamate N-acetyltransferase
EC 2.3.1.36 D-amino-acid N-acetyltransferase
EC 2.3.1.37 5-aminolevulinate synthase
EC 2.3.1.38 [acyl-carrier-protein] S-acetyltransferase
EC 2.3.1.39 [acyl-carrier-protein] S-malonyltransferase
EC 2.3.1.40 acyl-[acyl-carrier-protein]—phospholipid O-acyltransferase
EC 2.3.1.41 β-ketoacyl-acyl-carrier-protein synthase I
EC 2.3.1.42 glycerone-phosphate O-acyltransferase
EC 2.3.1.43 phosphatidylcholine—sterol O-acyltransferase
EC 2.3.1.44 N-acetylneuraminate 4-O-acetyltransferase
EC 2.3.1.45 N-acetylneuraminate 7-O(or 9-O)-acetyltransferase
EC 2.3.1.46 homoserine O-succinyltransferase
EC 2.3.1.47 8-amino-7-oxononanoate synthase
EC 2.3.1.48 histone acetyltransferase
EC 2.3.1.49 deacetyl-[citrate-(pro-3S)-lyase] S-acetyltransferase
EC 2.3.1.50 serine C-palmitoyltransferase
See the following files 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
EC 2.3.1.200 to EC 2.3.1.264

Entries

EC 2.3.1.1

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.

[EC 2.3.1.1 created 1961]

EC 2.3.1.2

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.

[EC 2.3.1.2 created 1961]

EC 2.3.1.3

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, 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.

[EC 2.3.1.3 created 1961]

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 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]

[EC 2.3.1.4 created 1961, modified 2002]

EC 2.3.1.5

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, EXPASY, GTD, KEGG, Metacyc, PDB, UM-BBD, 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.

[EC 2.3.1.5 created 1961]

EC 2.3.1.6

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.

[EC 2.3.1.6 created 1961]

EC 2.3.1.7

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.

[EC 2.3.1.7 created 1961]

EC 2.3.1.8

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.

[EC 2.3.1.8 created 1961, modified 1976]

EC 2.3.1.9

Accepted name: acetyl-CoA C-acetyltransferase

Reaction: 2 acetyl-CoA = CoA + acetoacetyl-CoA

For diagram click here (another example).

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

Systematic name: acetyl-CoA:acetyl-CoA C-acetyltransferase

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, UM-BBD, 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.

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.

[EC 2.3.1.9 created 1961]

EC 2.3.1.10

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.

[EC 2.3.1.10 created 1961]

EC 2.3.1.11

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.

[EC 2.3.1.11 created 1961, modified 2006]

EC 2.3.1.12

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]

[EC 2.3.1.12 created 1961, modified 2003]

EC 2.3.1.13

Accepted name: ATP carbamoyltransferase

Reaction: carbamoyl phosphate + ATP + H2O = diphosphate + O-carbamoyladenylate + phosphate

For diagram of reaction click here.

Other name(s): TobZ (ambiguous)

Systematic name: carbamoyl phosphate:ATP carbamoyl-transferase

Comments: The enzyme from the bacterium Streptoalloteichus tenebrarius catalyses the activation of carbamoyl phosphate to O-carbamoyladenylate, and the subsequent carbamoylation of kanamycin and tobramycin. cf. EC 2.1.3.14, tobramycin carbamoyltransferase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Parthier, C., Gorlich, S., Jaenecke, F., Breithaupt, C., Brauer, U., Fandrich, U., Clausnitzer, D., Wehmeier, U.F., Bottcher, C., Scheel, D. and Stubbs, M.T. The O-carbamoyltransferase TobZ catalyzes an ancient enzymatic reaction. Angew. Chem. Int. Ed. Engl. 51 (2012) 4046-4052. [PMID: 22383337]

[EC 2.1.3.13 created 2013]

EC 2.3.1.14

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.

[EC 2.3.1.14 created 1961]

EC 2.3.1.15

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]

[EC 2.3.1.15 created 1961, modified 1976, modified 1990]

EC 2.3.1.16

Accepted name: acetyl-CoA C-acyltransferase

Reaction: acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA

For diagram of reaction click here or another example 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; 2-methylacetoacetyl-CoA thiolase [misleading]

Systematic name: acyl-CoA:acetyl-CoA C-acyltransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, 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.

3. Stern, J.R., Coon, M.J. and del Campillo, A. Enzymatic breakdown and synthesis of acetoacetate. Nature 171 (1953) 28-30.

[EC 2.3.1.16 created 1961]

EC 2.3.1.17

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]

[EC 2.3.1.17 created 1965]

EC 2.3.1.18

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.

[EC 2.3.1.18 created 1965]

EC 2.3.1.19

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, 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.

[EC 2.3.1.19 created 1965]

EC 2.3.1.20

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, 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.

[EC 2.3.1.20 created 1965]

EC 2.3.1.21

Accepted name: carnitine O-palmitoyltransferase

Reaction: palmitoyl-CoA + L-carnitine = CoA + L-palmitoylcarnitine

Other name(s): CPT; 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]

[EC 2.3.1.21 created 1972]

EC 2.3.1.22

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]

[EC 2.3.1.22 created 1972, modified 1986, modified 1989]

EC 2.3.1.23

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, 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]

[EC 2.3.1.23 created 1972]

EC 2.3.1.24

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, CAS registry number: 37257-09-3

References:

1. Sribney, M. Enzymatic synthesis of ceramide. Biochim. Biophys. Acta 125 (1966) 542-547. [PMID: 5973195]

[EC 2.3.1.24 created 1972]

EC 2.3.1.25

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]

[EC 2.3.1.25 created 1972, modified 2013]

EC 2.3.1.26

Accepted name: sterol O-acyltransferase

Reaction: acyl-CoA + cholesterol = CoA + cholesterol ester

Other name(s): cholesterol acyltransferase; sterol-ester synthase; sterol-ester synthetase; 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

Systematic name: acyl-CoA:cholesterol O-acyltransferase

Comments: The animal enzyme is highly specific for transfer of acyl groups with a single cis double bond that is nine carbon atoms distant from the carboxy group.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9027-63-8

References:

1. Sgoutas, D.S. Effect of geometry and position of ethylenic bond upon acyl coenzymeA--cholesterol-O-acyltransferase. Biochemistry 9 (1970) 1826-1833. [PMID: 5439042]

2. 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]

3. Taketani, S., Nishino, T. and Katsuki, H. Characterization of sterol-ester synthetase in Saccharomyces cerevisiae. Biochim. Biophys. Acta 575 (1979) 148-155. [PMID: 389289]

[EC 2.3.1.26 created 1972]

EC 2.3.1.27

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]

[EC 2.3.1.27 created 1972]

EC 2.3.1.28

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]

[EC 2.3.1.28 created 1972]

EC 2.3.1.29

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]

[EC 2.3.1.29 created 1972]

EC 2.3.1.30

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]

[EC 2.3.1.30 created 1972]

EC 2.3.1.31

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]

[EC 2.3.1.31 created 1972]

EC 2.3.1.32

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.

[EC 2.3.1.32 created 1972]

EC 2.3.1.33

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]

[EC 2.3.1.33 created 1972]

EC 2.3.1.34

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.

[EC 2.3.1.34 created 1972]

EC 2.3.1.35

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; acetylornithinase; acetylornithine glutamate acetyltransferase; glutamate acetyltransferase; N-acetyl-L-glutamate synthetase; N-acetylglutamate synthase; N-acetylglutamate synthetase; ornithine acetyltransferase

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]

[EC 2.3.1.35 created 1972]

EC 2.3.1.36

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.

[EC 2.3.1.36 created 1972]

EC 2.3.1.37

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]

[EC 2.3.1.37 created 1972]

EC 2.3.1.38

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; ACAT

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, 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]

[EC 2.3.1.38 created 1972, modified 2006]

EC 2.3.1.39

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 4.1.1.89 (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]

[EC 2.3.1.39 created 1972, modified 2006, modified 2008]

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

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] + 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.

[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

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. [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]

[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 Lokaslisation der Acetyl-Coenzym A: N-Acetylneuraminat-7- und 8-O-Acetyltransferase vom 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 reaction 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.

[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. [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]

[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. [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]

[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. [PMID: 4741546]

[EC 2.3.1.49 created 1976]

EC 2.3.1.50

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]

[EC 2.3.1.50 created 1976, modified 1982]


Continued with EC 2.3.1.51 to EC 2.3.1.100
Return to EC 2 home page
Return to Enzymes home page
Return to IUBMB Biochemical Nomenclature home page