EC |
2.3.1.13 |
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] |
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[EC 2.3.1.13 created 1961] |
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EC |
2.3.1.130 |
Accepted name: |
galactarate O-hydroxycinnamoyltransferase |
Reaction: |
feruloyl-CoA + galactarate = CoA + O-feruloylgalactarate |
Other name(s): |
galacturate hydroxycinnamoyltransferase |
Systematic name: |
feruloyl-CoA:galactarate O-(hydroxycinnamoyl)transferase |
Comments: |
Sinapoyl-CoA and 4-coumaroyl-CoA can also act as donors. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 112956-50-0 |
References: |
1. |
Strack, D., Keller, H. and Weissenböck, G. Enzymatic-synthesis of hydroxycinnamic acid-esters of sugar acids and hydroaromatic acids by protein preparations from rye (Secale cereale) primary leaves. J. Plant Physiol. 131 (1987) 61–73. |
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[EC 2.3.1.130 created 1990] |
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EC |
2.3.1.131 |
Accepted name: |
glucarate O-hydroxycinnamoyltransferase |
Reaction: |
sinapoyl-CoA + glucarate = CoA + O-sinapoylglucarate |
Systematic name: |
sinapoyl-CoA:glucarate O-(hydroxycinnamoyl)transferase |
Comments: |
4-Coumaroyl-CoA, feruloyl-CoA and caffeoyl-CoA can also act as donors, but more slowly. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 112956-51-1 |
References: |
1. |
Strack, D., Keller, H. and Weissenböck, G. Enzymatic-synthesis of hydroxycinnamic acid-esters of sugar acids and hydroaromatic acids by protein preparations from rye (Secale cereale) primary leaves. J. Plant Physiol. 131 (1987) 61–73. |
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[EC 2.3.1.131 created 1990] |
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EC |
2.3.1.132 |
Accepted name: |
glucarolactone O-hydroxycinnamoyltransferase |
Reaction: |
sinapoyl-CoA + glucarolactone = CoA + O-sinapoylglucarolactone |
Systematic name: |
sinapoyl-CoA:glucarolactone O-(hydroxycinnamoyl)transferase |
Comments: |
4-Coumaroyl-CoA, feruloyl-CoA and caffeoyl-CoA can also act as donors, but more slowly. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 112956-52-2 |
References: |
1. |
Strack, D., Keller, H. and Weissenböck, G. Enzymatic-synthesis of hydroxycinnamic acid-esters of sugar acids and hydroaromatic acids by protein preparations from rye (Secale cereale) primary leaves. J. Plant Physiol. 131 (1987) 61–73. |
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[EC 2.3.1.132 created 1990] |
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EC |
2.3.1.133 |
Accepted name: |
shikimate O-hydroxycinnamoyltransferase |
Reaction: |
4-coumaroyl-CoA + shikimate = CoA + 4-coumaroylshikimate |
Other name(s): |
shikimate hydroxycinnamoyltransferase |
Systematic name: |
4-coumaroyl-CoA:shikimate O-(hydroxycinnamoyl)transferase |
Comments: |
Caffeoyl-CoA, feruloyl-CoA and sinapoyl-CoA can also act as donors, but more slowly. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 73904-44-6 |
References: |
1. |
Strack, D., Keller, H. and Weissenböck, G. Enzymatic-synthesis of hydroxycinnamic acid-esters of sugar acids and hydroaromatic acids by protein preparations from rye (Secale cereale) primary leaves. J. Plant Physiol. 131 (1987) 61–73. |
2. |
Ulbrich, B. and Zenk, M.H. Partial purification and properties of p-hydroxycinnamoyl-CoA:shikimate-p-hydroxycinnamoyl transferase from higher plants. Phytochemistry 19 (1980) 1625–1629. |
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[EC 2.3.1.133 created 1990] |
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EC |
2.3.1.134 |
Accepted name: |
galactolipid O-acyltransferase |
Reaction: |
2 mono-β-D-galactosyldiacylglycerol = acylmono-β-D-galactosyldiacylglycerol + mono-β-D-galactosylacylglycerol |
Other name(s): |
galactolipid:galactolipid acyltransferase |
Systematic name: |
mono-β-D-galactosyldiacylglycerol:mono-β-D-galactosyldiacylglycerol acyltransferase |
Comments: |
Di-D-galactosyldiacylglycerol can also act as acceptor. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 103537-09-3 |
References: |
1. |
Heemskerk, J.W.M., Wintermans, J.F.G.M., Joyard, J., Block, M.A., Dorne, A.-J. and Douce, R. Localization of galactolipid:galactolipid galactosyltransferase and acyltransferase in outer envelope membrane of spinach chloroplasts. Biochim. Biophys. Acta 877 (1986) 281–289. |
2. |
Heinz, E. Some properties of the acyl galactoside-forming enzyme from leaves. Z. Pflanzenphysiol. 69 (1973) 359–376. |
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[EC 2.3.1.134 created 1990] |
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EC |
2.3.1.135 |
Accepted name: |
phosphatidylcholine—retinol O-acyltransferase |
Reaction: |
phosphatidylcholine + retinol—[cellular-retinol-binding-protein] = 2-acylglycerophosphocholine + retinyl-ester—[cellular-retinol-binding-protein] |
Glossary: |
phosphatidylcholine = lecithin |
Other name(s): |
lecithin—retinol acyltransferase; phosphatidylcholine:retinol-(cellular-retinol-binding-protein) O-acyltransferase; lecithin:retinol acyltransferase; lecithin-retinol acyltransferase; retinyl ester synthase; LRAT; lecithin retinol acyl transferase |
Systematic name: |
phosphatidylcholine:retinol—[cellular-retinol-binding-protein] O-acyltransferase |
Comments: |
A key enzyme in retinoid metabolism, catalysing the transfer of an acyl group from the sn-1 position of phosphatidylcholine to retinol, forming retinyl esters which are then stored. Recognizes the substrate both in free form and when bound to cellular-retinol-binding-protein, but has higher affinity for the bound form. Can also esterify 11-cis-retinol. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 117444-03-8 |
References: |
1. |
MacDonald, P.N. and Ong, D.E. Evidence for a lecithin-retinol acyltransferase activity in the rat small intestine. J. Biol. Chem. 263 (1988) 12478–12482. [PMID: 3410848] |
2. |
Saari, J.C. and Bredberg, D.L. Lecithin:retinol acyltransferase in retinal pigment epithelial microsomes. J. Biol. Chem. 264 (1989) 8636. [PMID: 2722792] |
3. |
Saari, J.C., Bredberg, D.L. and Farrell, D.F. Retinol esterification in bovine retinal pigment epithelium: reversibility of lecithin:retinol acyltransferase. Biochem. J. 291 (1993) 697–700. [PMID: 8489497] |
4. |
Mata, N.L. and Tsin, A.T. Distribution of 11-cis LRAT, 11-cis RD and 11-cis REH in bovine retinal pigment epithelium membranes. Biochim. Biophys. Acta 1394 (1998) 16–22. [DOI] [PMID: 9767084] |
5. |
Ruiz, A., Winston, A., Lim, Y.H., Gilbert, B.A., Rando, R.R. and Bok, D. Molecular and biochemical characterization of lecithin retinol acyltransferase. J. Biol. Chem. 274 (1999) 3834–3841. [DOI] [PMID: 9920938] |
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[EC 2.3.1.135 created 1992, modified 2011] |
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EC |
2.3.1.136 |
Accepted name: |
polysialic-acid O-acetyltransferase |
Reaction: |
acetyl-CoA + an α-2,8-linked polymer of sialic acid = CoA + polysialic acid acetylated at O-7 or O-9 |
Systematic name: |
acetyl-CoA:polysialic-acid O-acetyltransferase |
Comments: |
Acts only on substrates containing more than 14 sialosyl residues. Catalyses the modification of capsular polysaccharides in some strains of Escherichia coli. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 116412-21-6 |
References: |
1. |
Higa, H.H. and Varki, A. Acetyl-coenzyme A:polysialic acid O-acetyltransferase from K1-positive Escherichia coli. The enzyme responsible for the O-acetyl plus phenotype and for O-acetyl form variation. J. Biol. Chem. 263 (1988) 8872–8878. [PMID: 2897964] |
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[EC 2.3.1.136 created 1992] |
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EC |
2.3.1.137 |
Accepted name: |
carnitine O-octanoyltransferase |
Reaction: |
octanoyl-CoA + L-carnitine = CoA + L-octanoylcarnitine |
Other name(s): |
medium-chain/long-chain carnitine acyltransferase; carnitine medium-chain acyltransferase; easily solubilized mitochondrial carnitine palmitoyltransferase; overt mitochondrial carnitine palmitoyltransferase |
Systematic name: |
octanoyl-CoA:L-carnitine O-octanoyltransferase |
Comments: |
Acts on a range of acyl-CoAs, with optimal activity with C6 or C8 acyl groups. cf. EC 2.3.1.7 (carnitine O-acetyltransferase) and EC 2.3.1.21 (carnitine O-palmitoyltransferase). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 39369-19-2 |
References: |
1. |
Farrell, S.O., Fiol, C.J., Reddy, J.K. and Bieber, L.L. Properties of purified carnitine acyltransferases of mouse liver peroxisomes. J. Biol. Chem. 259 (1984) 13089–13095. [PMID: 6436243] |
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] |
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[EC 2.3.1.137 created 1992] |
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EC |
2.3.1.138 |
Accepted name: |
putrescine N-hydroxycinnamoyltransferase |
Reaction: |
caffeoyl-CoA + putrescine = CoA + N-caffeoylputrescine |
Glossary: |
putrescine = butane-1,4-diamine |
Other name(s): |
caffeoyl-CoA putrescine N-caffeoyl transferase; PHT; putrescine hydroxycinnamoyl transferase; hydroxycinnamoyl-CoA:putrescine hydroxycinnamoyltransferase; putrescine hydroxycinnamoyltransferase |
Systematic name: |
caffeoyl-CoA:putrescine N-(3,4-dihydroxycinnamoyl)transferase |
Comments: |
Feruloyl-CoA, cinnamoyl-CoA and sinapoyl-CoA can also act as donors, but more slowly. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 120598-69-8 |
References: |
1. |
Negrel, J. The biosynthesis of cinnamoylputrescines in callus-tissue cultures of Nicotiana tabacum. Phytochemistry 28 (1989) 477–481. |
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[EC 2.3.1.138 created 1992] |
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EC |
2.3.1.139 |
Accepted name: |
ecdysone O-acyltransferase |
Reaction: |
palmitoyl-CoA + ecdysone = CoA + ecdysone palmitate |
Other name(s): |
acyl-CoA:ecdysone acyltransferase; fatty acyl-CoA:ecdysone acyltransferase |
Systematic name: |
palmitoyl-CoA:ecdysone palmitoyltransferase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 120038-26-8 |
References: |
1. |
Slinger, A.J. and Isaac, R.E. Acyl-CoA-ecdysone acyltransferase activity from the ovary of P. americana. Insect Biochem. 18 (1988) 779–784. |
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[EC 2.3.1.139 created 1992] |
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