EC 2.3.1 (continued)

EC 2.3.1.1 to EC 2.3.1.50
EC 2.3.1.51 to EC 2.3.1.100

Contents

See the following file for:

EC 2.3.1.151 to EC 2.3.1.222

Accepted name: formylmethanofuran—tetrahydromethanopterin N-formyltransferase

Reaction: formylmethanofuran + 5,6,7,8-tetrahydromethanopterin = methanofuran + 5-formyl-5,6,7,8-tetrahydromethanopterin

For diagram of reaction click here

Glossary: methanofuran = 4-[4-(2-{[(4R*,5S*)-4,5,7-tricarboxyheptanoyl]-γ-L-glutamyl-γ-L-glutamylamino}ethyl)phenoxymethyl]furfurylamine
tetrahydromethanopterin = 1-(4-{(1R)-1-[(6S,7S)-2-amino-7-methyl-4-oxo-3,4,5,6,7,8-hexahydropteridin-6-yl]ethylamino}phenyl)-1-deoxy-5-O-{5-O-[(1S)-1,3-dicarboxypropylphosphonato]-α-D-ribofuranosyl}-D-ribitol

Other name(s): formylmethanofuran-tetrahydromethanopterin formyltransferase; formylmethanofuran:tetrahydromethanopterin formyltransferase; N-formylmethanofuran(CHO-MFR):tetrahydromethanopterin(H4MPT) formyltransferase; FTR; formylmethanofuran:5,6,7,8-tetrahydromethanopterin N⁵-formyltransferase

Systematic name: formylmethanofuran:5,6,7,8-tetrahydromethanopterin 5-formyltransferase

Comments: Methanofuran is a complex 4-substituted furfurylamine and is involved in the formation of methane from CO₂ in Methanobacterium thermoautotrophicum.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, CAS registry number: 105669-83-8

References:

1. Donnelly, M.I. and Wolfe, R.S. The role of formylmethanofuran: tetrahydromethanopterin formyltransferase in methanogenesis from carbon dioxide. J. Biol. Chem. 261 (1986) 16653-16659. [PMID: 3097011]

2. Leigh, J.A., Rinehart, K.L. and Wolfe, R.S. Structure of methanofuran, the carbon-dioxide reduction factor of Methanobacterium thermoautotrophicum. J. Am. Chem. Soc. 106 (1984) 3636-3640.

EC 2.3.1.102

Accepted name: N⁶-hydroxylysine O-acetyltransferase

Reaction: acetyl-CoA + N⁶-hydroxy-L-lysine = CoA + N⁶-acetyl-N⁶-hydroxy-L-lysine

Other name(s): N⁶-hydroxylysine:acetyl CoA N⁶-transacetylase; N⁶-hydroxylysine acetylase

Systematic name: acetyl-CoA:N⁶-hydroxy-L-lysine 6-acetyltransferase

Comments: Involved in the synthesis of aerobactin from lysine in a strain of Escherichia coli.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 101077-53-6

References:

1. Coy, M., Paw, B.H., Bindereif, A. and Neilands, J.B. Isolation and properties of N^ε-hydroxylysine:acetyl coenzyme A N^ε-transacetylase from Escherichia coli pABN11. Biochemistry 25 (1986) 2485-2489. [PMID: 3521734]

2. De Lorenzo, V., Bindereif, A., Paw, B.H. and Neilands, J.B. Aerobactin biosynthesis and transport genes of plasmid ColV-K30 in Escherichia coli K-12. J. Bacteriol. 165 (1986) 570-578. [PMID: 2935523]

EC 2.3.1.103

Accepted name: sinapoylglucose—sinapoylglucose O-sinapoyltransferase

Reaction: 2 1-O-sinapoyl β-D-glucoside = D-glucose + 1,2-bis-O-sinapoyl β-D-glucoside

Other name(s): hydroxycinnamoylglucose-hydroxycinnamoylglucose hydroxycinnamoyltransferase; 1-(hydroxycinnamoyl)-glucose:1-(hydroxycinnamoyl)-glucose hydroxycinnamoyltransferase

Systematic name: 1-O-(4-hydroxy-3,5-dimethoxycinnamoyl)-β-D-glucoside:1-O-(4-hydroxy-3,5-dimethoxycinnamoyl)-β-D-glucoside 1-O-sinapoyltransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 103537-11-7

References:

1. Dahlbender, B. and Strack, D. Purification and properties of 1-(hydroxycinnamoyl)-glucose-1-(hydroxycinnamoyl)-glucose hydroxycinnamoyl-transferase from radish seedlings. Phytochemistry 25 (1986) 1043-1046.

[EC 2.3.1.104 Deleted entry: 1-alkenylglycerophosphocholine O-acyltransferase. The activity is covered by EC 2.3.1.25, plasmalogen synthase (EC 2.3.1.104 created 1989, deleted 2013)]

EC 2.3.1.105

Accepted name: alkylglycerophosphate 2-O-acetyltransferase

Reaction: acetyl-CoA + 1-alkyl-sn-glycero-3-phosphate = CoA + 1-alkyl-2-acetyl-sn-glycero-3-phosphate

Other name(s): alkyllyso-GP:acetyl-CoA acetyltransferase

Systematic name: acetyl-CoA:1-alkyl-sn-glycero-3-phosphate 2-O-acetyltransferase

Comments: Involved in the biosynthesis of thrombocyte activating factor in animal tissues.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 76773-96-1 (not distinguishable from EC 2.3.1.67 1-alkylglycerophosphocholine O-acetyltransferase in Chemical Abstracts)

References:

1. Lee, T.-C., Malone, B. and Snyder, F. A new de novo pathway for the formation of 1-alkyl-2-acetyl-sn-glycerols, precursors of platelet activating factor. Biochemical characterization of 1-alkyl-2-lyso-sn-glycero-3-P:acetyl-CoA acetyltransferase in rat spleen. J. Biol. Chem. 261 (1986) 5373-5377. [PMID: 3007498]

EC 2.3.1.106

Accepted name: tartronate O-hydroxycinnamoyltransferase

Reaction: sinapoyl-CoA + 2-hydroxymalonate = CoA + sinapoyltartronate

For diagram click here.

Glossary:
sinapic acid = 4-hydroxy-3,5-dimethoxycinnamic acid
tartonic acid = 2-hydroxymalonic acid

Other name(s): tartronate sinapoyltransferase; hydroxycinnamoyl-coenzyme-A:tartronate hydroxycinnamoyltransferase

Systematic name: sinapoyl-CoA:2-hydroxymalonate O-(hydroxycinnamoyl)transferase

Comments: 4-Coumaroyl-CoA (4-hydroxycinnamoyl-CoA), caffeoyl-CoA (3,4-dihydroxycinnamoyl-CoA) and feruloyl-CoA (4-hydroxy-3-methoxycinnamoyl-CoA) can also act as donors for the enzyme from the mung bean (Vigna radiata).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 102484-57-1

References:

1. Strack, D., Ruhoff, R. and Gräwe, W. Hydroxycinnamoyl-Coenzyme-A-tartronate hydroxycinnamoyltransferase in protein preparations from mung bean. Phytochemistry 25 (1986) 833-837.

EC 2.3.1.107

Accepted name: deacetylvindoline O-acetyltransferase

Reaction: acetyl-CoA + deacetylvindoline = CoA + vindoline

For diagram click here.

Other name(s): deacetylvindoline acetyltransferase; DAT; 17-O-deacetylvindoline-17-O-acetyltransferase; acetylcoenzyme A-deacetylvindoline 4-O-acetyltransferase; acetyl-CoA-17-O-deacetylvindoline 17-O-acetyltransferase; acetylcoenzyme A:deacetylvindoline 4-O-acetyltransferase; acetylcoenzyme A:deacetylvindoline O-acetyltransferase; 17-O-deacetylvindoline O-acetyltransferase; acetyl-CoA:17-O-deacetylvindoline 17-O-acetyltransferase

Systematic name: acetyl-CoA:deacetylvindoline 4-O-acetyltransferase

Comments: Catalyses the final step in the biosynthesis of vindoline from tabersonine in the Madagascar periwinkle, Catharanthus roseus.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 100630-41-9

References:

1. Fahn, W., Gundlach, H., Deus-Neumann, B. and Stöckigt, J. Late enzymes of vindoline biosynthesis. Acetyl-CoA:17-O-deactylvindoline 17-O-acetyl-transferase. Plant Cell Rep. 4 (1985) 333-336.

EC 2.3.1.108

Accepted name: α-tubulin N-acetyltransferase

Reaction: acetyl-CoA + [α-tubulin]-L-lysine = CoA + [α-tubulin]-N⁶-acetyl-L-lysine

Other name(s): α-tubulin acetylase; TAT; α-tubulin acetyltransferase; tubulin N-acetyltransferase; acetyl-CoA:α-tubulin-L-lysine N^ε-acetyltransferase

Systematic name: acetyl-CoA:[α-tubulin]-L-lysine N⁶-acetyltransferase

Comments: The enzyme from Chlamydomonas flagella also acetylates mammalian brain α-tubulin.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 99889-90-4

References:

1. Greer, K., Maruta, H., L'Hernault, S.W. and Rosenbaum, J.L. α-Tubulin acetylase activity in isolated Chlamydomonas flagella. J. Cell Biol. 101 (1985) 2081-2084. [PMID: 4066751]

EC 2.3.1.109

Accepted name: arginine N-succinyltransferase

Reaction: succinyl-CoA + L-arginine = CoA + N²-succinyl-L-arginine

For diagram, click here

Other name(s): arginine succinyltransferase; AstA; arginine and ornithine N²-succinyltransferase; AOST; AST

Systematic name: succinyl-CoA:L-arginine N²-succinyltransferase

Comments: Also acts on L-ornithine. This is the first enzyme in the arginine succinyltransferase (AST) pathway for the catabolism of arginine [1]. This pathway converts the carbon skeleton of arginine into glutamate, with the concomitant production of ammonia and conversion of succinyl-CoA into succinate and CoA. The five enzymes involved in this pathway are EC 2.3.1.109 (arginine N-succinyltransferase), EC 3.5.3.23 (N-succinylarginine dihydrolase), EC 2.6.1.81 (succinylornithine transaminase), EC 1.2.1.71 (succinylglutamate-semialdehyde dehydrogenase) and EC 3.5.1.96 (succinylglutamate desuccinylase) [2,6].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 99676-48-9

References:

1. Vander Wauven, C., Jann, A., Haas, D., Leisinger, T. and Stalon, V. N²-succinylornithine in ornithine catabolism of Pseudomonas aeruginosa. Arch. Microbiol. 150 (1988) 400-404. [PMID: 3144259]

2. Vander Wauven, C. and Stalon, V. Occurrence of succinyl derivatives in the catabolism of arginine in Pseudomonas cepacia. J. Bacteriol. 164 (1985) 882-886. [PMID: 2865249]

3. Tricot, C., Vander Wauven, C., Wattiez, R., Falmagne, P. and Stalon, V. Purification and properties of a succinyltransferase from Pseudomonas aeruginosa specific for both arginine and ornithine. Eur. J. Biochem. 224 (1994) 853-861. [PMID: 7523119]

4. Itoh, Y. Cloning and characterization of the aru genes encoding enzymes of the catabolic arginine succinyltransferase pathway in Pseudomonas aeruginosa. J. Bacteriol. 179 (1997) 7280-7290. [PMID: 9393691]

5. Schneider, B.L., Kiupakis, A.K. and Reitzer, L.J. Arginine catabolism and the arginine succinyltransferase pathway in Escherichia coli. J. Bacteriol. 180 (1998) 4278-4286. [PMID: 9696779]

6. Cunin, R., Glansdorff, N., Pierard, A. and Stalon, V. Biosynthesis and metabolism of arginine in bacteria. Microbiol. Rev. 50 (1986) 314-352. [PMID: 3534538]

EC 2.3.1.110

Accepted name: tyramine N-feruloyltransferase

Reaction: feruloyl-CoA + tyramine = CoA + N-feruloyltyramine

Other name(s): tyramine N-feruloyl-CoA transferase; feruloyltyramine synthase; feruloyl-CoA tyramine N-feruloyl-CoA transferase; tyramine feruloyltransferase

Systematic name: feruloyl-CoA:tyramine N-(hydroxycinnamoyl)transferase

Comments: Cinnamoyl-CoA, 4-coumaroyl-CoA and sinapoyl-CoA can also act as donors, and some aromatic amines can act as acceptors.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 128909-19-3

References:

1. Negrel, J. and Martin, C. The biosynthesis of feruloyltyramine in Nicotiana tabacum. Phytochemistry 23 (1984) 2797-2801.

EC 2.3.1.111

Accepted name: mycocerosate synthase

Reaction: acyl-CoA + n methylmalonyl-CoA + 2n NADPH + 2n H⁺ = multi-methyl-branched acyl-CoA + n CoA + n CO₂ + 2n NADP⁺

Other name(s): mycocerosic acid synthase

Systematic name: acyl-CoA:methylmalonyl-CoA C-acyltransferase (decarboxylating, oxoacyl- and enoyl-reducing)

Comments: The enzyme elongates CoA esters of fatty acids from C₆ to C₂₀ by incorporation of methylmalonyl, but not malonyl, residues, to form multimethyl-branched fatty-acyl-CoAs such as 2,4,6,8-tetramethyl-octanoyl-CoA.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 95229-19-9

References:

1. Rainwater, D.L. and Kollattukudy, P.E. Fatty acid biosynthesis in Mycobacterium tuberculosis var. bovis Bacillus Calmette-Guerin. Purification and characterization of a novel fatty acid synthase, mycocerosic acid synthase, which elongates n-fatty acyl-CoA with methylmalonyl-CoA. J. Biol. Chem. 260 (1985) 616-623. [PMID: 3880746]

EC 2.3.1.112

Accepted name: D-tryptophan N-malonyltransferase

Reaction: malonyl-CoA + D-tryptophan = CoA + N²-malonyl-D-tryptophan

Systematic name: malonyl-CoA:D-tryptophan N-malonyltransferase

Comments: 1-Aminocyclopropane-1-carboxylate can act instead of malonyl-CoA.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 94490-01-4

References:

1. Matern, U., Feser, C. and Heller, W. N-Malonyltransferases from peanut. Arch. Biochem. Biophys. 235 (1984) 218-227. [PMID: 6497391]

EC 2.3.1.113

Accepted name: anthranilate N-malonyltransferase

Reaction: malonyl-CoA + anthranilate = CoA + N-malonylanthranilate

Systematic name: malonyl-CoA:anthranilate N-malonyltransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 94489-98-2

References:

1. Matern, U., Feser, C. and Heller, W. N-Malonyltransferases from peanut. Arch. Biochem. Biophys. 235 (1984) 218-227. [PMID: 6497391]

EC 2.3.1.114

Accepted name: 3,4-dichloroaniline N-malonyltransferase

Reaction: malonyl-CoA + 3,4-dichloroaniline = CoA + N-(3,4-dichlorophenyl)-malonamate

Systematic name: malonyl-CoA:3,4-dichloroaniline N-malonyltransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 94489-99-3

References:

1. Matern, U., Feser, C. and Heller, W. N-Malonyltransferases from peanut. Arch. Biochem. Biophys. 235 (1984) 218-227. [PMID: 6497391]

EC 2.3.1.115

Accepted name: isoflavone-7-O-β-glucoside 6"-O-malonyltransferase

Reaction: malonyl-CoA + biochanin A 7-O-β-D-glucoside = CoA + biochanin A 7-O-(6-O-malonyl-β-D-glucoside)

See diagram for reaction with 7-O-β-D-glucosides of biochanin A or apigenin.

Other name(s): flavone/flavonol 7-O-β-D-glucoside malonyltransferase; flavone (flavonol) 7-O-glycoside malonyltransferase; malonyl-CoA:flavone/flavonol 7-O-glucoside malonyltransferase; MAT-7; malonyl-coenzyme A:isoflavone 7-O-glucoside-6"-malonyltransferase; malonyl-coenzyme A:flavone/flavonol-7-O-glycoside malonyltransferase

Systematic name: malonyl-CoA:isoflavone-7-O-β-D-glucoside 6"-O-malonyltransferase

Comments: The 6-position of the glucose residue of formononetin can also act as acceptor; some other 7-O-glucosides of isoflavones, flavones and flavonols can also act, but more slowly.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 93585-97-8 and 78413-09-9

References:

1. Koester, J., Bussmann, R. and Barz, W. Malonyl-coenzyme A:isoflavone 7-O-glucoside-6"-O-malonyltransferase from roots of chick pea (Cicer arietinum L.). Arch. Biochem. Biophys. 234 (1984) 513-521. [PMID: 6497385]

2. Matern, U., Feser, C. and Hammer, D. Further characterization and regulation of malonyl-coenzyme A: flavonoid glucoside malonyltransferases from parsley cell suspension cultures. Arch. Biochem. Biophys. 226 (1983) 206-217. [PMID: 6639051]

EC 2.3.1.116

Accepted name: flavonol-3-O-β-glucoside O-malonyltransferase

Reaction: malonyl-CoA + flavonol 3-O-β-D-glucoside = CoA + flavonol 3-O-(6-O-malonyl-β-D-glucoside)

For diagram click here.

Other name(s): flavonol 3-O-glucoside malonyltransferase; MAT-3; malonyl-coenzyme A:flavonol-3-O-glucoside malonyltransferase

Systematic name: malonyl-CoA:flavonol-3-O-β-D-glucoside 6"-O-malonyltransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 78413-11-3

References:

1. Matern, U., Feser, C. and Hammer, D. Further characterization and regulation of malonyl-coenzyme A: flavonoid glucoside malonyltransferases from parsley cell suspension cultures. Arch. Biochem. Biophys. 226 (1983) 206-217. [PMID: 6639051]

EC 2.3.1.117

Accepted name: 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase

Reaction: succinyl-CoA + (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + H₂O = CoA + N-succinyl-L-2-amino-6-oxoheptanedioate

For diagram click here.

Glossary:
dipicolinate = pyridine-2,6-dicarboxylate

Other name(s): tetrahydropicolinate succinylase; tetrahydrodipicolinate N-succinyltransferase; tetrahydrodipicolinate succinyltransferase; succinyl-CoA:tetrahydrodipicolinate N-succinyltransferase; succinyl-CoA:2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase

Systematic name: succinyl-CoA:(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase

Comments: Involved in the biosynthesis of lysine in bacteria (including cyanobacteria) and higher plants. The 1992 edition of the Enzyme List erroneously gave the name 2,3,4,5-tetrahydropyridine-2-carboxylate N-succinyltransferase to this enzyme.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 88086-34-4

References:

1. Simms, S.A., Voige, W.H. and Gilvarg, C. Purification and characterization of succinyl-CoA: tetrahydrodipicolinate N-succinyltransferase from Escherichia coli. J. Biol. Chem. 259 (1984) 2734-2741. [PMID: 6365916]

EC 2.3.1.118

Accepted name: N-hydroxyarylamine O-acetyltransferase

Reaction: acetyl-CoA + an N-hydroxyarylamine = CoA + an N-acetoxyarylamine

Other name(s): arylhydroxamate N,O-acetyltransferase; arylamine N-acetyltransferase; N-hydroxy-2-aminofluorene-O-acetyltransferase

Systematic name: acetyl-CoA:N-hydroxyarylamine O-acetyltransferase

Comments: The enzyme from liver, but not that from bacteria, can also catalyse N-acetylation of arylamines and N,O-acetylation of arylhydroxamates.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 100984-92-7

References:

1. Saito, K., Shinohara, A. and Kamataki, T. N-Hydroxyarylamine O-acetyltransferase in hamster liver: identity with arylhydroxamic acid N,O-acetyltransferase and arylamine N-acetyltransferase. J. Biochem. (Tokyo) 99 (1986) 1689-1697. [PMID: 3745141]

EC 2.3.1.119

Accepted name: icosanoyl-CoA synthase

Reaction: stearoyl-CoA + malonyl-CoA + 2 NAD(P)H + 2 H⁺ = icosanoyl-CoA + CO₂ + CoA + 2 NAD(P)⁺ + H₂O

Other name(s): acyl-CoA elongase; C₁₈-CoA elongase; stearoyl-CoA elongase

Systematic name: stearoyl-CoA:malonyl-CoA C-acyltransferase (decarboxylating, oxoacyl- and enoyl-reducing)

Comments: Icosanoyl-CoA can act in place of stearoyl-CoA. The membrane enzyme brings about the elongation of these long-chain fatty-acyl-CoAs.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 141256-55-5

References:

1. Bessoule, J.-J., Lessire, R. and Cassagne, C. Partial purification of the acyl-CoA elongase of Allium porrum leaves. Arch. Biochem. Biophys. 268 (1989) 475-484. [PMID: 2913944]

2. Bessoule, J.-J., Lessire, R., Rigoulet, M., Guerin, B. and Cassagne, C. Fatty acid synthesis in mitochondria from Saccharomyces cerevisiae. FEBS Lett. 214 (1987) 158-162. [PMID: 3552725]

3. Lessire, R., Bessoule, J.-J. and Cassagne, C. Solubilization of C₁₈ CoA and C₂₀ CoA elongases from Allium porrum L. epidermal-cell microsomes. FEBS Lett. 187 (1985) 314-320.

[EC 2.3.1.120 Deleted entry: 6'-deoxychalcone synthase. The reaction listed is due to EC 2.3.1.74 naringenin-chalcone synthase (EC 2.3.1.120 created 1990, deleted 1992)]

EC 2.3.1.121

Accepted name: 1-alkenylglycerophosphoethanolamine O-acyltransferase

Reaction: acyl-CoA + 1-alkenylglycerophosphoethanolamine = CoA + 1-alkenyl-2-acylglycerophosphoethanolamine

Systematic name: acyl-CoA:1-alkenylglycerophosphoethanolamine O-acyltransferase

Comments: Long-chain unsaturated acyl-CoAs are the best substrates.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 112445-17-7

References:

1. Arthur, G., Page, L. and Choy, P.C. Acylation of 1-alkenylglycerophosphoethanolamine and 1-acylglycerophosphoethanolamine in guinea-pig heart microsomes. Biochim. Biophys. Acta 921 (1987) 259-265. [PMID: 3651487]

EC 2.3.1.122

Accepted name: trehalose O-mycolyltransferase

Reaction: 2 α,α-trehalose 6-mycolate = α,α-trehalose + α,α-trehalose 6,6'-bismycolate

Other name(s): α,α'-trehalose 6-monomycolate:α,α'-trehalose mycolyltransferase; α,α&'-trehalose-6-mycolate:α,α'-trehalose-6-mycolate 6'-mycolyltransferase

Systematic name: α,α-trehalose-6-mycolate:α,α-trehalose-6-mycolate 6'-mycolyltransferase

Comments: Catalyses the exchange of mycolic acid between trehalose, trehalose mycolate and trehalose bismycolate. Trehalose 6-palmitate can also act as donor.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 111694-11-2

References:

1. Sathyamoorthy, N. and Takayama, K. Purification and characterization of a novel mycolic acid exchange enzyme from Mycobacterium smegmatis. J. Biol. Chem. 262 (1987) 13417-13423. [PMID: 3654621]

EC 2.3.1.123

Accepted name: dolichol O-acyltransferase

Reaction: palmitoyl-CoA + dolichol = CoA + dolichyl palmitate

Other name(s): acyl-CoA:dolichol acyltransferase

Systematic name: palmitoyl-CoA:dolichol O-palmitoyltransferase

Comments: Other acyl-CoAs can also act, but more slowly. α-Saturated dolichols are acylated more rapidly than the α-unsaturated analogues.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 111839-04-4

References:

1. Tollbom, Ö., Valtersson, C., Chojnacki, T. and Dallner, G. Esterification of dolichol in rat liver. J. Biol. Chem. 263 (1988) 1347-1352. [PMID: 3121628]

[EC 2.3.1.124 Deleted entry: already listed as EC 2.3.1.20 diacylglycerol O-acyltransferase (EC 2.3.1.124 created 1990, deleted 1992)]

EC 2.3.1.125

Accepted name: 1-alkyl-2-acetylglycerol O-acyltransferase

Reaction: acyl-CoA + 1-O-alkyl-2-acetyl-sn-glycerol = CoA + 1-O-alkyl-2-acetyl-3-acyl-sn-glycerol

Other name(s): 1-hexadecyl-2-acetylglycerol acyltransferase

Systematic name: acyl-CoA:1-O-alkyl-2-acetyl-sn-glycerol O-acyltransferase

Comments: A number of acyl-CoAs can act as acyl donor; maximum activity is obtained with linoleoyl-CoA. Not identical with EC 2.3.1.20 diacylglycerol O-acyltransferase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 114704-90-4

References:

1. 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]

EC 2.3.1.126

Accepted name: isocitrate O-dihydroxycinnamoyltransferase

Reaction: caffeoyl-CoA + isocitrate = CoA + 2-O-caffeoylisocitrate

2-O-caffeoylisocitrate = (1R,2S)-1-{[3-(E)-(3,4-dihydroxyphenyl)acryloyl]oxy}propane-1,2,3-tricarboxylate = (3S,4R)-3-carboxy-2,3-dideoxy-4-O-[(2E)-3-(3,4-dihydroxyphenyl)prop-2-enoyl]pentarate
isocitrate = (1R,2S)-1-hydroxypropane-1,2,3-tricarboxylate = threo-D_s-isocitrate

Systematic name: caffeoyl-CoA:isocitrate 2-O-(3,4-dihydroxycinnamoyl)transferase

Comments: Feruloyl-CoA and 4-coumaroyl-CoA can also act as donors.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 112352-88-2

References:

1. Strack, D., Leicht, P., Bokern, M., Wray, V. and Grotjahn, L. Hydroxycinnamic acid-esters of isocitric acid - accumulation and enzymatic-synthesis in Amaranthus cruentus. Phytochemistry 26 (1987) 2919-2922.

EC 2.3.1.127

Accepted name: ornithine N-benzoyltransferase

Reaction: 2 benzoyl-CoA + L-ornithine = 2 CoA + N²,N⁵-dibenzoyl-L-ornithine

Other name(s): ornithine N-acyltransferase

Systematic name: benzoyl-CoA:L-ornithine N-benzoyltransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 111693-97-1

References:

1. Seymour, M.A., Millburn, P. and Tait, G.H. Renal biosynthesis of ornithuric acid in quail. Biochem. Soc. Trans. 15 (1987) 1108-1109.

EC 2.3.1.128

Accepted name: ribosomal-protein-alanine N-acetyltransferase

Reaction: acetyl-CoA + ribosomal-protein L-alanine = CoA + ribosomal-protein N-acetyl-L-alanine

Other name(s): ribosomal protein S18 acetyltransferase

Systematic name: acetyl-CoA:ribosomal-protein-L-alanine N-acetyltransferase

Comments: A group of enzymes in Escherichia coli that acetylate the N-terminal alanine residues of specific ribosomal proteins. cf. EC 2.3.1.88, peptide α-N-acetyltransferase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 113383-52-1

References:

1. Yoshikawa, A., Isono, S., Sheback, A. and Isono, K. Cloning and nucleotide sequencing of the genes rimI and rimJ which encode enzymes acetylating ribosomal proteins S18 and S5 of Escherichia coli K12. Mol. Gen. Genet. 209 (1987) 481-488. [PMID: 2828880]

EC 2.3.1.129

Accepted name: acyl-[acyl-carrier-protein]—UDP-N-acetylglucosamine O-acyltransferase

Reaction: an (R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetyl-α-D-glucosamine = an [acyl-carrier protein] + UDP-3-O-[(3R)-3-hydroxytetradecanoyl)-N-acetyl-α-D-glucosamine

Glossary: tetradecanoyl = myristoyl

Other name(s): UDP-N-acetylglucosamine acyltransferase; uridine diphosphoacetylglucosamine acyltransferase

Systematic name: (R)-3-hydroxytetradecanoyl-[acyl-carrier protein]:UDP-N-acetylglucosamine 3-O-(3-hydroxytetradecanoyl)transferase

Comments: Involved with EC 2.4.1.182 (lipid-A-disaccharide synthase) and EC 2.7.1.130 (tetraacyldisaccharide 4'-kinase) in the biosynthesis of the phosphorylated glycolipid, Lipid A, in the outer membrane of Escherichia coli.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 105843-69-4

References:

1. Anderson, M.S., Bulawa, C.E. and Raetz, C.R.H. The biosynthesis of gram-negative endotoxin. Formation of lipid A precursors from UDP-GlcNAc in extracts of Escherichia coli. J. Biol. Chem. 260 (1985) 15536-15541. [PMID: 3905795]

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.

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.

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.

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, 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.

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.

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, 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. [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. [PMID: 9920938]

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, 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]

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]

EC 2.3.1.138

Accepted name: putrescine N-hydroxycinnamoyltransferase

Reaction: caffeoyl-CoA + putrescine = CoA + N-caffeoylputrescine

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.

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.

EC 2.3.1.140

Accepted name: rosmarinate synthase

Reaction: caffeoyl-CoA + (R)-3-(3,4-dihydroxyphenyl)lactate = CoA + rosmarinate

For diagram of reaction click here.

Glossary: (R)-3-(3,4-dihydroxyphenyl)lactate = (2R)-3-(3,4-dihydroxyphenyl)-2-hydroxypropanoate
rosmarinate = (2R)-3-(3,4-dihydroxyphenyl)-2-{[(2E)-3-(3,4-dihydroxyphenyl)prop-2-enoyl]oxy}propanoate

Other name(s): rosmarinic acid synthase; caffeoyl-coenzyme A:3,4-dihydroxyphenyllactic acid caffeoyltransferase; 4-coumaroyl-CoA:4-hydroxyphenyllactic acid 4-coumaroyl transferase; RAS (gene name)

Systematic name: caffeoyl-CoA:(R)-3-(3,4-dihydroxyphenyl)lactate 2'-O-caffeoyl-transferase

Comments: Involved, with EC 1.1.1.237 (hydroxyphenylpyruvate reductase) in the biosynthesis of rosmarinic acid. Characterized from the plant Melissa officinalis L.(lemon balm).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 117590-80-4

References:

1. Petersen, M. and Alfermann, A.W. Two new enzymes of rosmarinic acid biosynthesis from cell cultures of Coleus blumei: hydroxyphenylpyruvate reductase and rosmarinic acid synthase. Z. Naturforsch. C: Biosci. 43 (1988) 501-504.

2. Petersen, M. S. Characterization of rosmarinic acid synthase from cell cultures of Coleus blumei. Phytochemistry 30 (1991) 2877-2881.

3. Weitzel, C. and Petersen, M. Cloning and characterisation of rosmarinic acid synthase from Melissa officinalis L. Phytochemistry 72 (2011) 572-578. [PMID: 21354582]

EC 2.3.1.141

Accepted name: galactosylacylglycerol O-acyltransferase

Reaction: an acyl-[acyl-carrier protein] + sn-3-D-galactosyl-sn-2-acylglycerol = an [acyl-carrier protein] + D-galactosyldiacylglycerol

Other name(s): acyl-acyl-carrier protein: lysomonogalactosyldiacylglycerol acyltransferase; acyl-ACP:lyso-MGDG acyltransferase

Systematic name: acyl-[acyl-carrier protein]:D-galactosylacylglycerol O-acyltransferase

Comments: Transfers long-chain acyl groups to the sn-1 position of the glycerol residue.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 119129-68-9

References:

1. Chen, H.-H., Wickrema, A. and Jaworski, J.G. Acyl-acyl-carrier protein: lysomonogalactosyldiacylglycerol acyltransferase from the cyanobacterium Anabaena variabilis. Biochim. Biophys. Acta 963 (1988) 493-500. [PMID: 3143419]

EC 2.3.1.142

Accepted name: glycoprotein O-fatty-acyltransferase

Reaction: palmitoyl-CoA + mucus glycoprotein = CoA + O-palmitoylglycoprotein

Other name(s): protein acyltransferase

Systematic name: fatty-acyl-CoA:mucus-glycoprotein fatty-acyltransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 122191-29-1

References:

1. Kasinathan, C., Grzelinska, E., Okazaki, F., Slomiany, B.L. and Slomiany, A. Purification of protein fatty acyltransferase and determination of its distribution and topology. J. Biol. Chem. 265 (1990) 5139-5144. [PMID: 2318887]

EC 2.3.1.143

Accepted name: β-glucogallin—tetrakisgalloylglucose O-galloyltransferase

Reaction: 1-O-galloyl-β-D-glucose + 1,2,3,6-tetrakis-O-galloyl-β-D-glucose = D-glucose + 1,2,3,4,6-pentakis-O-galloyl-β-D-glucose

Other name(s): β-glucogallin-tetragalloylglucose 4-galloyltransferase; β-glucogallin:1,2,3,6-tetra-O-galloylglucose 4-O-galloyltransferase; β-glucogallin:1,2,3,6-tetra-O-galloyl-β-D-glucose 4-O-galloyltransferase

Systematic name: 1-O-galloyl-β-D-glucose:1,2,3,6-tetrakis-O-galloyl-β-D-glucose 4-O-galloyltransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 122653-70-7

References:

1. Cammann, J., Denzel, K., Schilling, G. and Gross, G.G. Biosynthesis of gallotannins: β-glucogallin-dependent formation of 1,2,3,4,6-pentagalloylglucose by enzymatic galloylation of 1,2,3,6-tetragalloylglucose. Arch. Biochem. Biophys. 273 (1989) 58-63. [PMID: 2757399]

EC 2.3.1.144

Accepted name: anthranilate N-benzoyltransferase

Reaction: benzoyl-CoA + anthranilate = CoA + N-benzoylanthranilate

Systematic name: benzoyl-CoA:anthranilate N-benzoyltransferase

Comments: Cinnamoyl-CoA, 4-coumaroyl-CoA and salicyloyl-CoA can act as donors, but more slowly. Involved in the biosynthesis of phytoalexins.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 125498-59-1

References:

1. Reinhard, K. and Matern, U. The biosynthesis of phytoalexins in Dianthus caryophyllus L. cell cultures: induction of benzoyl-CoA:anthranilate N-benzoyltransferase activity. Arch. Biochem. Biophys. 275 (1989) 295-301. [PMID: 2817901]

EC 2.3.1.145

Accepted name: piperidine N-piperoyltransferase

Reaction: (E,E)-piperoyl-CoA + piperidine = CoA + N-[(E,E)-piperoyl]-piperidine

Other name(s): piperidine piperoyltransferase; piperoyl-CoA:piperidine N-piperoyltransferase

Systematic name: (E,E)-piperoyl-CoA:piperidine N-piperoyltransferase

Comments: Pyrrolidine and 3-pyrroline can also act as acceptors, but more slowly.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 126806-22-2

References:

1. Geisler, J.G. and Gross, G.G. The biosynthesis of piperine in Piper nigrum. Phytochemistry 29 (1990) 489-492.

EC 2.3.1.146

Accepted name: pinosylvin synthase

Reaction: 3 malonyl-CoA + cinnamoyl-CoA = 4 CoA + pinosylvin + 4 CO₂

For diagram click here.

Other name(s): stilbene synthase; pine stilbene synthase

Systematic name: malonyl-CoA:cinnamoyl-CoA malonyltransferase (cyclizing)

Comments: Not identical with EC 2.3.1.74 (naringenin-chalcone synthase) or EC 2.3.1.95 (trihydroxystilbene synthase).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 72994-49-1

References:

1. Gehlert, R., Schöppner, A. and Kindl, H. Stilbene synthase from seedlings of Pinus sylvestris - purification and induction in response to fungal infection. Mol. Plant-Microbe Interaction 3 (1990) 444-449.

EC 2.3.1.147

Accepted name: glycerophospholipid arachidonoyl-transferase (CoA-independent)

Reaction: 1-organyl-2-arachidonoyl-sn-glycero-3-phosphocholine + 1-organyl-2-lyso-sn-glycero-3-phosphoethanolamine = 1-organyl-2-arachidonoyl-sn-glycero-3-phosphoethanolamine + 1-organyl-2-lyso-sn-glycero-3-phosphocholine

Systematic name: 1-organyl-2-arachidonoyl-sn-glycero-3-phosphocholine:1-organyl-2-lyso-sn-glycero-3-phosphoethanolamine arachidonoyltransferase (CoA-independent)

Comments: catalyses the transfer of arachidonate and other polyenoic fatty acids from intact choline or ethanolamine-containing glycerophospholipids to the sn-2 position of a lyso-glycerophospholipid. The organyl group on sn-1 of the donor or acceptor molecule can be alkyl, acyl or alk-1-enyl. The term 'radyl' has sometimes been used to refer to such substituting groups. Differs from EC 2.3.1.148 glycerophospholipid acyltransferase (CoA-dependent) in not requiring CoA and in its specificity for poly-unsaturated acyl groups.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 102347-79-5

References:

1. Robinson, M., Blank, M.L., Snyder, F. Acylation of lysophospholipids by rabbit alveolar macrophages. Specific CoA-dependent and CoA-independent reactions. J. Biol. Chem. 260 (1985) 7889-7895. [PMID: 4008481]

2. Snyder, F., Lee, T.C., Blank, M.L. The role of transacylases in the metabolism of arachidonate and platelet-activating factor. Prog. Lipid Res. 31 (1992) 65-86. [PMID: 1641397]

EC 2.3.1.148

Accepted name: glycerophospholipid acyltransferase (CoA-dependent)

Reaction: 1-organyl-2-acyl-sn-glycero-3-phosphocholine + 1-organyl-2-lyso-sn-glycero-3-phosphoethanolamine = 1-organyl-2-acyl-sn-glycero-3-phosphoethanolamine + 1-organyl-2-lyso-sn-glycero-3-phosphocholine

Systematic name: 1-organyl-2-acyl-sn-glycero-3-phosphocholine:1-organyl-2-lyso-sn-glycero-3-phosphoethanolamine acyltransferase (CoA-dependent)

Comments: catalyses the transfer of fatty acids from intact choline- or ethanolamine-containing glycerophospholipids to the sn-2 position of a lyso-glycerophospholipid. The organyl group on sn-1 of the donor or acceptor molecule can be alkyl, acyl or alk-1-enyl. The term 'radyl' has sometimes been used to refer to such substituting groups. Differs from EC 2.3.1.147 glycerophospholipid arachidonoyl-transferase (CoA-independent) in requiring CoA and not favouring the transfer of polyunsaturated acyl groups.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9054-54-0

References:

1. Irvine, R.F., Dawson, R.M.C. Transfer of arachidonic acid between phospholipids in rat liver microsomes. Biochem. Biophys. Res. Commun. 91 (1979) 1399-1405. [PMID: 526311]

2. Robinson, M., Blank, M.L., Snyder, F. Acylation of lysophospholipids by rabbit alveolar macrophages. Specific CoA-dependent and CoA-independent reactions. J. Biol. Chem. 260 (1985) 7889-7895. [PMID: 4008481]

3. Snyder, F., Lee, T.C., Blank, M.L. The role of transacylases in the metabolism of arachidonate and platelet-activating factor. Prog. Lipid Res. 31 (1992) 65-86. [PMID: 1641397]

EC 2.3.1.149

Accepted name: platelet-activating factor acetyltransferase

Reaction: 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine + 1-organyl-2-lyso-sn-glycero-3-phospholipid = 1-organyl-2-lyso-sn-glycero-3-phosphocholine + 1-alkyl-2-acetyl-sn-glycero-3-phospholipid

Other name(s): PAF acetyltransferase

Systematic name: 1-alkyl-2-acyl-sn-glycero-3-phosphocholine:1-organyl-2-lyso-sn-glycero-3-phospholipid acetyltransferase

Comments: catalyses the transfer of the acetyl group from 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine (platelet-activating factor) to the sn-2 position of lyso-glycerophospholipids containing ethanolamine, choline, serine, inositol or phosphate groups at the sn-3 position as well as to sphingosine and long-chain fatty alcohols. The organyl group can be alkyl, acyl or alk-1-enyl (sometimes also collectively referred to as 'radyl').

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9012-30-0

References:

1. Lee, T.C., Uemura, Y., Snyder, F. A novel CoA-independent transacetylase produces the ethanolamine plasmalogen and acyl analogs of platelet-activating factor (PAF) with PAF as the acetate donor in HL-60 cells. J. Biol. Chem. 267 (1992) 19992-20001. [PMID: 1400315]

EC 2.3.1.150

Accepted name: salutaridinol 7-O-acetyltransferase

Reaction: acetyl-CoA + salutaridinol = CoA + 7-O-acetylsalutaridinol

For diagram click here.

Systematic name: acetyl-CoA:salutaridinol 7-O-acetyltransferase

Comments: the enzyme is present in the poppy, Papaver somniferum. At pH 8-9 the product, 7-O-acetylsalutaridinol, spontaneously closes the 45 oxide bridge by allylic elimination to form the morphine precursor thebaine

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 156859-13-1

References:

1. Lenz, R., Zenk, M.H. Closure of the oxide bridge in morphine biosynthesis. Tetrahedron Lett. 35 (1994) 3897-3900.

2. Lenz, R., Zenk, M.H. Acetyl-CoA:salutaridinol 7-O-acetyltransferase from Papaver somniferum plant cell cultures. The enzyme catalyzing the formation of thebaine in morphine biosynthesis. J. Biol. Chem. 270 (1995) 31091-31096. [PMID: 8537369]