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 2.3.1.200, EC 2.3.1.201 to EC 2.3.1.328

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, EAWAG-BBD, EXPASY, KEGG, Metacyc, PDB, 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 N-acetyltransferase

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

For diagram of reaction click here.

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

Glossary: 1-O-sinapoyl-β-D-glucose = 1-O-[(2E)-3-(4-hydroxy-3,5-dimethoxyphenyl)-2-propenoyl]-β-D-glucopyranose

Other name(s): hydroxycinnamoylglucose-hydroxycinnamoylglucose hydroxycinnamoyltransferase; 1-(hydroxycinnamoyl)-glucose:1-(hydroxycinnamoyl)-glucose hydroxycinnamoyltransferase; 1-O-(4-hydroxy-3,5-dimethoxycinnamoyl)-β-D-glucoside:1-O-(4-hydroxy-3,5-dimethoxycinnamoyl)-β-D-glucoside 1-O-sinapoyltransferase

Systematic name: 1-O-sinapoyl-β-D-glucose:1-O-sinnapoyl-β-D-glucose 1-O-sinapoyltransferase

Comments: The plant enzyme, characterized from Brassicaceae, is involved in secondary metabolism.

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): ATAT1 (gene name); MEC17 (gene name); α-tubulin acetylase; TAT; α-tubulin acetyltransferase; tubulin N-acetyltransferase (ambiguous); acetyl-CoA:α-tubulin-L-lysine N-acetyltransferase; acetyl-CoA:[α-tubulin]-L-lysine 6-N-acetyltransferase

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

Comments: The enzyme is conserved from protists to mammals and is present in flowering plants. In most organisms it acetylates L-lysine at position 40 of 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]

2. Akella, J.S., Wloga, D., Kim, J., Starostina, N.G., Lyons-Abbott, S., Morrissette, N.S., Dougan, S.T., Kipreos, E.T. and Gaertig, J. MEC-17 is an α-tubulin acetyltransferase. Nature 467 (2010) 218-222. [PMID: 20829795]

3. Shida, T., Cueva, J.G., Xu, Z., Goodman, M.B. and Nachury, M.V. The major α-tubulin K40 acetyltransferase αTAT1 promotes rapid ciliogenesis and efficient mechanosensation. Proc. Natl. Acad. Sci. USA 107 (2010) 21517-21522. [PMID: 21068373]

4. Taschner, M., Vetter, M. and Lorentzen, E. Atomic resolution structure of human α-tubulin acetyltransferase bound to acetyl-CoA. Proc. Natl. Acad. Sci. USA 109 (2012) 19649-19654. [PMID: 23071318]

5. Friedmann, D.R., Aguilar, A., Fan, J., Nachury, M.V. and Marmorstein, R. Structure of the α-tubulin acetyltransferase, αTAT1, and implications for tubulin-specific acetylation. Proc. Natl. Acad. Sci. USA 109 (2012) 19655-19660. [PMID: 23071314]

6. Kalebic, N., Sorrentino, S., Perlas, E., Bolasco, G., Martinez, C. and Heppenstall, P.A. αTAT1 is the major α-tubulin acetyltransferase in mice. Nat. Commun. 4 (2013) 1962. [PMID: 23748901]

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 (ambiguous); succinyl-CoA:L-arginine 2-N-succinyltransferase

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: (1) a long-chain acyl-[mycocerosic acid synthase] + 3 methylmalonyl-CoA + 6 NADPH + 6 H⁺ = a trimethylated-mycocerosoyl-[mycocerosate synthase] + 3 CoA + 3 CO₂ + 6 NADP⁺ + 3 H₂O
(2) a long-chain acyl-[mycocerosic acid synthase] + 4 methylmalonyl-CoA + 8 NADPH + 8 H⁺ = a tetramethylated-mycocerosoyl-[mycocerosate synthase] + 4 CoA + 4 CO₂ + 8 NADP⁺ + 4 H₂O

Glossary: mycocerosic acid = a long-chain fatty acid with 3 or 4 methyl branches at positions 2,4,6 or 2,4,6,8, respectively. The carbon atoms bearing the methyl groups have the (R)-configuration.

Other name(s): mas (gene name); mycocerosic acid synthase; acyl-CoA:methylmalonyl-CoA C-acyltransferase (decarboxylating, oxoacyl- and enoyl-reducing); long-chain acyl-CoA:methylmalonyl-CoA C-acyltransferase (mycocerosate-forming)

Systematic name: long-chain acyl-[mycocerosic acid synthase]:methylmalonyl-CoA C-acyltransferase (mycocerosate-forming)

Comments: The enzyme, characterized from mycobacteria, is loaded with a long-chain acyl moiety by EC 6.2.1.49, long-chain fatty acid adenylyltransferase FadD28, and elongates it by incorporation of three or four methylmalonyl (but not malonyl) residues, to form tri- or tetramethyl-branched fatty-acids, respectively, such as 2,4,6,8-tetramethyloctacosanoate (C₃₂-mycocerosate). Since the enzyme lacks a thioesterase domain, the product remains bound and requires additional enzyme(s) for removal. Even though the enzyme can accept C₆ to C₂₀ substrates in vitro, it prefers to act on C₁₄-C₂₀ substrates in vivo.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, 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-Guérin. 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]

2. Mathur, M. and Kolattukudy, P.E. Molecular cloning and sequencing of the gene for mycocerosic acid synthase, a novel fatty acid elongating multifunctional enzyme, from Mycobacterium tuberculosis var. bovis Bacillus Calmette-Guerin. J. Biol. Chem. 267 (1992) 19388-19395. [PMID: 1527058]

3. Trivedi, O.A., Arora, P., Vats, A., Ansari, M.Z., Tickoo, R., Sridharan, V., Mohanty, D. and Gokhale, R.S. Dissecting the mechanism and assembly of a complex virulence mycobacterial lipid. Mol. Cell 17 (2005) 631-643. [PMID: 15749014]

4. Menendez-Bravo, S., Comba, S., Sabatini, M., Arabolaza, A. and Gramajo, H. Expanding the chemical diversity of natural esters by engineering a polyketide-derived pathway into Escherichia coli. Metab. Eng. 24 (2014) 97-106. [PMID: 24831705]

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, PDB, 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 Deleted entry: icosanoyl-CoA synthase. Now covered by EC 2.3.1.199, very-long-chain 3-oxoacyl-CoA synthase, EC 1.1.1.330, very-long-chain 3-oxoacyl-CoA reductase, EC 4.2.1.134, very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase, and EC 1.3.1.93, very-long-chain enoyl-CoA reductase. (EC 2.3.1.119 created 1990, deleted 2015)]

[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: carbendazim hydrolysing esterase

Reaction: carbendazim + H₂O = 2-aminobenzimidazole + CO₂ + methanol (overall reaction)
(1a) carbendazim + H₂O = N-(1H-1,3-benzodiazol-2-yl)carbamate + methanol
(1b) N-(1H-1,3-benzodiazol-2-yl)carbamate = 2-aminobenzimidazole + CO₂ (spontaneous)

Glossary: carbendazim = methyl 1H-benzimidazol-2-ylcarbamate; 2-aminobenzimidazole = 1H-benzimidazol-2-amine

Other name(s): mheI (gene name)

Systematic name: carbendazim methanol hydrolase (decarboxylating)

Comments: The enzyme, which is inducible in the soil bacterium Nocardioides sp. (strain SG-4G), catalyses the degradation of the fungicide carbendazim. Following hydrolysis of the carbamate ester, the carbamate decarboxylates spontaneously.

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

References:

1. Pandey, G., Dorrian, S.J., Russell, R.J., Brearley, C., Kotsonis, S. and Oakeshott, J.G. Cloning and biochemical characterization of a novel carbendazim (methyl-1H-benzimidazol-2-ylcarbamate)-hydrolyzing esterase from the newly isolated Nocardioides sp. strain SG-4G and its potential for use in enzymatic bioremediation. Appl. Environ. Microbiol. 76 (2010) 2940-2945. [PMID: 20228105]

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 Transferred entry: ribosomal-protein-alanine N-acetyltransferase, now classified as EC 2.3.1.266, [ribosomal protein S18]-alanine N-acetyltransferase, and EC 2.3.1.267, [ribosomal protein S5]-alanine N-acetyltransferase. (EC 2.3.1.128 created 1990, deleted 2018)]

EC 2.3.1.129

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

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

For diagram of reaction click here

Other name(s): lpxA (gene name); UDP-N-acetylglucosamine acyltransferase; uridine diphosphoacetylglucosamine acyltransferase; acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferase; (R)-3-hydroxytetradecanoyl-[acyl-carrier-protein]:UDP-N-acetylglucosamine 3-O-(3-hydroxytetradecanoyl)transferase

Systematic name: (3R)-3-hydroxyacyl-[acyl-carrier protein]:UDP-N-acetyl-α-D-glucosamine 3-O-(3-hydroxyacyl)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 Gram-negative bacteria.

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]

2. Anderson, M.S., Bull, H.G., Galloway, S.M., Kelly, T.M., Mohan, S., Radika, K. and Raetz, C.R. UDP-N-acetylglucosamine acyltransferase of Escherichia coli. The first step of endotoxin biosynthesis is thermodynamically unfavorable. J. Biol. Chem. 268 (1993) 19858-19865. [PMID: 8366124]

3. Raetz, C.R. and Roderick, S.L. A left-handed parallel β helix in the structure of UDP-N-acetylglucosamine acyltransferase. Science 270 (1995) 997-1000. [PMID: 7481807]

4. Williams, A.H. and Raetz, C.R. Structural basis for the acyl chain selectivity and mechanism of UDP-N-acetylglucosamine acyltransferase. Proc. Natl. Acad. Sci. USA 104 (2007) 13543-13550. [PMID: 17698807]

5. Bainbridge, B.W., Karimi-Naser, L., Reife, R., Blethen, F., Ernst, R.K. and Darveau, R.P. Acyl chain specificity of the acyltransferases LpxA and LpxD and substrate availability contribute to lipid A fatty acid heterogeneity in Porphyromonas gingivalis, J. Bacteriol. 190 (2008) 4549-4558. [PMID: 18456814]

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, 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.

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, 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. [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, 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]

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, PDB, 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] + a 2-acyl-3-O-(β-D-galactosyl)-sn-glycerol = an [acyl-carrier protein] + a 1,2-diacyl-3-O-(β-D-galactosyl)-sn-glycerol

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: 2-methylbutanoate polyketide synthase

Reaction: 2 malonyl-CoA + [2-methylbutanoate polyketide synthase] + 2 NADPH + 3 H⁺ + S-adenosyl-L-methionine = (S)-2-methylbutanoyl-[2-methylbutanoate polyketide synthase] + 2 CoA + 2 CO₂ + 2 NADP⁺ + S-adenosyl-L-homocysteine + H₂O

For diagram of reaction click here.

Other name(s): LovF

Systematic name: acyl-CoA:malonyl-CoA C-acyltransferase (2-methylbutanoate-forming)

Comments: This polyketide synthase enzyme forms the (S)-2-methylbutanoate side chain during lovastatin biosynthesis by the filamentous fungus Aspergillus terreus. The overall reaction comprises a single condensation reaction followed by α-methylation, β-ketoreduction, dehydration, and α,β-enoyl reduction.

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

References:

1. Kennedy, J., Auclair, K., Kendrew, S.G., Park, C., Vederas, J.C. and Hutchinson, C.R. Modulation of polyketide synthase activity by accessory proteins during lovastatin biosynthesis. Science 284 (1999) 1368-1372. [PMID: 10334994]

2. Meehan, M.J., Xie, X., Zhao, X., Xu, W., Tang, Y. and Dorrestein, P.C. FT-ICR-MS characterization of intermediates in the biosynthesis of the α-methylbutyrate side chain of lovastatin by the 277 kDa polyketide synthase LovF. Biochemistry 50 (2011) 287-299. [PMID: 21069965]

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 (ambiguous); pine stilbene synthase (ambiguous)

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, PDB, 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 4→5 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]