See separate file for EC 2.3.1.101 to EC 2.1.1.150, EC 2.3.1.151 to EC 2.3.1.200 and EC 2.3.1.201 to EC 2.3.1.313.
See the following file for:
EC 2.3.1.101 to EC 2.1.1.150
EC 2.3.1.151 to EC 2.3.1.200
EC 2.3.1.201 to EC 2.3.1.313
Accepted name: 1-acylglycerol-3-phosphate O-acyltransferase
Reaction: acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate
Other name(s): 1-acyl-sn-glycero-3-phosphate acyltransferase; 1-acyl-sn-glycerol 3-phosphate acyltransferase; 1-acylglycero-3-phosphate acyltransferase; 1-acylglycerolphosphate acyltransferase; 1-acylglycerophosphate acyltransferase; lysophosphatidic acid-acyltransferase
Systematic name: acyl-CoA:1-acyl-sn-glycerol-3-phosphate 2-O-acyltransferase
Comments: Acyl-[acyl-carrier protein] can also act as an acyl donor. The animal enzyme is specific for the transfer of unsaturated fatty acyl groups.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 51901-16-7
References:
1. Frentzen, M., Heinz, E., McKeon, T.A. and Stumpf, P.K. Specificities and selectivities of glycerol-3-phosphate acyltransferase and monoacylglycerol-3-phosphate acyltransferase from pea and spinach chloroplasts. Eur. J. Biochem. 129 (1983) 629-636. [PMID: 6825679]
2. Hill, E.E. and Lands, W.E.M. Incorporation of long-chain and polyunsaturated acids into phosphatidate and phosphatidylcholine. Biochim. Biophys. Acta 152 (1968) 645-648. [PMID: 5661029]
3. Yamashita, S., Hosaka, K. and Numa, S. Acyl-donor specificities of partially purified 1-acylglycerophosphate acyltransferase, 2-acylglycerophosphate acyltransferase and 1-acylglycerophosphorylcholine acyltransferase from rat-liver microsomes. Eur. J. Biochem. 38 (1973) 25-31. [PMID: 4774123]
Accepted name: 2-acylglycerol-3-phosphate O-acyltransferase
Reaction: acyl-CoA + 2-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate
Other name(s): 2-acylglycerophosphate acyltransferase
Systematic name: acyl-CoA:2-acyl-sn-glycerol 3-phosphate O-acyltransferase
Comments: Saturated acyl-CoA thioesters are the most effective acyl donors.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 51901-17-8
References:
1. Yamashita, S., Hosaka, K. and Numa, S. Acyl-donor specificities of partially purified 1-acylglycerophosphate acyltransferase, 2-acylglycerophosphate acyltransferase and 1-acylglycerophosphorylcholine acyltransferase from rat-liver microsomes. Eur. J. Biochem. 25 (1973) 25-31. [PMID: 4774123]
Accepted name: phenylalanine N-acetyltransferase
Reaction: acetyl-CoA + L-phenylalanine = CoA + N-acetyl-L-phenylalanine
Other name(s): acetyl-CoA-L-phenylalanine α-N-acetyltransferase
Systematic name: acetyl-CoA:L-phenylalanine N-acetyltransferase
Comments: Also acts, more slowly, on L-histidine and L-alanine.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9075-16-5
References:
1. Leuzinger, W., Baker, A.L. and Cauvin, E. Acetylcholinesterase. II. Crystallization, absorption spectra, isoionic point. Proc. Natl. Acad. Sci. USA 59 (1968) 620-623. [PMID: 5238989]
Accepted name: formate C-acetyltransferase
Reaction: acetyl-CoA + formate = CoA + pyruvate
Other name(s): pyruvate formate-lyase; pyruvic formate-lyase; formate acetyltransferase
Systematic name: acetyl-CoA:formate C-acetyltransferase
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9068-08-0
References:
1. Knappe, J., Blaschkowski, H.P., Grobner, P. and Schmitt, T. Pyruvate formate-lyase of Escherichia coli: the acetyl-enzyme intermediate. Eur. J. Biochem. 50 (1974) 253-263. [PMID: 4615902]
[EC 2.3.1.55 Deleted entry: kanamycin 6'-N-acetyltransferase identical to EC 2.3.1.82 aminoglycoside N6'-acetyltransferase (EC 2.3.1.55 created 1976, deleted 1999)]
Accepted name: aromatic-hydroxylamine O-acetyltransferase
Reaction: N-hydroxy-4-acetylaminobiphenyl + N-hydroxy-4-aminobiphenyl = N-hydroxy-4-aminobiphenyl + N-acetoxy-4-aminobiphenyl
Other name(s): aromatic hydroxylamine acetyltransferase; arylhydroxamate acyltransferase; arylhydroxamate N,O-acetyltransferase; arylhydroxamic acid N,O-acetyltransferase; arylhydroxamic acyltransferase; N,O-acetyltransferase; N-hydroxy-2-acetylaminofluorene N-O acyltransferase
Systematic name: N-hydroxy-4-acetylaminobiphenyl:N-hydroxy-4-aminobiphenyl O-acetyltransferase
Comments: Transfers the N-acetyl group of some aromatic acethydroxamates to the O-position of some aromatic hydroxylamines.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 52660-15-8
References:
1. Bartsch, H., Dworkin, C., Miller, E.C. and Miller, J.A. Formation of electrophilic N-acetoxyarylamines in cytosoles from rat mammary gland and other tissues by transacetylation from the carcinogen N-hydroxy-4-acetylaminobiphenyl. Biochim. Biophys. Acta 304 (1973) 42-55. [PMID: 4699998]
Accepted name: diamine N-acetyltransferase
Reaction: acetyl-CoA + an alkane-α,ω-diamine = CoA + an N-acetyldiamine
Glossary: spermidine
spermine
Other name(s): spermidine acetyltransferase; putrescine acetyltransferase; putrescine (diamine)-acetylating enzyme; diamine acetyltransferase; spermidine/spermine N1-acetyltransferase; spermidine N1-acetyltransferase; acetyl-coenzyme A-1,4-diaminobutane N-acetyltransferase; putrescine acetylase; putrescine N-acetyltransferase
Systematic name: acetyl-CoA:alkane-<α,ω-diamine N-acetyltransferase
Comments: Acts on 1,3-diaminopropane, 1,5-diaminopentane, putrescine, spermidine (forming N1- and N8-acetylspermidine), spermine, N1-acetylspermidine and N8-acetylspermidine.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 54596-36-0
References:
1. Della Ragione, F. and Pegg, A.E. Purification and characterization of spermidine/spermine N1-acetyltransferase from rat liver. Biochemistry 21 (1982) 6152-6158. [PMID: 7150547]
Accepted name: 2,3-diaminopropionate N-oxalyltransferase
Reaction: oxalyl-CoA + L-2,3-diaminopropanoate = CoA + N3-oxalyl-L-2,3-diaminopropanoate
For diagram of reaction click here.
Other name(s): oxalyldiaminopropionate synthase; ODAP synthase; oxalyl-CoA:L-α,β-diaminopropionic acid oxalyltransferase; oxalyldiaminopropionic synthase
Systematic name: oxalyl-CoA:L-2,3-diaminopropanoate N3-oxalyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 62213-48-3
References:
1. Malathi, K., Padmanaban, G. and Sarma, P.S. Biosynthesis of β-N-oxalyl-L-α,β-diaminopropionic acid, the Lathyrus sativus neurotoxin. Phytochemistry 9 (1970) 1603-1610.
Accepted name: gentamicin 2'-N-acetyltransferase
Reaction: acetyl-CoA + gentamyicin C1a = CoA + N2'-acetylgentamicin C1a
Glossary: kanamycin
Other name(s): gentamycin acetyltransferase II; acetyl-CoA:gentamycin-C1a N2'-acetyltransferase
Systematic name: acetyl-CoA:gentamicin-C1a N2'-acetyltransferase
Comments: The antibiotics gentamicin A, sisomicin, tobramycin, paromomycin, neomycin B, kanamycin B and kanamycin C can also act as acceptors.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 50864-40-9
References:
1. Benveniste, R. and Davies, J. Aminoglycoside antibiotic-inactivating enzymes in actinomycetes similar to those present in clinical isolates of antibiotic-resistant bacteria. Proc. Natl. Acad. Sci. USA 70 (1973) 2276-2280. [PMID: 4209515]
Accepted name: gentamicin 3-N-acetyltransferase
Reaction: acetyl-CoA + gentamicin C = CoA + N3-acetylgentamicin C
Other name(s): gentamycin acetyltransferase I; aminoglycoside acetyltransferase AAC(3)-1; gentamycin 3-N-acetyltransferase; acetyl-CoA:gentamycin-C N3-acetyltransferase; acetyl-CoA:gentamicin-C N3'-acetyltransferase (incorrect); gentamicin 3'-N-acetyltransferase (incorrect)
Systematic name: acetyl-CoA:gentamicin-C N3-acetyltransferase
Comments: Also acetylates sisomicin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 58500-58-6
References:
1. Angelatou, F., Litsas, S.B. and Kontomichalou, P. Purification and properties of two gentamicin-modifying enzymes, coded by a single plasmid pPK237 originating from Pseudomonas aeruginosa. J. Antibiot. 35 (1982) 235-244. [PMID: 6281224]
2. Biddlecome, S., Haas, J., Davies, G.H., Miller, D., Rane, F. and Daniels, P.J.L. Enzymatic modification of aminoglycoside antibiotics: a new 3-N-acetylating enzyme from a Pseudomonas aeruginosa isolate. Antimicrob. Agents Chemother. 9 (1976) 951-955. [PMID: 820250]
3. Williams, J.W. and Northrop, D.B. Purification and properties of gentamicin acetyltransferase I. Biochemistry 15 (1976) 125-131. [PMID: 764855]
Accepted name: dihydrolipoyllysine-residue succinyltransferase
Reaction: succinyl-CoA + enzyme N6-(dihydrolipoyl)lysine = CoA + enzyme N6-(S-succinyldihydrolipoyl)lysine
For diagram of reaction click here (mechanism).
Glossary: dihydrolipoyl group
Other name(s): dihydrolipoamide S-succinyltransferase; dihydrolipoamide succinyltransferase; dihydrolipoic transsuccinylase; dihydrolipolyl transsuccinylase; dihydrolipoyl transsuccinylase; lipoate succinyltransferase (Escherichia coli); lipoic transsuccinylase; lipoyl transsuccinylase; succinyl-CoA:dihydrolipoamide S-succinyltransferase; succinyl-CoA:dihydrolipoate S-succinyltransferase
Systematic name: succinyl-CoA:enzyme-N6-(dihydrolipoyl)lysine S-succinyltransferase
Comments: A multimer (24-mer) of this enzyme forms the core of the multienzyme complex, and binds tightly both EC 1.2.4.2, oxoglutarate dehydrogenase (succinyl-transferring) and EC 1.8.1.4, dihydrolipoyl dehydrogenase. The lipoyl group of this enzyme is reductively succinylated by EC 1.2.4.2, and the only observed direction catalysed by EC 2.3.1.61 is that where this succinyl group is passed to coenzyme A.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9032-28-4
References:
1. Derosier, D.J., Oliver, R.M. and Reed, L.J. Crystallization and preliminary structural analysis of dihydrolipoyl transsuccinylase, the core of the 2-oxoglutarate dehydrogenase complex. Proc. Natl. Acad. Sci. USA 68 (1971) 1135-1137. [PMID: 4942179]
2. Reed, L.J. and Cox, D.J. Multienzyme complexes. In: Boyer, P.D. (Ed.), The Enzymes 3rd ed., vol. 1, Academic Press, New York, 1970, pp. 213-240.
3. Knapp, J.E., Mitchell, D.T., Yazdi, M.A., Ernst, S.R., Reed, L.J. and Hackert, M.L. Crystal structure of the truncated cubic core component of the Escherichia coli 2-oxoglutarate dehydrogenase multienzyme complex. J. Mol. Biol. 280 (1998) 655-668. [PMID: 9677295]
4. Perham, R.N. Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions. Annu. Rev. Biochem. 69 (2000) 961-1004. [PMID: 10966480]
Accepted name: 2-acylglycerophosphocholine O-acyltransferase
Reaction: acyl-CoA + 2-acyl-sn-glycero-3-phosphocholine = CoA + phosphatidylcholine
Other name(s): 2-acylglycerol-3-phosphorylcholine acyltransferase; 2-acylglycerophosphocholine acyltransferase
Systematic name: acyl-CoA:2-acyl-sn-glycero-3-phosphocholine O-acyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 64295-73-4
References:
1. Lands, W.E.M. and Hart, P. Metabolism of glycerolipids. VI. Specificities of acyl coenzyme A:phospholipid acyltransferases. J. Biol. Chem. 240 (1965) 1905-1911.
2. van den Bosch, H., van Golde, L.M.G., Slotboom, A.J. and van Deenen, L.L.M. The acylation of isomeric monoacyl phosphatidylcholines. Biochim. Biophys. Acta 152 (1968) 694-703. [PMID: 5660084]
Accepted name: 1-alkylglycerophosphocholine O-acyltransferase
Reaction: acyl-CoA + 1-alkyl-sn-glycero-3-phosphocholine = CoA + 2-acyl-1-alkyl-sn-glycero-3-phosphocholine
Systematic name: acyl-CoA:1-alkyl-sn-glycero-3-phosphocholine O-acyltransferase
Comments: May be identical with EC 2.3.1.23 1-acylglycerophosphocholine O-acyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 58693-63-3
References:
1. Waku, K. and Nakazawa, Y. Acyltransferase activity to 1-O-alkyl-glycero-3-phosphorylcholine in sarcoplasmic reticulum. J. Biochem. (Tokyo) 68 (1970) 459-466. [PMID: 5488773]
2. Waku, K. and Nakazawa, Y. Acyltransferae activity to 1-acyl-, 1-O-alkenyl-, and 1-O-alkyl-glycero-3-phosphorylcholine in Ehrlich ascites tumor cells. J. Biochem. (Tokyo) 72 (1972) 495-497. [PMID: 4644313]
Accepted name: agmatine N4-coumaroyltransferase
Reaction: 4-coumaroyl-CoA + agmatine = CoA + N-(4-guanidinobutyl)-4-hydroxycinnamamide
Glossary: agmatine = (4-aminobutyl)guanidine
Other name(s): p-coumaroyl-CoA-agmatine N-p-coumaroyltransferase; agmatine coumaroyltransferase
Systematic name: 4-coumaroyl-CoA:agmatine N4-coumaroyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 85030-72-4
References:
1. Bird, C.R. and Smith, T.A. The biosynthesis of coumarylagmatine in barley seedlings. Phytochemistry 20 (1981) 2345-2346.
Accepted name: bile acid-CoA:amino acid N-acyltransferase
Reaction: choloyl-CoA + glycine = CoA + glycocholate
For diagram click here.
Other name(s): glycine—taurine N-acyltransferase; amino acid N-choloyltransferase; BAT; glycine N-choloyltransferase; BACAT; cholyl-CoA glycine-taurine N-acyltransferase; cholyl-CoA:taurine N-acyltransferase
Systematic name: choloyl-CoA:glycine N-choloyltransferase
Comments: Also acts on CoA derivatives of other bile acids. Taurine and 2-fluoro-β-alanine can act as substrates, but more slowly [4]. The enzyme can also conjugate fatty acids to glycine and can act as a very-long-chain acyl-CoA thioesterase [7]. Bile-acid—amino-acid conjugates serve as detergents in the gastrointestinal tract, solubilizing long chain fatty acids, mono- and diglycerides, fat-soluble vitamins and cholesterol [4]. This is the second enzyme in a two-step process leading to the conjugation of bile acids with amino acids; the first step is the conversion of bile acids into their acyl-CoA thioesters, which is catalysed by EC 6.2.1.7, cholate—CoA ligase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 65979-40-0
References:
1. Czuba, B. and Vessey, D.A. Kinetic characterization of cholyl-CoA glycine-taurine N-acyltransferase from bovine liver. J. Biol. Chem. 255 (1980) 5296-5299. [PMID: 7372637]
2. Jordan, T.W., Lee, R. and Lim, W.C. Isoelectric focussing of soluble and particulate benzoyl-CoA and cholyl-CoA:amino acid N-acyltransferases from rat liver. Biochem. Int. 1 (1980) 325-330.
3. Vessey, D.A. The co-purification and common identity of cholyl CoA:glycine- and cholyl CoA:taurine-N-acyltransferase activities from bovine liver. J. Biol. Chem. 254 (1979) 2059-2063. [PMID: 422567]
4. Johnson, M.R., Barnes, S., Kwakye, J.B. and Diasio, R.B. Purification and characterization of bile acid-CoA:amino acid N-acyltransferase from human liver. J. Biol. Chem. 266 (1991) 10227-10233. [PMID: 2037576]
5. Falany, C.N., Xie, X., Wheeler, J.B., Wang, J., Smith, M., He, D. and Barnes, S. Molecular cloning and expression of rat liver bile acid CoA ligase. J. Lipid Res. 43 (2002) 2062-2071. [PMID: 12454267]
6. He, D., Barnes, S. and Falany, C.N. Rat liver bile acid CoA:amino acid N-acyltransferase: expression, characterization, and peroxisomal localization. J. Lipid Res. 44 (2003) 2242-2249. [PMID: 12951368]
7. O'Byrne, J., Hunt, M.C., Rai, D.K., Saeki, M. and Alexson, S.E. The human bile acid-CoA:amino acid N-acyltransferase functions in the conjugation of fatty acids to glycine. J. Biol. Chem. 278 (2003) 34237-34244. [PMID: 12810727]
Accepted name: leucine N-acetyltransferase
Reaction: acetyl-CoA + L-leucine = CoA + N-acetyl-L-leucine
Other name(s): leucine acetyltransferase
Systematic name: acetyl-CoA:L-leucine N-acetyltransferase
Comments: Propanoyl-CoA can act as a donor, but more slowly. L-Arginine, L-valine, L-phenylalanine and peptides containing L-leucine can act as acceptors.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 75496-56-9
References:
1. Suzukake, S., Hayashi, H., Hori, M. and Umezawa, H. Biosnthesis of leupeptin III. Isolation and properties of an enzyme synthesizing acetyl-L-leucine. J. Antibiot. 33 (1982) 857-862.
Accepted name: 1-alkylglycerophosphocholine O-acetyltransferase
Reaction: acetyl-CoA + 1-alkyl-sn-glycero-3-phosphocholine = CoA + 2-acetyl-1-alkyl-sn-glycero-3-phosphocholine
Other name(s): acetyl-CoA:1-alkyl-2-lyso-sn-glycero-3-phosphocholine 2-O-acetyltransferase; acetyl-CoA:lyso-PAF acetyltransferase; 1-alkyl-2-lysolecithin acetyltransferase; acyl-CoA:1-alkyl-sn-glycero-3-phosphocholine acyltransferase; blood platelet-activating factor acetyltransferase; lyso-GPC:acetyl CoA acetyltransferase; lyso-platelet activating factor:acetyl-CoA acetyltransferase; lysoPAF:acetyl CoA acetyltransferase; PAF acetyltransferase; platelet-activating factor acylhydrolase; platelet-activating factor-synthesizing enzyme; 1-alkyl-2-lyso-sn-glycero-3-phosphocholine acetyltransferase; lyso-platelet-activating factor:acetyl-CoA acetyltransferase
Systematic name: acetyl-CoA:1-alkyl-sn-glycero-3-phosphocholine 2-O-acetyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 76773-96-1
References:
1. Wykle, R.L., Malone, B. and Snyder, F. Enzymatic synthesis of 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine, a hypotensive and platelet-aggregating lipid. J. Biol. Chem. 255 (1980) 10256-10260. [PMID: 7430122]
Accepted name: glutamine N-acyltransferase
Reaction: acyl-CoA + L-glutamine = CoA + N-acyl-L-glutamine
Systematic name: acyl-CoA:L-glutamine N-acyltransferase
Comments: Phenylacetyl-CoA and (indol-3-yl)acetyl-CoA, but not benzoyl-CoA, can act as acyl donors. Not identical with EC 2.3.1.13 glycine N-acyltransferase or EC 2.3.1.71 glycine N-benzoyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9030-00-6
References:
1. Webster, L.T., Jr., Siddiqui, U.A., Lucas, S.V., Strong, J.M. and Mieyal, J.J. Identification of separate acyl-CoA:glycine and acyl-CoA:L-glutamine N-acyltransferase activities in mitochondrial fractions from liver of rhesus monkey and man. J. Biol. Chem. 251 (1976) 3352-3358. [PMID: 931988]
Accepted name: monoterpenol O-acetyltransferase
Reaction: acetyl-CoA + a monoterpenol = CoA + a monoterpenol acetate ester
For diagram click here.
Other name(s): menthol transacetylase
Systematic name: acetyl-CoA:monoterpenol O-acetyltransferase
Comments: (–)-Menthol, (+)-neomenthol, borneol, and also cyclohexanol and decan-1-ol can be acetylated.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 78990-59-7
References:
1. Croteau, R. and Hooper, C.L. Metabolism of monoterpenes. Acetylation of (–)-menthol by a soluble enzyme preparation from peppermint (Mentha piperita) leaves. Plant Physiol. 61 (1978) 737-742.
2. Martinkus, C. and Croteau, R. Metabolism of monoterpenes - evidence for compartmentation of L-menthone metabolism in peppermint (Mentha piperita) leaves. Plant Physiol. 68 (1981) 99-106.
[EC 2.3.1.70 Deleted entry: CDP-acylglycerol O-arachidonoyltransferase. This enzyme was deleted following a retraction of the evidence upon which the entry had been drafted (Thompson, W. and Zuk, R.T. Acylation of CDP-monoacylglycerol cannot be confirmed. J. Biol. Chem. 258 (1983) 9623. [PMID: 6885763]). (EC 2.3.1.70 created 1984, deleted 2009)]
Accepted name: glycine N-benzoyltransferase
Reaction: benzoyl-CoA + glycine = CoA + hippurate
Glossary: hippurate = N-benzoylglycine
Other name(s): benzoyl CoA-amino acid N-acyltransferase; benzoyl-CoA:glycine N-acyltransferase
Systematic name: benzoyl-CoA:glycine N-benzoyltransferase
Comments: Not identical with EC 2.3.1.13 glycine N-acyltransferase or EC 2.3.1.68 glutamine N-acyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 71567-07-2
References:
1. Nandi, D.L., Lucas, S.V. and Webster, L.T. Benzoyl-coenzyme A:glycine N-acyltransferase and phenylacetyl-coenzyme A:glycine N-acyltransferase from bovine liver mitochondria. Purification and characterization. J. Biol. Chem. 254 (1979) 7230-7237. [PMID: 457678]
Accepted name: indoleacetylglucose—inositol O-acyltransferase
Reaction: 1-O-(indol-3-yl)acetyl-β-D-glucose + myo-inositol = D-glucose + O-(indol-3-yl)acetyl-myo-inositol
Other name(s): indole-3-acetyl-β-1-D-glucoside:myo-inositol indoleacetyltransferase; 1-O-(indol-3-ylacetyl)-β-D-glucose:myo-inositol indole-3-ylacetyltransferase
Systematic name: 1-O-(indol-3-yl)acetyl-β-D-glucose:myo-inositol (indol-3-yl)acetyltransferase
Comments: The position of acylation is indeterminate because of the ease of acyl transfer between hydroxy groups.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 74082-57-8
References:
1. Michalczuk, L. and Bandurski, R.S. Enzymic synthesis of 1-O-indol-3-ylacetyl-β-D-glucose and indol-3-ylacetyl-myo-inositol. Biochem. J. 207 (1982) 273-281. [PMID: 6218801]
2. Michalczuk, L. and Bandurski, R.S. UDP-glucose: indoleacetic acid glucosyl transferase and indoleacetyl-glucose: myo-inositol indoleacetyl transferase. Biochem. Biophys. Res. Commun. 93 (1980) 588-592. [PMID: 6446303]
Accepted name: diacylglycerol—sterol O-acyltransferase
Reaction: 1,2-diacyl-sn-glycerol + sterol = a 1-acyl-sn-glycerol + sterol ester
Other name(s): 1,2-diacyl-sn-glycerol:sterol acyl transferase
Systematic name: 1,2-diacyl-sn-glycerol:sterol O-acyltransferase
Comments: Cholesterol, sitosterol, campesterol and diacylglycerol can act as acceptors. Transfers a number of long-chain fatty acyl groups.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 79586-23-5
References:
1. Bartlett, K., Keat, M.J. and Mercer, E.I. Biosynthesis of sterol esters in Phycomyces blakesleeanus. Phytochemistry 13 (1974) 1107-1113.
2. Garcia, R.E. and Mudd, J.B. Metabolism of monoacylglycerol and diacylglycerol by enzyme preparations from spinach leaves. Arch. Biochem. Biophys. 191 (1978) 487-493. [PMID: 742884]
3. Garcia, R.E. and Mudd, J.B. 1,2-Diacyl-sn-glycerol:sterol acyl transferase from spinach leaves (Spinacia oleracea L.). Methods Enzymol. 71 (1981) 768-772.
Accepted name: chalcone synthase
Reaction: 3 malonyl-CoA + 4-coumaroyl-CoA = 4 CoA + naringenin chalcone + 3 CO2
For diagram of reaction click here.
Glossary: phloretin = 3-(4-hydroxyphenyl)-1-(2,4,6-trihydroxyphenyl)propan-1-one
Other name(s): naringenin-chalcone synthase; flavanone synthase; 6'-deoxychalcone synthase; chalcone synthetase; DOCS; CHS
Systematic name: malonyl-CoA:4-coumaroyl-CoA malonyltransferase (cyclizing)
Comments: The enzyme catalyses the first committed step in the biosynthesis of flavonoids. It can also act on dihydro-4-coumaroyl-CoA, forming phloretin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 56803-04-4
References:
1. Ayabe, S.-I., Udagawa, A. and Furuya, T. NAD(P)H-dependent 6'-deoxychalcone synthase activity in Glycyrrhiza echinata cells induced by yeast extract. Arch. Biochem. Biophys. 261 (1988) 458-462. [PMID: 3355160]
2. Heller, W. and Hahlbrock, K. Highly purified "flavanone synthase" from parsley catalyzes the formation of naringenin chalcone. Arch. Biochem. Biophys. 200 (1980) 617-619. [PMID: 7436427]
3. Yahyaa, M., Ali, S., Davidovich-Rikanati, R., Ibdah, M., Shachtier, A., Eyal, Y., Lewinsohn, E. and Ibdah, M. Characterization of three chalcone synthase-like genes from apple (Malus x domestica Borkh.). Phytochemistry 140 (2017) 125-133. [PMID: 28482241]
Accepted name: long-chain-alcohol O-fatty-acyltransferase
Reaction: acyl-CoA + a long-chain alcohol = CoA + a long-chain ester
Other name(s): wax synthase; wax-ester synthase
Systematic name: acyl-CoA:long-chain-alcohol O-acyltransferase
Comments: Transfers saturated or unsaturated acyl residues of chain-length C18 to C20 to long-chain alcohols, forming waxes. The best acceptor is cis-icos-11-en-1-ol.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 64060-40-8
References:
1. Wu, X.-Y., Moreau, R.A. and Stumpf, P.K. Studies of biosynthesis of waxes by developing jojoba seed. 3. Biosynthesis of wax esters from acyl-CoA and long-chain alcohols. Lipids 16 (1981) 897-902.
Accepted name: retinol O-fatty-acyltransferase
Reaction: acyl-CoA + retinol = CoA + retinyl ester
For diagram of reaction click here.
Other name(s): retinol acyltransferase; retinol fatty-acyltransferase
Systematic name: acyl-CoA:retinol O-acyltransferase
Comments: Acts on palmitoyl-CoA and other long-chain fatty-acyl derivatives of CoA.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 81295-48-9
References:
1. Helgerud, P., Petersen, L.B. and Norum, K.R. Retinol esterification by microsomes from the mucosa of human small intestine. Evidence for acyl-Coenzyme A retinol acyltransferase activity. J. Clin. Invest. 71 (1983) 747-753. [PMID: 6826734]
2. Ross, A.C. Retinol esterification by rat liver microsomes. Evidence for a fatty acyl coenzyme A: retinol acyltransferase. J. Biol. Chem. 257 (1982) 2453-2459. [PMID: 7061433]
Accepted name: triacylglycerol—sterol O-acyltransferase
Reaction: triacylglycerol + a 3β-hydroxysteroid = diacylglycerol + a 3β-hydroxysteroid ester
Other name(s): triacylglycerol:sterol acyltransferase
Systematic name: triacylglycerol:3β-hydroxysteroid O-acyltransferase
Comments: Tripalmitoylglycerol and, more slowly, other triacylglycerols containing C6 to C22 fatty acids, can act as donors. The best acceptors are 3β-hydroxysterols with a planar ring system.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 80487-96-3
References:
1. Zimowski, J. and Wojciechowski, Z.A. Acyl donors for sterol esterification by cell-free preparations from Sinapis alba roots. Phytochemistry 20 (1981) 1799-1803.
Accepted name: heparan-α-glucosaminide N-acetyltransferase
Reaction: acetyl-CoA + heparan sulfate α-D-glucosaminide = CoA + heparan sulfate N-acetyl-α-D-glucosaminide
Other name(s): acetyl-CoA:α-glucosaminide N-acetyltransferase
Systematic name: acetyl-CoA:heparan-α-D-glucosaminide N-acetyltransferase
Comments: Brings about the acetylation of glucosamine groups of heparan sulfate and heparin from which the sulfate has been removed. Also acts on heparin. Not identical with EC 2.3.1.3 glucosamine N-acetyltransferase or EC 2.3.1.4 glucosamine-phosphate N-acetyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 79955-83-2
References:
1. Klein, V., Kresse, H. and von Figura, K. Sanfilippo syndrome type C: deficiency of acetyl-CoA:α-glucosaminide N-acetyltransferase in skin fibroblasts. Proc. Natl. Acad. Sci. USA 75 (1978) 5185-5189. [PMID: 33384]
2. Pohlmann, R., Klein, U., Fromme, H.G. and von Figura, K. Localisation of acetyl-CoA: α-glucosaminide N-acetyltransferase in microsomes and lysosomes of rat liver. Hoppe-Seyler's Z. Physiol. Chem. 362 (1981) 1199-1207. [PMID: 7346380]
Accepted name: maltose O-acetyltransferase
Reaction: acetyl-CoA + maltose = CoA + 6-O-acetyl-α-D-glucopyranosyl-(1→4)-D-glucose
Other name(s): maltose transacetylase; maltose O-acetyltransferase; MAT
Systematic name: acetyl-CoA:maltose O-acetyltransferase
Comments: Not identical with EC 2.3.1.18 galactoside O-acetyltransferase. The acetyl group is added exclusively to the C6 position of glucose and to the C6 position of the non-reducing glucose residue of maltose [3]. Other substrates of this enzyme are glucose, which is a better substrate than maltose [2], and mannose and frucose, which are poorer substrates than maltose [2]. Isopropyl-β-thio-galactose, which is a good substrate for EC 2.3.1.118 is a poor substrate for this enzyme [3].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 81295-47-8
References:
1. Freundlieb, S. and Boos, W. Maltose transacetylase of Escherichia coli: a preliminary report. Ann. Microbiol. (Paris) 133A (1982) 181-189. [PMID: 7041741]
2. Brand, B. and Boos, W. Maltose transacetylase of Escherichia coli. Mapping and cloning of its structural, gene, mac, and characterization of the enzyme as a dimer of identical polypeptides with a molecular weight of 20,000. J. Biol. Chem. 266 (1991) 14113-14118. [PMID: 1856235]
3. Lo Leggio, L., Dal Degan, F., Poulsen, P., Andersen, S.M. and Larsen, S. The structure and specificity of Escherichia coli maltose acetyltransferase give new insight into the LacA family of acyltransferases. Biochemistry 42 (2003) 5225-5235. [PMID: 12731863]
Accepted name: cysteine-S-conjugate N-acetyltransferase
Reaction: acetyl-CoA + an L-cysteine-S-conjugate = CoA + an N-acetyl L-cysteine-S-conjugate
Glossary: N-acetyl-L-cysteine-S-conjugate = mercapturic acid
Systematic name: acetyl-CoA:S-substituted L-cysteine N-acetyltransferase
Comments: S-Benzyl-L-cysteine and, in decreasing order of activity, S-butyl-L-cysteine, S-propyl-L-cysteine, O-benzyl-L-serine and S-ethyl-L-cysteine, can act as acceptors.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 81725-80-6
References:
1. Duffel, M.W. and Jakoby, W.B. Cysteine S-conjugate N-acetyltransferase from rat kidney microsomes. Mol. Pharmacol. 21 (1982) 444-448. [PMID: 6892478]
Accepted name: aminoglycoside 3-N-acetyltransferase
Reaction: acetyl-CoA + a 2-deoxystreptamine antibiotic = CoA + N3-acetyl-2-deoxystreptamine antibiotic
For diagram of reaction click here.
Glossary: kanamycin
Other name(s): 3-aminoglycoside acetyltransferase; 3-N-aminoglycoside acetyltransferase; aminoglycoside N3-acetyltransferase; acetyl-CoA:2-deoxystreptamine-antibiotic N3'-acetyltransferase (incorrect); aminoglycoside N3'-acetyltransferase (incorrect)
Systematic name: acetyl-CoA:2-deoxystreptamine-antibiotic N3-acetyltransferase
Comments: Different from EC 2.3.1.60 gentamicin 3-N-acetyltransferase. A wide range of antibiotics containing the 2-deoxystreptamine ring can act as acceptors, including gentamicin, kanamycin, tobramycin, neomycin and apramycin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 60120-42-5
References:
1. Davies, J. and O'Connor, S. Enzymatic modification of aminoglycoside antibiotics: 3-N-Acetyltransferase with broad specificity that determines resistance to the novel aminoglycoside apramycin. Antimicrob. Agents Chemother. 14 (1978) 69-72. [PMID: 356726]
Accepted name: aminoglycoside 6'-N-acetyltransferase
Reaction: acetyl-CoA + kanamycin-B = CoA + N6'-acetylkanamycin-B
Glossary: kanamycin
Other name(s): aminoglycoside N6'-acetyltransferase; aminoglycoside-6'-acetyltransferase; aminoglycoside-6-N-acetyltransferase; kanamycin acetyltransferase
Systematic name: acetyl-CoA:kanamycin-B N6'-acetyltransferase
Comments: The antibiotics kanamycin A, kanamycin B, neomycin, gentamicin C1a, gentamicin C2 and sisomicin are substrates. The antibiotic tobramycin, but not paromomycin, can also act as acceptor. The 6-amino group of the purpurosamine ring is acetylated.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 56467-65-3
References:
1. le Goffic, F. and Martel, A. La résistance aux aminosides provoquée par une isoenzyme la kanamycine acétyltransférase. Biochimie 56 (1974) 893-897. [PMID: 4614862]
2. Benveniste, R. and Davies, J.E. Enzymatic acetylation of aminoglycoside antibiotics by Escherichia coli carrying an R factor. Biochemistry 10 (1971) 1787-1796. [PMID: 4935296]
3. Dowding, J.E. Mechanisms of gentamicin resistance in Staphylococcus aureus. Antimicrob. Agents Chemother. 11 (1977) 47-50. [PMID: 836013]
Accepted name: phosphatidylcholine—dolichol O-acyltransferase
Reaction: 3-sn-phosphatidylcholine + dolichol = 1-acyl-sn-glycero-3-phosphocholine + acyldolichol
Systematic name: 3-sn-phosphatidylcholine:dolichol O-acyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 111839-04-4
References:
1. Keenan, R. and Kruczek, H. The esterification of dolichol by rat liver microsomes. Biochemistry 15 (1976) 1586-1591. [PMID: 4095]
2. Radominska-Pyrek, A., Chojnachi, T. and Zulezyk, W. Acyl esters of polyprenols: specificity of microsomal transacylase for polyprenols of different chain length and saturation. Acta Biochim. Pol. 26 (1979) 125-134. [PMID: 506613]
Accepted name: alcohol O-acetyltransferase
Reaction: acetyl-CoA + an alcohol = CoA + an acetyl ester
Other name(s): alcohol acetyltransferase
Systematic name: acetyl-CoA:alcohol O-acetyltransferase
Comments: Acts on a range of short-chain aliphatic alcohols, including methanol and ethanol
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 80237-89-4
References:
1. Yoshioka, K. and Hashimoto, N. Ester formation by alcohol acetyltransferase from brewers' yeast. Agric. Biol. Chem. 45 (1981) 2183-2190.
EC 2.3.1.85
Accepted name: fatty-acid synthase system
Reaction: acetyl-CoA + n malonyl-CoA + 2n NADPH + 2n H+ = a long-chain fatty acid + (n+1) CoA + n CO2 + 2n NADP+
Glossary: a long-chain-fatty acid = a fatty acid with an aliphatic chain of 13-22 carbons.
Other name(s): FASN (gene name); fatty-acid synthase
Systematic name: acyl-CoA:malonyl-CoA C-acyltransferase (decarboxylating, oxoacyl- and enoyl-reducing and thioester-hydrolysing)
Comments: The animal enzyme is a multi-functional protein catalysing the reactions of EC 2.3.1.38 [acyl-carrier-protein] S-acetyltransferase, EC 2.3.1.39 [acyl-carrier-protein] S-malonyltransferase, EC 2.3.1.41 β-ketoacyl-[acyl-carrier-protein] synthase I, EC 1.1.1.100 3-oxoacyl-[acyl-carrier-protein] reductase, EC 4.2.1.59 3-hydroxyacyl-[acyl-carrier-protein] dehydratase, EC 1.3.1.39 enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific) and EC 3.1.2.14 oleoyl-[acyl-carrier-protein] hydrolase. cf. EC 2.3.1.86, fatty-acyl-CoA synthase system.
Links to other databases:
BRENDA,
EXPASY,
ExplorEnz,
KEGG,
MetaCyc,
PDB,
CAS registry number: 9045-77-6
References:
1. Stoops, J.K., Ross, P., Arslanian, M.J., Aune, K.C., Wakil, S.J. and Oliver, R.M. Physicochemical studies of the rat liver and adipose fatty acid synthetases. J. Biol. Chem. 254 (1979) 7418-7426. [PMID: 457689]
2. Wakil, S.J., Stoops, J.K. and Joshi, V.C. Fatty acid synthesis and its regulation. Annu. Rev. Biochem. 52 (1983) 537-579. [PMID: 6137188]
Accepted name: fatty-acyl-CoA synthase system
Reaction: acetyl-CoA + n malonyl-CoA + 2n NADPH + 4n H+ = long-chain-acyl-CoA + n CoA + n CO2 + 2n NADP+
Other name(s): yeast fatty acid synthase; FAS1 (gene name); FAS2 (gene name); fatty-acyl-CoA synthase
Systematic name: acyl-CoA:malonyl-CoA C-acyltransferase (decarboxylating, oxoacyl- and enoyl-reducing)
Comments: The enzyme from yeasts (Ascomycota and Basidiomycota) is a multi-functional protein complex composed of two subunits. One subunit catalyses the reactions EC 1.1.1.100, 3-oxoacyl-[acyl-carrier-protein] reductase and EC 2.3.1.41, β-ketoacyl-[acyl-carrier-protein] synthase I, while the other subunit catalyses the reactions of EC 2.3.1.38, [acyl-carrier-protein] S-acetyltransferase, EC 2.3.1.39, [acyl-carrier-protein] S-malonyltransferase, EC 4.2.1.59, 3-hydroxyacyl-[acyl-carrier-protein] dehydratase, EC 1.3.1.10, enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific) and EC 1.1.1.279, (R)-3-hydroxyacid-ester dehydrogenase. The enzyme system differs from the animal system (EC 2.3.1.85, fatty-acid synthase system) in that the enoyl reductase domain requires FMN as a cofactor, and the ultimate product is an acyl-CoA (usually palmitoyl-CoA) instead of a free fatty acid.
Links to other databases:
BRENDA,
EXPASY,
ExplorEnz,
KEGG,
MetaCyc,
PDB,
CAS registry number: 94219-29-1
References:
1. Schweitzer, E., Kniep, B., Castorph, H. and Holzner, U. Pantetheine-free mutants of the yeast fatty-acid-synthetase complex. Eur. J. Biochem. 39 (1973) 353-362. [PMID: 4590449]
2. Wakil, S.J., Stoops, J.K. and Joshi, V.C. Fatty acid synthesis and its regulation. Annu. Rev. Biochem. 52 (1983) 537-579. [PMID: 6137188]
3. Tehlivets, O., Scheuringer, K. and Kohlwein, S.D. Fatty acid synthesis and elongation in yeast. Biochim. Biophys. Acta 1771 (2007) 255-270. [PMID: 16950653]
Accepted name: aralkylamine N-acetyltransferase
Reaction: acetyl-CoA + a 2-arylethylamine = CoA + an N-acetyl-2-arylethylamine
Other name(s): serotonin acetyltransferase; serotonin acetylase; arylalkylamine N-acetyltransferase; serotonin N-acetyltransferase; AANAT; melatonin rhythm enzyme
Systematic name: acetyl-CoA:2-arylethylamine N-acetyltransferase
Comments: Narrow specificity towards 2-arylethylamines, including serotonin (5-hydroxytryptamine), tryptamine, 5-methoxytryptamine and phenylethylamine. This is the penultimate enzyme in the production of melatonin (5-methoxy-N-acetyltryptamine) and controls its synthesis (cf. EC 2.1.1.4, acetylserotonin O-methyltransferase). Differs from EC 2.3.1.5 arylamine N-acetyltransferase.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
PDB,
CAS registry number: 92941-56-5
References:
1. Voisin, P., Namboodiri, M.A.A. and Klein, D.C. Arylamine N-acetyltransferase and arylalkylamine N-acetyltransferase in the mammalian pineal gland. J. Biol. Chem. 259 (1984) 10913-10918. [PMID: 6469990]
2. Ferry, G., Loynel, A., Kucharczyk, N., Bertin, S., Rodriguez, M., Delagrange, P., Galizzi, J.P., Jacoby, E., Volland, J.P., Lesieur, D., Renard, P., Canet, E., Fauchere, J.L. and Boutin, J.A. Substrate specificity and inhibition studies of human serotonin N-acetyltransferase. J. Biol. Chem. 275 (2000) 8794-8805. [PMID: 10722724]
3. Khalil, E.M. and Cole, P.A. A potent inhibitor of the melatonin rhythm enzyme. J. Am. Chem. Soc. 120 (1998) 6195-6196.
[EC 2.3.1.88 Transferred entry: peptide α-N-acetyltransferase. Now covered by EC 2.3.1.254, N-terminal methionine Nα-acetyltransferase NatB, EC 2.3.1.255, N-terminal amino-acid Nα-acetyltransferase NatA, EC 2.3.1.256, N-terminal methionine Nα-acetyltransferase NatC, EC 2.3.1.257, N-terminal L-serine Nα-acetyltransferase NatD, EC 2.3.1.258, N-terminal methionine Nα-acetyltransferase NatE and EC 2.3.1.259, N-terminal methionine Nα-acetyltransferase NatF (EC 2.3.1.88 created 1986, modified 1989, deleted 2016)]
Accepted name: tetrahydrodipicolinate N-acetyltransferase
Reaction: acetyl-CoA + (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + H2O = CoA + L-2-acetamido-6-oxoheptanedioate
Other name(s): tetrahydrodipicolinate acetylase; tetrahydrodipicolinate:acetyl-CoA acetyltransferase; acetyl-CoA:L-2,3,4,5-tetrahydrodipicolinate N2-acetyltransferase; acetyl-CoA:(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N2-acetyltransferase
Systematic name: acetyl-CoA:(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N2-acetyltransferase
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
PDB,
CAS registry number: 83588-91-4
References:
1. Chatterjee, S.P. and White, P.J. Activities and regulation of the enzymes of lysine biosynthesis in a lysine-excreting strain of Bacillus megaterium. J. Gen. Microbiol. 128 (1982) 1073-1081.
Accepted name: β-glucogallin O-galloyltransferase
Reaction: 2 1-O-galloyl-β-D-glucose = D-glucose + 1-O,6-O-digalloyl-β-D-glucose
Systematic name: 1-O-galloyl-β-D-glucose:1-O-galloyl-β-D-glucose O-galloyltransferase
Comments: β-Glucogallin can act as donor and as acceptor. Digalloylglucose can also act as acceptor, with the formation of 1-O,2-O,6-O-trigalloylglucose
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
CAS registry number: 87502-55-4
References:
1. Denzel, K., Schilling, G. and Gross, G.G. Biosynthesis of gallotannins - enzymatic conversion of 1,6-digalloylglucose to 1,2,6-trigalloylglucose. Planta 176 (1988) 135-137.
2. Gross, G.G. Synthesis of mono-galloyl-β-D-glucose di-galloyl-β-D-glucose and trigalloyl-β-D-glucose by β-glucogallin-dependent galloyltransferases from oak leaves. Z. Natursforsch. C: Biosci. 38 (1983) 519-523.
Accepted name: sinapoylglucose—choline O-sinapoyltransferase
Reaction: 1-O-sinapoyl-β-D-glucose + choline = D-glucose + sinapoylcholine
Glossary: sinapoyl = 4-hydroxy-3,5-dimethoxycinnamoyl
Other name(s): sinapine synthase; 1-O-(4-hydroxy-3,5-dimethoxycinnamoyl)-β-D-glucose:choline 1-O-(4-hydroxy-3,5-dimethoxycinnamoyl)transferase
Systematic name: 1-O-sinapoyl-β-D-glucose:choline 1-O-sinapoyltransferase
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
PDB,
CAS registry number: 85205-00-1
References:
1. Gräwe, W. and Strack, D. Partial-purification and some properties of 1-sinapoylglucose-choline sinapoyltransferase (sinapine synthase) from seeds of Raphanus sativus L. and Sinapis alba L. Z. Naturforsch. C: Biosci. 41 (1986) 28-33.
Accepted name: sinapoylglucose—malate O-sinapoyltransferase
Reaction: 1-O-sinapoyl-β-D-glucose + (S)-malate = D-glucose + sinapoyl-(S)-malate
Other name(s): 1-sinapoylglucose-L-malate sinapoyltransferase; sinapoylglucose:malate sinapoyltransferase
Systematic name: 1-O-sinapoyl-β-D-glucose:(S)-malate O-sinapoyltransferase
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
PDB,
CAS registry number: 76095-65-3
References:
1. Strack, D. Development of 1-O-sinapoyl-β-D-glucose-l-malate sinapoyltransferase activity in cotyledons of red radish (Raphanus sativus L. var sativus). Planta 155 (1982) 31-36.
Accepted name: 13-hydroxylupanine O-tigloyltransferase
Reaction: (E)-2-methylcrotonoyl-CoA + 13-hydroxylupanine = CoA + 13-[(E)-2-methylcrotonoyl]oxylupanine
Glossary: (E)-2-methylcrotonoyl-CoA = tigloyl-CoA = (E)-2-methylbut-2-enoyl-CoA
Other name(s): tigloyl-CoA:13-hydroxylupanine O-tigloyltransferase; 13-hydroxylupanine acyltransferase
Systematic name: (E)-2-methylcrotonoyl-CoA:13-hydroxylupanine O-2-methylcrotonoyltransferase
Comments: Benzoyl-CoA and, more slowly, pentanoyl-CoA, 3-methylbutanoyl-CoA and butanoyl-CoA can act as acyl donors. Involved in the synthesis of lupanine alkaloids.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
CAS registry number: 85341-00-0
References:
1. Wink, M. and Hartmann, T. Enzymatic synthesis of quinolizidine alkaloid esters: a tigloyl-CoA:13-hydroxylupanine O-tigloyl transferase from Lupinus albus L. Planta 156 (1982) 560-565.
2. Okada, T.. Hirai, M.Y., Suzuki, H., Yamazaki, M. and Saito, K. Molecular characterization of a novel quinolizidine alkaloid O-tigloyltransferase: cDNA cloning, catalytic activity of recombinant protein and expression analysis in Lupinus plants. Plant Cell Physiol. 46 (2005) 233-244.
3. Suzuki, H., Murakoshi, I. and Saito, K. A novel O-tigloyltransferase for alkaloid biosynthesis in plants. Purification, characterization, and distribution in Lupinus plants. J. Biol. Chem. 269 (1994) 15853-15860. [PMID: 8195240]
Accepted name: 6-deoxyerythronolide-B synthase
Reaction: propanoyl-CoA + 6 (2S)-methylmalonyl-CoA + 6 NADPH + 6 H+ = 6-deoxyerythronolide B + 7 CoA + 6 CO2 + H2O + 6 NADP+
For diagram of reaction, click here.
Other name(s): erythronolide condensing enzyme; malonyl-CoA:propionyl-CoA malonyltransferase (cyclizing); erythronolide synthase; malonyl-CoA:propanoyl-CoA malonyltransferase (cyclizing); deoxyerythronolide B synthase; 6-deoxyerythronolide B synthase; DEBS
Systematic name: propanoyl-CoA:(2S)-methylmalonyl-CoA malonyltransferase (cyclizing)
Comments: The product, 6-deoxyerythronolide B, contains a 14-membered lactone ring and is an intermediate in the biosynthesis of erythromycin antibiotics. Biosynthesis of 6-deoxyerythronolide B requires 28 active sites that are precisely arranged along three large polypeptides, denoted DEBS1, -2 and -3 [6]. The polyketide product is synthesized by the processive action of a loading didomain, six extension modules and a terminal thioesterase domain [5]. Each extension module contains a minimum of a ketosynthase (KS), an acyltransferase (AT) and an acyl-carrier protein (ACP). The KS domain both accepts the growing polyketide chain from the previous module and catalyses the subsequent decarboxylative condensation between this substrate and an ACP-bound methylmalonyl extender unit, introduce by the AT domain. This combined effort gives rise to a new polyketide intermediate that has been extended by two carbon atoms [5].
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
PDB,
CAS registry number: 87683-77-0
References:
1. Omura, S. and Nakagawa, A. Biosynthesis of 16-membered macrolide antibiotics. Antibiotics 4 (1981) 175-192.
2. Roberts, G. and Leadley, P.F. Use of [3H]tetrahydrocerulenin to assay condensing enzyme activity in Streptomyces erythreus. Biochem. Soc. Trans. 12 (1984) 642-643.
3. Pfeifer, B.A., Admiraal, S.J., Gramajo, H., Cane, D.E. and Khosla, C. Biosynthesis of complex polyketides in a metabolically engineered strain of E. coli. Science 291 (2001) 1790-1792. [PMID: 11230695]
4. Tsai, S.C., Miercke, L.J., Krucinski, J., Gokhale, R., Chen, J.C., Foster, P.G., Cane, D.E., Khosla, C. and Stroud, R.M. Crystal structure of the macrocycle-forming thioesterase domain of the erythromycin polyketide synthase: versatility from a unique substrate channel. Proc. Natl. Acad. Sci. USA 98 (2001) 14808-14813. [PMID: 11752428]
5. Khosla, C., Tang, Y., Chen, A.Y., Schnarr, N.A. and Cane, D.E. Structure and mechanism of the 6-deoxyerythronolide B synthase. Annu. Rev. Biochem. 76 (2007) 195-221. [PMID: 17328673]
Accepted name: trihydroxystilbene synthase
Reaction: 3 malonyl-CoA + 4-coumaroyl-CoA = 4 CoA + trans-resveratrol + 4 CO2
For diagram click here.
Glossary: trans-resveratrol = 3,4',5-trihydroxy-trans-stilbene
Other name(s): resveratrol synthase; stilbene synthase
Systematic name: malonyl-CoA:4-coumaroyl-CoA malonyltransferase (cyclizing)
Comments: Not identical with EC 2.3.1.74 naringenin-chalcone synthase or EC 2.3.1.146 pinosylvin synthase.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
PDB,
CAS registry number: 128449-70-7
References:
1. Schöppner, A. and Kindl, H. Purification and properties of a stilbene synthase from induced cell suspension cultures of peanut. J. Biol. Chem. 259 (1984) 6806-6811. [PMID: 6427224]
[EC 2.3.1.96 Deleted entry: glycoprotein N-palmitoyltransferase (EC 2.3.1.96 created 1989, deleted 2018)]
Accepted name: glycylpeptide N-tetradecanoyltransferase
Reaction: tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein]
Glossary: tetradecanoyl-CoA = myristoyl-CoA
Other name(s): NMT (gene name); peptide N-myristoyltransferase; myristoyl-CoA-protein N-myristoyltransferase; myristoyl-coenzyme A:protein N-myristoyl transferase; myristoylating enzymes; protein N-myristoyltransferase; tetradecanoyl-CoA:glycylpeptide N-tetradecanoyltransferase
Systematic name: tetradecanoyl-CoA:N-terminal-glycine-[protein] N-tetradecanoyltransferase
Comments: The enzyme catalyses the transfer of myristic acid from myristoyl-CoA to the amino group of the N-terminal glycine residue in a variety of eukaryotic proteins. It uses an ordered Bi Bi reaction in which myristoyl-CoA binds to the enzyme prior to the binding of the peptide substrate, and CoA release precedes the release of the myristoylated peptide. The enzyme from yeast is profoundly affected by amino acids further from the N-terminus, and is particularly stimulated by a serine residue at position 5.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
MetaCyc,
PDB,
CAS registry number: 110071-61-9
References:
1. Guertin, D., Gris-Miron, L. and Riendeau, D. Identification of a 51-kilodalton polypeptide fatty acyl chain acceptor in soluble extracts from mouse cardiac tissue. Biochem. Cell Biol. 64 (1986) 1249-1255. [PMID: 3566958]
2. Heuckeroth, R.O., Towler, D.A., Adams, S.P., Glaser, L. and Gordon, J.I. 11-(Ethylthio)undecanoic acid. A myristic acid analogue of altered hydrophobicity which is functional for peptide N-myristoylation with wheat germ and yeast acyltransferase. J. Biol. Chem. 263 (1988) 2127-2133. [PMID: 3123489]
3. Towler, D.A., Adams, S.P., Eubanks, S.R., Towery, D.S., Jackson-Machelski, E., Glaser, L. and Gordon, J.I. Purification and characterization of yeast myristoyl CoA:protein N-myristoyltransferase. Proc. Natl Acad. Sci. USA 84 (1987) 2708-2712. [PMID: 3106975]
4. McIlhinney, R.A., Young, K., Egerton, M., Camble, R., White, A. and Soloviev, M. Characterization of human and rat brain myristoyl-CoA:protein N-myristoyltransferase: evidence for an alternative splice variant of the enzyme. Biochem. J. 333 (1998) 491-495. [PMID: 9677304]
5. Farazi, T.A., Waksman, G. and Gordon, J.I. Structures of Saccharomyces cerevisiae N-myristoyltransferase with bound myristoylCoA and peptide provide insights about substrate recognition and catalysis. Biochemistry 40 (2001) 6335-6343. [PMID: 11371195]
Accepted name: chlorogenate—glucarate O-hydroxycinnamoyltransferase
Reaction: chlorogenate + glucarate = quinate + 2-O-caffeoylglucarate
Other name(s): chlorogenate:glucarate caffeoyltransferase; chlorogenic acid:glucaric acid O-caffeoyltransferase; chlorogenate:glucarate caffeoyltransferase
Systematic name: chlorogenate:glucarate O-(hydroxycinnamoyl)transferase
Comments: Galactarate can act as acceptor, more slowly. Involved with EC 2.3.1.99 quinate O-hydroxycinnamoyltransferase in the formation of caffeoylglucarate in tomato.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
CAS registry number: 126124-92-3
References:
1. Strack, D. and Gross, W. Properties and activity changes of chlorogenic acid - glucaric acid caffeoyltransferase from tomato (Lycopersicon esculentum). Plant Physiol. 92 (1990) 41-47.
2. Strack, D., Gross, W., Wray, V. and Grotjahn, L. Enzymatic-synthesis of caffeoylglucaric acid from chlorogenic acid and glucaric acid by a protein preparation from tomato cotyledons. Plant Physiol. 83 (1987) 475-478.
Accepted name: quinate O-hydroxycinnamoyltransferase
Reaction: feruloyl-CoA + quinate = CoA + O-feruloylquinate
Other name(s): hydroxycinnamoyl coenzyme A-quinate transferase
Systematic name: feruloyl-CoA:quinate O-(hydroxycinnamoyl)transferase
Comments: Caffeoyl-CoA and 4-coumaroyl-CoA can also act as donors, but more slowly. Involved in the biosynthesis of chlorogenic acid in sweet potato and, with EC 2.3.1.98 chlorogenate—glucarate O-hydroxycinnamoyltransferase, in the formation of caffeoyl-CoA in tomato.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
PDB,
CAS registry number: 60321-02-0
References:
1. Strack, D., Gross, W., Wray, V. and Grotjahn, L. Enzymic sythesis of caffeoylglucaric acid from chlorogenic acid and glucaric acid by a protein preparation from tomato cotyledons. Plant Physiol. 83 (1987) 475-478.
2. 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.
3. Villegas, R.J.A. and Kojima, M. Purification and characterization of hydroxycinnamoyl D-glucose. Quinate hydroxycinnamoyl transferase in the root of sweet potato, Ipomoea batatas Lam. J. Biol. Chem. 261 (1986) 8729-8733. [PMID: 3722170]
Accepted name: [myelin-proteolipid] O-palmitoyltransferase
Reaction: palmitoyl-CoA + [myelin proteolipid] = CoA + O-palmitoyl-[myelin proteolipid]
Other name(s): myelin PLP acyltransferase; acyl-protein synthetase; myelin-proteolipid O-palmitoyltransferase
Systematic name: palmitoyl-CoA:[myelin-proteolipid] O-palmitoyltransferase
Comments: The enzyme in brain transfers long-chain acyl residues to the endogenous myelin proteolipid
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
CAS registry number: 82657-98-5
References:
1. Bizzozero, O.A., McGarry, J.F. and Lees, M.B. Acylation of endogenous myelin proteolipid protein with different acyl-CoAs. J. Biol. Chem. 262 (1987) 2138-2145. [PMID: 3818589]
Continued with EC 2.3.1.101 to EC 2.3.1.150
Return to EC 2 home page
Return to Enzymes home page
Return to IUBMB Biochemical Nomenclature home page