ExplorEnz: EC 2.3.1.7*

Your query returned 11 entries. Printable version

2.3.1.7

Accepted name:

carnitine O-acetyltransferase

Reaction:

acetyl-CoA + carnitine = CoA + O-acetylcarnitine

Other name(s):

acetyl-CoA-carnitine O-acetyltransferase; acetylcarnitine transferase; carnitine acetyl coenzyme A transferase; carnitine acetylase; carnitine acetyltransferase; carnitine-acetyl-CoA transferase; CATC

Systematic name:

acetyl-CoA:carnitine O-acetyltransferase

Comments:

Also acts on propanoyl-CoA and butanoyl-CoA (cf. EC 2.3.1.21 carnitine O-palmitoyltransferase and EC 2.3.1.137 carnitine O-octanoyltransferase).

Links to other databases:

BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9029-90-7

References:

1.	Chase, J.F.A., Pearson, D.J. and Tubbs, P.K. The preparation of crystalline carnitine acetyltransferase. Biochim. Biophys. Acta 96 (1965) 162–165. [DOI] [PMID: 14285260]
2.	Friedman, S. and Fraenkel, G. Reversible enzymatic acetylation of carnitine. Arch. Biochem. Biophys. 59 (1955) 491–501. [DOI] [PMID: 13275966]
3.	Miyazawa, S., Ozasa, H., Furuta, S., Osumi, T. and Hashimoto, T. Purification and properties of carnitine acetyl transferase from rat liver. J. Biochem. (Tokyo) 93 (1983) 439–451. [PMID: 6404901]

[EC 2.3.1.7 created 1961]

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]

2.3.1.71

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]

[EC 2.3.1.71 created 1984]

2.3.1.72

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. [DOI] [PMID: 6446303]

[EC 2.3.1.72 created 1984, modified 2003]

2.3.1.73

Accepted name:

diacylglycerol—sterol O-acyltransferase

Reaction:

a 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. [DOI] [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.

[EC 2.3.1.73 created 1984]

2.3.1.74

Accepted name:

chalcone synthase

Reaction:

3 malonyl-CoA + 4-coumaroyl-CoA = 4 CoA + naringenin chalcone + 3 CO₂

For diagram of chalcone and stilbene biosynthesis, 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. [DOI] [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. [DOI] [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. [DOI] [PMID: 28482241]

[EC 2.3.1.74 created 1984, modified 2018]

2.3.1.75

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.

[EC 2.3.1.75 created 1984]

2.3.1.76

Accepted name:

retinol O-fatty-acyltransferase

Reaction:

acyl-CoA + retinol = CoA + retinyl ester

For diagram of biosynthesis of retinal and derivatives, 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. [DOI] [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]

[EC 2.3.1.76 created 1984]

2.3.1.77

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-hydroxysteroids 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.

[EC 2.3.1.77 created 1984]

2.3.1.78

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. [DOI] [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]

[EC 2.3.1.78 created 1984]

2.3.1.79

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. [DOI] [PMID: 12731863]

[EC 2.3.1.79 created 1984]