ExplorEnz: EC 2.3.1.16*

Your query returned 11 entries. Printable version

2.3.1.16

Accepted name:

acetyl-CoA C-acyltransferase

Reaction:

acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA (overall reaction)
(1a) [acetyl-CoA C-acyltransferase]-S-acyl-L-cysteine + acetyl-CoA = 3-oxoacyl-CoA + [acetyl-CoA C-acyltransferase]-L-cysteine
(1b) acyl-CoA + [acetyl-CoA C-acyltransferase]-L-cysteine = [acetyl-CoA C-acyltransferase]-S-acyl-L-cysteine + CoA

For diagram of aerobic phenylacetate catabolism, click here and for diagram of Benzoyl-CoA catabolism, click here

Other name(s):

β-ketothiolase; 3-ketoacyl-CoA thiolase; KAT; β-ketoacyl coenzyme A thiolase; β-ketoacyl-CoA thiolase; β-ketoadipyl coenzyme A thiolase; β-ketoadipyl-CoA thiolase; 3-ketoacyl CoA thiolase; 3-ketoacyl coenzyme A thiolase; 3-ketoacyl thiolase; 3-ketothiolase; 3-oxoacyl-CoA thiolase; 3-oxoacyl-coenzyme A thiolase; 6-oxoacyl-CoA thiolase; acetoacetyl-CoA β-ketothiolase; acetyl-CoA acyltransferase; ketoacyl-CoA acyltransferase; ketoacyl-coenzyme A thiolase; long-chain 3-oxoacyl-CoA thiolase; oxoacyl-coenzyme A thiolase; pro-3-ketoacyl-CoA thiolase; thiolase I; type I thiolase; 2-methylacetoacetyl-CoA thiolase [misleading]

Systematic name:

acyl-CoA:acetyl-CoA C-acyltransferase

Comments:

The enzyme, found in both eukaryotes and in prokaryotes, is involved in degradation pathways such as fatty acid β-oxidation. The enzyme acts on 3-oxoacyl-CoAs to produce acetyl-CoA and an acyl-CoA shortened by two carbon atoms. The reaction starts with the acylation of a nucleophilic cysteine at the active site by a 3-oxoacyl-CoA, with the concomitant release of acetyl-CoA. In the second step the acyl group is transferred to CoA. Most enzymes have a broad substrate range for the 3-oxoacyl-CoA. cf. EC 2.3.1.9, acetyl-CoA C-acetyltransferase.

Links to other databases:

BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9029-97-4

References:

1.	Beinert, H., Bock, R.M., Goldman, D.S., Green, D.E., Mahler, H.R., Mii, S., Stansly, P.G. and Wakil, S.J. A synthesis of dl-cortisone acetate. J. Am. Chem. Soc. 75 (1953) 4111–4112.
2.	Goldman, D.S. Studies on the fatty acid oxidizing system of animal tissue. VII. The β-ketoacyl coenzyme A cleavage enzyme. J. Biol. Chem. 208 (1954) 345–357. [PMID: 13174544]
3.	Stern, J.R., Coon, M.J. and del Campillo, A. Enzymatic breakdown and synthesis of acetoacetate. Nature 171 (1953) 28–30. [PMID: 13025466]

[EC 2.3.1.16 created 1961, modified 2019]

2.3.1.160

Accepted name:

vinorine synthase

Reaction:

acetyl-CoA + 16-epivellosimine = CoA + vinorine

For diagram of ajmaline, vinorine, vomilenine and raucaffricine biosynthesis, click here

Systematic name:

acyl-CoA:16-epivellosimine O-acetyltransferase (cyclizing)

Comments:

The reaction proceeds in two stages. The indole nitrogen of 16-epivellosimine interacts with its aldehyde group giving an hydroxy-substituted new ring. This alcohol is then acetylated. Also acts on gardneral (11-methoxy-16-epivellosimine). Generates the ajmalan skeleton, which forms part of the route to ajmaline.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 88844-97-7

References:

1.	Pfitzner, A., Polz, L. and Stöckligt, J. Properties of vinorine synthase the Rauwolfia enzyme involved in the formation of the ajmaline skeleton. Z. Naturforsch. C: Biosci. 41 (1986) 103–114.
2.	Bayer, A., Ma, X. and Stöckigt, J. Acetyltransfer in natural product biosynthesis—functional cloning and molecular analysis of vinorine synthase. Bioorg. Med. Chem. 12 (2004) 2787–2795. [DOI] [PMID: 15110860]
3.	Ma, X., Koepke, J., Bayer, A., Linhard, V., Fritzsch, G., Zhang, B., Michel, H. and Stöckigt, J. Vinorine synthase from Rauvolfia: the first example of crystallization and preliminary X-ray diffraction analysis of an enzyme of the BAHD superfamily. Biochim. Biophys. Acta 1701 (2004) 129–132. [DOI] [PMID: 15450182]
4.	Ma, X., Koepke, J., Panjikar, S., Fritzsch, G. and Stöckigt, J. Crystal structure of vinorine synthase, the first representative of the BAHD superfamily. J. Biol. Chem. 280 (2005) 13576–13583. [DOI] [PMID: 15665331]

[EC 2.3.1.160 created 2002]

2.3.1.161

Accepted name:

lovastatin nonaketide synthase

Reaction:

9 malonyl-CoA + 11 NADPH + 10 H⁺ + S-adenosyl-L-methionine + holo-[lovastatin nonaketide synthase] = dihydromonacolin L-[lovastatin nonaketide synthase] + 9 CoA + 9 CO₂ + 11 NADP⁺ + S-adenosyl-L-homocysteine + 6 H₂O

For diagram of polyketides biosynthesis, click here

Glossary:

dihydromonacolin L acid = (3R,5R)-7-[(1S,2S,4aR,6R,8aS)-2,6-dimethyl-1,2,4a,5,6,7,8,8a-octahydronaphthalen-1-yl]-3,5-dihydroxyheptanoate

Other name(s):

LNKS; LovB; LovC; acyl-CoA:malonyl-CoA C-acyltransferase (decarboxylating, oxoacyl- and enoyl-reducing, thioester-hydrolysing)

Systematic name:

acyl-CoA:malonyl-CoA C-acyltransferase (dihydromonacolin L acid-forming)

Comments:

This fungal enzyme system comprises a multi-functional polyketide synthase (PKS) and an enoyl reductase. The PKS catalyses many of the chain building reactions of EC 2.3.1.85, fatty-acid synthase system, as well as a reductive methylation and a Diels-Alder reaction, while the reductase is responsible for three enoyl reductions that are necessary for dihydromonacolin L acid production.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 235426-97-8

References:

1.	Ma, S.M., Li, J.W., Choi, J.W., Zhou, H., Lee, K.K., Moorthie, V.A., Xie, X., Kealey, J.T., Da Silva, N.A., Vederas, J.C. and Tang, Y. Complete reconstitution of a highly reducing iterative polyketide synthase. Science 326 (2009) 589–592. [DOI] [PMID: 19900898]
2.	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. [DOI] [PMID: 10334994]
3.	Auclair, K., Sutherland, A., Kennedy, J., Witter, D.J., van der Heever, J.P., Hutchinson, C.R. and Vederas, J.C. Lovastatin nonaketide synthase catalyses an intramolecular Diels-Alder reaction of a substrate analogue. J. Am. Chem. Soc. 122 (2000) 11519–11520.

[EC 2.3.1.161 created 2002, modified 2015, modified 2016, modified 2019]

2.3.1.162

Accepted name:

taxadien-5α-ol O-acetyltransferase

Reaction:

acetyl-CoA + taxa-4(20),11-dien-5α-ol = CoA + taxa-4(20),11-dien-5α-yl acetate

For diagram of taxadiene biosynthesis, click here

Other name(s):

acetyl coenzyme A:taxa-4(20),11(12)-dien-5α-ol O-acetyl transferase

Systematic name:

acetyl-CoA:taxa-4(20),11-dien-5α-ol O-acetyltransferase

Comments:

This is the third enzyme in the biosynthesis of the diterpenoid antineoplastic drug taxol (paclitaxel), which is widely used in the treatment of carcinomas, sarcomas and melanomas.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 229032-29-5

References:

1.	Walker, K., Ketchum, R.E., Hezari, M., Gatfield, D., Goleniowski, M., Barthol, A. and Croteau, R. Partial purification and characterization of acetyl coenzyme A: taxa-4(20),11(12)-dien-5α-ol O-acetyl transferase that catalyzes the first acylation step of taxol biosynthesis. Arch. Biochem. Biophys. 364 (1999) 273. [DOI] [PMID: 10190984]
2.	Walker, K., Schoendorf, A. and Croteau, R. Molecular cloning of a taxa-4(20),11(12)-dien-5α-ol-O-acetyl transferase cDNA from Taxus and functional expression in Escherichia coli. Arch. Biochem. Biophys. 374 (2000) 371–380. [DOI] [PMID: 10666320]

[EC 2.3.1.162 created 2002]

2.3.1.163

Accepted name:

10-hydroxytaxane O-acetyltransferase

Reaction:

acetyl-CoA + 10-desacetyltaxuyunnanin C = CoA + taxuyunnanin C

For diagram of reaction, click here

Other name(s):

acetyl coenzyme A: 10-hydroxytaxane O-acetyltransferase

Systematic name:

acetyl-CoA:taxan-10β-ol O-acetyltransferase

Comments:

Acts on a number of related taxane diterpenoids with a free 10β-hydroxy group. May be identical to EC 2.3.1.167, 10-deacetylbaccatin III 10-O-acetyltransferase.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 220946-63-4

References:

1.	Menhard, B. and Zenk, M.H. Purification and characterization of acetyl coenzyme A: 10-hydroxytaxane O-acetyltransferase from cell suspension cultures of Taxus chinensis. Phytochemistry 50 (1999) 763. [DOI] [PMID: 10192963]

[EC 2.3.1.163 created 2002]

2.3.1.164

Accepted name:

isopenicillin-N N-acyltransferase

Reaction:

phenylacetyl-CoA + isopenicillin N + H₂O = CoA + penicillin G + L-2-aminohexanedioate

For diagram of penicillin biosynthesis and metabolism, click here

Other name(s):

acyl-coenzyme A:isopenicillin N acyltransferase; isopenicillin N:acyl-CoA: acyltransferase

Systematic name:

acyl-CoA:isopenicillin N N-acyltransferase

Comments:

Proceeds by a two stage mechanism via 6-aminopenicillanic acid. Different from EC 3.5.1.11, penicillin amidase.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 54576-90-8

References:

1.	Tobin, M.B., Fleming, M.D., Skatrud, P.L. and Miller, J.R. Molecular characterization of the acyl-coenzyme A:isopenicillin N acyltransferase gene (penDE) from Penicillium chrysogenum and Aspergillus nidulans and activity of recombinant enzyme in Escherichia coli. J. Bacteriol. 172 (1990) 5908–5914. [DOI] [PMID: 2120195]
2.	Aplin, R.T., Baldwin, J.E., Roach, P.L., Robinson, C.V. and Schofield, C.J. Investigations into the post-translational modification and mechanism of isopenicillin N:acyl-CoA acyltransferase using electrospray mass spectrometry. Biochem. J. 294 (1993) 357–363. [PMID: 8396910]

[EC 2.3.1.164 created 2002]

2.3.1.165

Accepted name:

6-methylsalicylic-acid synthase

Reaction:

acetyl-CoA + 3 malonyl-CoA + NADPH + H⁺ = 6-methylsalicylate + 4 CoA + 3 CO₂ + NADP⁺ + H₂O

For diagram of polyketides biosynthesis, click here

Other name(s):

MSAS; 6-methylsalicylic acid synthase

Systematic name:

acyl-CoA:malonyl-CoA C-acyltransferase (decarboxylating, oxoacyl-reducing, thioester-hydrolysing and cyclizing)

Comments:

A multienzyme complex with a tightly-bound 4′-phosphopantetheine cofactor on the acyl carrier protein. It has a similar sequence to vertebrate type I fatty acid synthase. Acetoacetyl-CoA can also act as a starter molecule.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9045-37-8

References:

1.	Spencer, J.B. and Jordan, P.M. Purification and properties of 6-methylsalicylic acid synthase from Penicillium patulum. Biochem. J. 288 (1992) 839–846. [PMID: 1471999]
2.	Child, C.J., Spencer, J.B., Bhogal, P. and Shoolingin-Jordan, P.M. Structural similarities between 6-methylsalicylic acid synthase from Penicillium patulum and vertebrate type I fatty acid synthase: evidence from thiol modification studies. Biochemistry 35 (1996) 12267–12274. [DOI] [PMID: 8823160]
3.	Richardson, M.T., Pohl, N.L., Kealey, J.T. and Khosla, C. Tolerance and specificity of recombinant 6-methylsalicyclic acid synthase. Metab. Eng. 1 (1999) 180–187. [DOI] [PMID: 10935930]

[EC 2.3.1.165 created 2002]

2.3.1.166

Accepted name:

2α-hydroxytaxane 2-O-benzoyltransferase

Reaction:

benzoyl-CoA + 10-deacetyl-2-debenzoylbaccatin III = CoA + 10-deacetylbaccatin III

For diagram of taxol biosynthesis, click here

Other name(s):

benzoyl-CoA:taxane 2α-O-benzoyltransferase

Systematic name:

benzoyl-CoA:taxan-2α-ol O-benzoyltransferase

Comments:

The enzyme was studied using the semisynthetic substrate 2-debenzoyl-7,13-diacetylbaccatin III. It will not acylate the hydroxy group at 1β, 7β, 10β or 13α of 10-deacetyl baccatin III, or at 2α or 5α of taxa-4(20),11-diene-2α,5α-diol.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 329318-50-5

References:

1.	Walker, K. and Croteau, R. Taxol biosynthesis: molecular cloning of a benzoyl-CoA:taxane 2α-O-benzoyltransferase cDNA from taxus and functional expression in Escherichia coli. Proc. Natl. Acad. Sci. USA 97 (2000) 13591. [DOI] [PMID: 11095755]

[EC 2.3.1.166 created 2002]

2.3.1.167

Accepted name:

10-deacetylbaccatin III 10-O-acetyltransferase

Reaction:

acetyl-CoA + 10-deacetylbaccatin III = CoA + baccatin III

For diagram of taxol biosynthesis, click here

Systematic name:

acetyl-CoA:taxan-10β-ol O-acetyltransferase

Comments:

The enzyme will not acylate the hydroxy group at 1β, 7β or 13α of 10-deacetyl baccatin III, or at 5α of taxa-4(20),11-dien-5α-ol. May be identical to EC 2.3.1.163, 10-hydroxytaxane O-acetyltransferase.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 220946-63-4

References:

1.	Walker, K. and Croteau, R. Molecular cloning of a 10-deacetylbaccatin III-10-O-acetyl transferase cDNA from Taxus and functional expression in Escherichia coli. Proc. Natl. Acad. Sci. USA 97 (2000) 583–587. [DOI] [PMID: 10639122]

[EC 2.3.1.167 created 2002]

2.3.1.168

Accepted name:

dihydrolipoyllysine-residue (2-methylpropanoyl)transferase

Reaction:

2-methylpropanoyl-CoA + enzyme N⁶-(dihydrolipoyl)lysine = CoA + enzyme N⁶-(S-[2-methylpropanoyl]dihydrolipoyl)lysine

For diagram of oxo-acid-dehydrogenase complexes, click here

Glossary:

dihydrolipoyl group

Other name(s):

dihydrolipoyl transacylase; enzyme-dihydrolipoyllysine:2-methylpropanoyl-CoA S-(2-methylpropanoyl)transferase; 2-methylpropanoyl-CoA:enzyme-6-N-(dihydrolipoyl)lysine S-(2-methylpropanoyl)transferase

Systematic name:

2-methylpropanoyl-CoA:enzyme-N⁶-(dihydrolipoyl)lysine S-(2-methylpropanoyl)transferase

Comments:

A multimer (24-mer) of this enzyme forms the core of the multienzyme 3-methyl-2-oxobutanoate dehydrogenase complex, and binds tightly both EC 1.2.4.4, 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) and EC 1.8.1.4, dihydrolipoyl dehydrogenase. The lipoyl group of this enzyme is reductively 2-methylpropanoylated by EC 1.2.4.4, and the only observed direction catalysed by EC 2.3.1.168 is that where this 2-methylpropanoyl is passed to coenzyme A. In addition to the 2-methylpropanoyl group, formed when EC 1.2.4.4 acts on the oxoacid that corresponds with valine, this enzyme also transfers the 3-methylbutanoyl and S-2-methylbutanoyl groups, donated to it when EC 1.2.4.4 acts on the oxo acids corresponding with leucine and isoleucine.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 102784-26-9

References:

1.	Massey, L.K., Sokatch, J.R. and Conrad, R.S. Branched-chain amino acid catabolism in bacteria. Bacteriol. Rev. 40 (1976) 42–54. [PMID: 773366]
2.	Chuang, D.T., Hu, C.C., Ku, L.S., Niu, W.L., Myers, D.E. and Cox, R.P. Catalytic and structural properties of the dihydrolipoyl transacylase component of bovine branched-chain α-keto acid dehydrogenase. J. Biol. Chem. 259 (1984) 9277–9284. [PMID: 6746648]
3.	Wynn, R.M., Davie, J.R., Zhi, W., Cox, R.P. and Chuang, D.T. In vitro reconstitution of the 24-meric E2 inner core of bovine mitochondrial branched-chain α-keto acid dehydrogenase complex: requirement for chaperonins GroEL and GroES. Biochemistry 33 (1994) 8962–8968. [PMID: 7913832]
4.	Perham, R.N. Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions. Annu. Rev. Biochem. 69 (2000) 961–1004. [DOI] [PMID: 10966480]

[EC 2.3.1.168 created 2003]

2.3.1.169

Accepted name:

CO-methylating acetyl-CoA synthase

Reaction:

acetyl-CoA + a [Co(I) corrinoid Fe-S protein] = CO + CoA + a [methyl-Co(III) corrinoid Fe-S protein]

Systematic name:

acetyl-CoA:corrinoid protein O-acetyltransferase

Comments:

Contains nickel, copper and iron-sulfur clusters. Involved, together with EC 1.2.7.4, carbon-monoxide dehydrogenase (ferredoxin), in the synthesis of acetyl-CoA from CO₂ and H₂.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 176591-19-8

References:

1.	Ragsdale, S.W. and Wood, H.G. Acetate biosynthesis by acetogenic bacteria. Evidence that carbon monoxide dehydrogenase is the condensing enzyme that catalyzes the final steps of the synthesis. J. Biol. Chem. 260 (1985) 3970–3977. [PMID: 2984190]
2.	Doukov, T.I., Iverson, T., Seravalli, J., Ragsdale, S.W. and Drennan, C.L. A Ni-Fe-Cu center in a bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase. Science 298 (2002) 567–572. [DOI] [PMID: 12386327]

[EC 2.3.1.169 created 2003, modified 2015]