Enzyme Nomenclature

Continued from EC 6.1.1

EC 6.2

Forming Carbon—Sulfur Bonds

EC 6.2.1 Acid—Thiol Ligases

Contents

EC 6.2.1.1 acetate—CoA ligase
EC 6.2.1.2 butyrate—CoA ligase
EC 6.2.1.3 long-chain-fatty-acid—CoA ligase
EC 6.2.1.4 succinate—CoA ligase (GDP-forming)
EC 6.2.1.5 succinate—CoA ligase (ADP-forming)
EC 6.2.1.6 glutarate—CoA ligase
EC 6.2.1.7 cholate—CoA ligase
EC 6.2.1.8 oxalate—CoA ligase
EC 6.2.1.9 malate—CoA ligase
EC 6.2.1.10 acid—CoA ligase (GDP-forming)
EC 6.2.1.11 biotin—CoA ligase
EC 6.2.1.12 4-coumarate—CoA ligase
EC 6.2.1.13 acetate—CoA ligase (ADP-forming)
EC 6.2.1.14 6-carboxyhexanoate—CoA ligase
EC 6.2.1.15 arachidonate—CoA ligase
EC 6.2.1.16 acetoacetate—CoA ligase
EC 6.2.1.17 propionate—CoA ligase
EC 6.2.1.18 citrate—CoA ligase
EC 6.2.1.19 long-chain-fatty-acid—protein ligase
EC 6.2.1.20 long-chain-fatty-acid—[acyl-carrier-protein] ligase
EC 6.2.1.21 covered by EC 6.2.1.30
EC 6.2.1.22 citrate (pro-3S)-lyase ligase
EC 6.2.1.23 dicarboxylate—CoA ligase
EC 6.2.1.24 phytanate—CoA ligase
EC 6.2.1.25 benzoate—CoA ligase
EC 6.2.1.26 o-succinylbenzoate—CoA ligase
EC 6.2.1.27 4-hydroxybenzoate—CoA ligase
EC 6.2.1.28 3α,7α-dihydroxy-5β-cholestanate—CoA ligase
EC 6.2.1.29 deleted now EC 6.2.1.7
EC 6.2.1.30 phenylacetate—CoA ligase
EC 6.2.1.31 2-furoate—CoA ligase
EC 6.2.1.32 anthranilate—CoA ligase
EC 6.2.1.33 4-chlorobenzoate—CoA ligase
EC 6.2.1.34 trans-feruloyl-CoA synthase
EC 6.2.1.35 ACP-SH:acetate ligase
EC 6.2.1.36 3-hydroxypropionyl-CoA synthase
EC 6.2.1.37 3-hydroxybenzoate—CoA ligase
EC 6.2.1.38 (2,2,3-trimethyl-5-oxocyclopent-3-enyl)acetyl-CoA synthase
EC 6.2.1.39 [butirosin acyl-carrier protein]—L-glutamate ligase
EC 6.2.1.40 4-hydroxybutyrate—CoA ligase
EC 6.2.1.41 3-[(3aS,4S,7aS)-7a-methyl-1,5-dioxo-octahydro-1H-inden-4-yl]propanoate—CoA ligase
EC 6.2.1.42 3-oxocholest-4-en-26-oate—CoA ligase
EC 6.2.1.43 2-hydroxy-7-methoxy-5-methyl-1-naphthoate—CoA ligase
EC 6.2.1.44 3-(methylthio)propionyl—CoA ligase
EC 6.2.1.45 E1 ubiquitin-activating enzyme
EC 6.2.1.46 L-allo-isoleucine:holo-[CmaA peptidyl-carrier protein] ligase
EC 6.2.1.47 medium-chain-fatty-acid—[acyl-carrier-protein] ligase

Entries

EC 6.2.1.1

Accepted name: acetate—CoA ligase

Reaction: ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA

Other name(s): acetyl-CoA synthetase; acetyl activating enzyme; acetate thiokinase; acyl-activating enzyme; acetyl coenzyme A synthetase; acetic thiokinase; acetyl CoA ligase; acetyl CoA synthase; acetyl-coenzyme A synthase; short chain fatty acyl-CoA synthetase; short-chain acyl-coenzyme A synthetase; ACS

Systematic name: acetate:CoA ligase (AMP-forming)

Comments: Also acts on propanoate and propenoate.

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9012-31-1

References:

1. Chou, T.C. and Lipmann, F. Separation of acetyl transfer enzymes in pigeon liver extract. J. Biol. Chem. 196 (1952) 89-103.

2. Eisenberg, M.A. The acetate-activating enzyme of Rhodospirillum rubrum. Biochim. Biophys. Acta 16 (1955) 58-65.

3. Hele, P. The acetate activating enzyme of beef heart. J. Biol. Chem. 206 (1954) 671-676.

4. Millerd, A. and Bonner, J. Acetate activation and acetoacetate formation in plant systems. Arch. Biochem. Biophys. 49 (1954) 343-355.

[EC 6.2.1.1 created 1961]

EC 6.2.1.2

Accepted name: butyrate—CoA ligase

Reaction: ATP + a carboxylate + CoA = AMP + diphosphate + an acyl-CoA

Other name(s): butyryl-CoA synthetase; fatty acid thiokinase (medium chain); acyl-activating enzyme; fatty acid elongase; fatty acid activating enzyme; fatty acyl coenzyme A synthetase; medium chain acyl-CoA synthetase; butyryl-coenzyme A synthetase; L-(+)-3-hydroxybutyryl CoA ligase; short-chain acyl-CoA synthetase

Systematic name: butanoate:CoA ligase (AMP-forming)

Comments: Acts on acids from C4 to C11 and on the corresponding 3-hydroxy- and 2,3- or 3,4-unsaturated acids.

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9080-51-7

References:

1. Mahler, H.R., Wakil, S.J. and Bock, R.M. Studies on fatty acid oxidation. I. Enzymatic activation of fatty acids. J. Biol. Chem. 204 (1953) 453-468. [PMID: 13084616]

2. Massaro, E.J. and Lennarz, W.J. The partial purification and characterization of a bacterial fatty acyl coenzyme A synthetase. Biochemistry 4 (1965) 85-90. [PMID: 14285249]

3. Websterlt, J.R., Gerowin, L.D. and Rakita, L. Purification and characteristics of a butyryl coenzyme A synthetase from bovine heart mitochondria. J. Biol. Chem. 240 (1965) 29-33. [PMID: 14253428]

[EC 6.2.1.2 created 1961, modified 2011]

EC 6.2.1.3

Accepted name: long-chain-fatty-acid—CoA ligase

Reaction: ATP + a long-chain carboxylate + CoA = AMP + diphosphate + an acyl-CoA

Other name(s): acyl-CoA synthetase; fatty acid thiokinase (long chain); acyl-activating enzyme; palmitoyl-CoA synthase; lignoceroyl-CoA synthase; arachidonyl-CoA synthetase; acyl coenzyme A synthetase; acyl-CoA ligase; palmitoyl coenzyme A synthetase; thiokinase; palmitoyl-CoA ligase; acyl-coenzyme A ligase; fatty acid CoA ligase; long-chain fatty acyl coenzyme A synthetase; oleoyl-CoA synthetase; stearoyl-CoA synthetase; long chain fatty acyl-CoA synthetase; long-chain acyl CoA synthetase; fatty acid elongase; LCFA synthetase; pristanoyl-CoA synthetase; ACS3; long-chain acyl-CoA synthetase I; long-chain acyl-CoA synthetase II; fatty acyl-coenzyme A synthetase; long-chain acyl-coenzyme A synthetase; FAA1

Systematic name: long-chain fatty acid:CoA ligase (AMP-forming)

Comments: Acts on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. The liver enzyme acts on acids from C6 to C20; that from brain shows high activity up to C24.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, CAS registry number: 9013-18-7

References:

1. Bakken, A.M. and Farstad, M. Identical subcellular distribution of palmitoyl-CoA and arachidonoyl-CoA synthetase activities in human blood platelets. Biochem. J. 261 (1989) 71-76. [PMID: 2528345]

2. Hosaka, K., Mishima, M., Tanaka, T., Kamiryo, T. and Numa, S. Acyl-coenzyme-A synthetase I from Candida lipolytica. Purification, properties and immunochemical studies. Eur. J. Biochem. 93 (1979) 197-203. [PMID: 108099]

3. Nagamatsu, K., Soeda, S., Mori, M. and Kishimoto, Y. Lignoceroyl-coenzyme A synthetase from developing rat brain: partial purification, characterization and comparison with palmitoyl-coenzyme A synthetase activity and liver enzyme. Biochim. Biophys. Acta 836 (1985) 80-88. [PMID: 3161545]

4. Tanaka, T., Hosaka, K., Hoshimaru, M. and Numa, S. Purification and properties of long-chain acyl-coenzyme-A synthetase from rat liver. Eur. J. Biochem. 98 (1979) 165-172. [PMID: 467438]

[EC 6.2.1.3 created 1961, modified 1989, modified 2011]

EC 6.2.1.4

Accepted name: succinate—CoA ligase (GDP-forming)

Reaction: GTP + succinate + CoA = GDP + phosphate + succinyl-CoA

For diagram of reaction click here.

Other name(s): succinyl-CoA synthetase (GDP-forming); succinyl coenzyme A synthetase (guanosine diphosphate-forming); succinate thiokinase; succinic thiokinase; succinyl coenzyme A synthetase; succinate-phosphorylating enzyme; P-enzyme; SCS; G-STK; succinyl coenzyme A synthetase (GDP-forming); succinyl CoA synthetase; succinyl coenzyme A synthetase

Systematic name: succinate:CoA ligase (GDP-forming)

Comments: Itaconate can act instead of succinate, and ITP instead of GTP.

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9014-36-2

References:

1. Hager, L.P. Succinyl CoA synthetase, in Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd edn., vol. 6, Academic Press, New York, 1962, pp. 387-399.

2. Kaufman, S., Gilvarg, C., Cori, O. and Ochoa, S. Enzymatic oxidation of α-ketoglutarate and coupled phosphorylation. J. Biol. Chem. 203 (1953) 869-888.

3. Mazumder, R., Sanadi, D.R. and Rodwell, W.V. Purification and properties of hog kidney succinic thiokinase. J. Biol. Chem. 235 (1960) 2546-2550.

4. Sanadi, D.R., Gibson, D.M. and Ayengar, P. Guanosine triphosphate, the primary product of phosphorylation coupled to the breakdown of succinyl coenzyme A. Biochim. Biophys. Acta 14 (1954) 434-436.

[EC 6.2.1.4 created 1961]

EC 6.2.1.5

Accepted name: succinate—CoA ligase (ADP-forming)

Reaction: ATP + succinate + CoA = ADP + phosphate + succinyl-CoA

For diagram of reaction click here.

Other name(s): succinyl-CoA synthetase (ADP-forming); succinic thiokinase; succinate thiokinase; succinyl-CoA synthetase; succinyl coenzyme A synthetase (adenosine diphosphate-forming); succinyl coenzyme A synthetase; A-STK (adenin nucleotide-linked succinate thiokinase); STK; A-SCS

Systematic name: succinate:CoA ligase (ADP-forming)

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, UM-BBD, CAS registry number: 9080-33-5

References:

1. Hager, L.P. Succinyl CoA synthetase, in Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd edn., vol. 6, Academic Press, New York, 1962, pp. 387-399.

2. Kaufman, S. Studies on the mechanism of the reaction catalyzed by the phosphorylating enzyme. J. Biol. Chem. 216 (1955) 153-164.

3. Kaufman, S. and Alivasatos, S.G.A. Purification and properties of the phosphorylating enzyme from spinach. J. Biol. Chem. 216 (1955) 141-152.

[EC 6.2.1.5 created 1961]

EC 6.2.1.6

Accepted name: glutarate—CoA ligase

Reaction: ATP + glutarate + CoA = ADP + phosphate + glutaryl-CoA

Other name(s): glutaryl-CoA synthetase; glutaryl coenzyme A synthetase

Systematic name: glutarate:CoA ligase (ADP-forming)

Comments: GTP or ITP can act instead of ATP.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9023-68-1

References:

1. Menon, G.K.K., Friedman, D.L. and Stern, J.R. Enzymic synthesis of glutaryl-coenzyme A. Biochim. Biophys. Acta 44 (1960) 375-377.

[EC 6.2.1.6 created 1961]

EC 6.2.1.7

Accepted name: cholate—CoA ligase

Reaction: (1) ATP + cholate + CoA = AMP + diphosphate + choloyl-CoA

(2) ATP + (25R)-3α,7α,12α-trihydroxy-5β-cholestanoate + CoA = AMP + diphosphate + (25R)-3α,7α,12α-trihydroxy-5β-cholestanoyl-CoA

For diagram click here.

Glossary: cholate = 3α,7α,12α-trihydroxy-5β-cholan-24-oate
trihydroxycoprostanoate = 3α,7α,12α-trihydroxy-5β-cholestan-26-oate

Other name(s): BAL; bile acid CoA ligase; bile acid coenzyme A ligase; choloyl-CoA synthetase; choloyl coenzyme A synthetase; cholic thiokinase; cholate thiokinase; cholic acid:CoA ligase; 3α,7α,12α-trihydroxy-5β-cholestanoyl coenzyme A synthetase; 3α,7α,12α-trihydroxy-5β-cholestanoate-CoA ligase; 3α,7α,12α-trihydroxy-5β-cholestanoate-CoA synthetase; THCA-CoA ligase; 3α,7α,12α-trihydroxy-5β-cholestanate—CoA ligase; 3α,7α,12α-trihydroxy-5β-cholestanate:CoA ligase (AMP-forming); cholyl-CoA synthetase; trihydroxycoprostanoyl-CoA synthetase

Systematic name: cholate:CoA ligase (AMP-forming)

Comments: Requires Mg2+ for activity. The mammalian enzyme is membrane-bound and catalyses the first step in the conjugation of bile acids with amino acids, converting bile acids into their acyl-CoA thioesters. Chenodeoxycholate, deoxycholate, lithocholate and trihydroxycoprostanoate can also act as substrates [7]. The bacterial enzyme is soluble and participates in an anaerobic bile acid 7 α-dehydroxylation pathway [5].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9027-90-1

References:

1. Elliott, W.H. The enzymic activation of cholic acid by guinea-pig-liver microsomes. Biochem. J. 62 (1956) 427-433. [PMID: 13303991]

2. Elliott, W.H. The breakdown of adenosine triphosphate accompanying cholic acid activation by guinea-pig liver microsomes. Biochem. J. 65 (1957) 315-321. [PMID: 13403911]

3. Prydz, K., Kase, B.F., Björkhem, I. and Pedersen, J.I. Subcellular localization of 3α,7α-dihydroxy- and 3α,7α,12α-trihydroxy-5β-cholestanoyl-coenzyme A ligase(s) in rat liver. J. Lipid Res. 29 (1988) 997-1004. [PMID: 3183523]

4. Schepers, L., Casteels, M., Verheyden, K., Parmentier, G., Asselberghs, S., Eyssen, H.J. and Mannaerts, G.P. Subcellular distribution and characteristics of trihydroxycoprostanoyl-CoA synthetase in rat liver. Biochem. J. 257 (1989) 221-229. [PMID: 2521999]

5. Mallonee, D.H., Adams, J.L. and Hylemon, P.B. The bile acid-inducible baiB gene from Eubacterium sp. strain VPI 12708 encodes a bile acid-coenzyme A ligase. J. Bacteriol. 174 (1992) 2065-2071. [PMID: 1551828]

6. Wheeler, J.B., Shaw, D.R. and Barnes, S. Purification and characterization of a rat liver bile acid coenzyme A ligase from rat liver microsomes. Arch. Biochem. Biophys. 348 (1997) 15-24. [PMID: 9390170]

7. 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]

[EC 6.2.1.7 created 1961 (EC 6.2.1.29 created 1992, incorporated 2005), modified 2005]

EC 6.2.1.8

Accepted name: oxalate—CoA ligase

Reaction: ATP + oxalate + CoA = AMP + diphosphate + oxalyl-CoA

Other name(s): oxalyl-CoA synthetase; oxalyl coenzyme A synthetase

Systematic name: oxalate:CoA ligase (AMP-forming)

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37318-57-3

References:

1. Giovanelli, J. Oxalyl-coenzyme A synthetase from pea seeds. Biochim. Biophys. Acta 118 (1966) 124-143. [PMID: 4288975]

[EC 6.2.1.8 created 1972]

EC 6.2.1.9

Accepted name: malate—CoA ligase

Reaction: ATP + malate + CoA = ADP + phosphate + malyl-CoA

Other name(s): malyl-CoA synthetase; malyl coenzyme A synthetase; malate thiokinase

Systematic name: malate:CoA ligase (ADP-forming)

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37318-58-4

References:

1. Mue, S., Tuboi, S. and Kikuchi, G. On malyl-coenzyme A synthetase. J. Biochem. (Tokyo) 56 (1964) 545-551.

[EC 6.2.1.9 created 1972]

EC 6.2.1.10

Accepted name: acid—CoA ligase (GDP-forming)

Reaction: GTP + a carboxylate + CoA = GDP + phosphate + acyl-CoA

Other name(s): acyl-CoA synthetase (GDP-forming); acyl coenzyme A synthetase (guanosine diphosphate forming)

Systematic name: carboxylic acid:CoA ligase (GDP-forming)

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37318-59-5

References:

1. Rossi, C.R. and Gibson, D.M. Activation of fatty acids by a guanosine triphosphate-specific thiokinase from liver mitochondria. J. Biol. Chem. 239 (1964) 1694-1699. [PMID: 14213337]

[EC 6.2.1.10 created 1972, modified 2011]

EC 6.2.1.11

Accepted name: biotin—CoA ligase

Reaction: ATP + biotin + CoA = AMP + diphosphate + biotinyl-CoA

Other name(s): biotinyl-CoA synthetase; biotin CoA synthetase; biotinyl coenzyme A synthetase

Systematic name: biotin:CoA ligase (AMP-forming)

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37318-60-8

References:

1. Christner, J.E., Schlesinger, M.J. and Coon, M.J. Enzymatic activation of biotin. Biotinyl adenylate formation. J. Biol. Chem. 239 (1964) 3997-4005.

[EC 6.2.1.11 created 1972]

EC 6.2.1.12

Accepted name: 4-coumarate—CoA ligase

Reaction: ATP + 4-coumarate + CoA = AMP + diphosphate + 4-coumaroyl-CoA

For diagram click here.

Glossary:
4-coumarate: 3-(4-hydroxyphenyl)prop-2-enoate

Other name(s): 4-coumaroyl-CoA synthetase; p-coumaroyl CoA ligase; p-coumaryl coenzyme A synthetase; p-coumaryl-CoA synthetase; p-coumaryl-CoA ligase; feruloyl CoA ligase; hydroxycinnamoyl CoA synthetase; 4-coumarate:coenzyme A ligase; caffeolyl coenzyme A synthetase; p-hydroxycinnamoyl coenzyme A synthetase; feruloyl coenzyme A synthetase; sinapoyl coenzyme A synthetase; 4-coumaryl-CoA synthetase; hydroxycinnamate:CoA ligase; p-coumaryl-CoA ligase; p-hydroxycinnamic acid:CoA ligase; 4CL

Systematic name: 4-coumarate:CoA ligase (AMP-forming)

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37332-51-7

References:

1. Gross, G.G. and Zenk, M.H. Isolation and properties of hydroxycinnamate: CoA ligase from lignifying tissue of Forsythia. Eur. J. Biochem. 42 (1974) 453-459. [PMID: 4364250]

2. Lindl, T., Kreuzaler, F. and Hahlbrock, F. Synthesis of p-coumaroyl coenzyme A with a partially purified p-coumarate:CoA ligase from cell suspension cultures of soybean (Glycine max). Biochim. Biophys. Acta 302 (1973) 457-464. [PMID: 4699252]

[EC 6.2.1.12 created 1976]

EC 6.2.1.13

Accepted name: acetate—CoA ligase (ADP-forming)

Reaction: ATP + acetate + CoA = ADP + phosphate + acetyl-CoA

Other name(s): acetyl-CoA synthetase (ADP-forming); acetyl coenzyme A synthetase (adenosine diphosphate-forming); acetate thiokinase

Systematic name: acetate:CoA ligase (ADP-forming)

Comments: Also acts on propanoate and, very slowly, on butanoate.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 62009-85-2

References:

1. Reeves, R.E., Warren, L.G., Susskind, B. and Lo, H.-S. An energy-conserving pyruvate-to-acetate pathway in Entamoeba histolytica. Pyruvate synthase and a new acetate thiokinase. J. Biol. Chem. 252 (1977) 726-731. [PMID: 13076]

[EC 6.2.1.13 created 1978]

EC 6.2.1.14

Accepted name: 6-carboxyhexanoate—CoA ligase

Reaction: ATP + 6-carboxyhexanoate + CoA = AMP + diphosphate + 6-carboxyhexanoyl-CoA

Other name(s): 6-carboxyhexanoyl-CoA synthetase; pimelyl-CoA synthetase

Systematic name: 6-carboxyhexanoate:CoA ligase (AMP-forming)

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 55467-50-0

References:

1. Izumi, Y., Morita, H., Sato, K., Tani, Y. and Ogata, K. Synthesis of biotin-vitamers from pimelic acid and coenzyme A by cell-free extracts of various bacteria. Biochim. Biophys. Acta 264 (1972) 210-213. [PMID: 4623286]

2. Izumi, Y., Morita, H., Tani, Y. and Ogata, K. The pimelyl-CoA synthetase responsible for the first step in biotin biosynthesis by microorganisms. Agric. Biol. Chem. 38 (1974) 2257-2262.

[EC 6.2.1.14 created 1983]

EC 6.2.1.15

Accepted name: arachidonate—CoA ligase

Reaction: ATP + arachidonate + CoA = AMP + diphosphate + arachidonoyl-CoA

Glossary:
arachidonate: (all-Z)-icosa-5,8,11,14-tetraenoate

Other name(s): arachidonoyl-CoA synthetase

Systematic name: arachidonate:CoA ligase (AMP-forming)

Comments: Not identical with EC 6.2.1.3 long-chain-fatty-acid—CoA ligase. Icosa-8,11,14-trienoate, but not the other long-chain fatty acids, can act in place of arachidonate.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 82047-87-8

References:

1. Wilson, D.B., Prescott, S.M. and Majerus, P.W. Discovery of an arachidonoyl coenzyme A synthetase in human platelets. J. Biol. Chem. 257 (1982) 3510-3515. [PMID: 7061494]

[EC 6.2.1.15 created 1984]

EC 6.2.1.16

Accepted name: acetoacetate—CoA ligase

Reaction: ATP + acetoacetate + CoA = AMP + diphosphate + acetoacetyl-CoA

For diagram click here.

Other name(s): acetoacetyl-CoA synthetase

Systematic name: acetoacetate:CoA ligase (AMP-forming)

Comments: Also acts, more slowly, on L-3-hydroxybutanoate.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 39394-62-2

References:

1. Fukui, T., Ito, M. and Tomita, K. Purification and characterization of acetoacetyl-CoA synthetase from Zoogloea ramigera I-16-M. Eur. J. Biochem. 127 (1982) 423-428. [PMID: 7140777]

[EC 6.2.1.16 created 1984]

EC 6.2.1.17

Accepted name: propionate—CoA ligase

Reaction: ATP + propanoate + CoA = AMP + diphosphate + propanoyl-CoA

Other name(s): propionyl-CoA synthetase

Systematic name: propanoate:CoA ligase (AMP-forming)

Comments: Propenoate can act instead of propanoate. Not identical with EC 6.2.1.1 (acetate—CoA ligase) or EC 6.2.1.2 (butyrate—CoA ligase).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 55326-49-3

References:

1. Ricks, C.A. and Cook, R.M. Regulation of volatile fatty acid uptake by mitochondrial acyl CoA synthetases of bovine liver. J. Dairy Sci. 64 (1981) 2324-2335. [PMID: 7341659]

[EC 6.2.1.17 created 1984]

EC 6.2.1.18

Accepted name: citrate—CoA ligase

Reaction: ATP + citrate + CoA = ADP + phosphate + (3S)-citryl-CoA

Glossary
citrate: 2-hydroxypropane-1,2,3-tricarboxylate

Other name(s): citryl-CoA synthetase; citrate:CoA ligase; citrate thiokinase

Systematic name: citrate:CoA ligase (ADP-forming)

Comments: The enzyme is a component of EC 2.3.3.8 ATP citrate synthase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 856428-87-0

References:

1. Lill, U., Schreil, A. and Eggerer, H. Isolation of enzymically active fragments formed by limited proteolysis of ATP citrate lyase. Eur. J. Biochem. 125 (1982) 645-650. [PMID: 6749502]

2. Aoshima, M., Ishii, M. and Igarashi, Y. A novel enzyme, citryl-CoA synthetase, catalysing the first step of the citrate cleavage reaction in Hydrogenobacter thermophilus TK-6. Mol. Microbiol. 52, (2004) 751-761. [PMID: 15101981]

[EC 6.2.1.18 created 1986]

EC 6.2.1.19

Accepted name: long-chain-fatty-acid—protein ligase

Reaction: ATP + a long-chain fatty acid + [protein]-L-cysteine = AMP + diphosphate + a [protein]-S-(long-chain-acyl)-L-cysteine

Other name(s): luxE (gene name); acyl-protein synthetase; long-chain-fatty-acid—luciferin-component ligase

Systematic name: long-chain-fatty-acid:protein ligase (AMP-forming)

Comments: Together with a transferase component (EC 3.1.2.2/EC 3.1.2.14) and a reductase component (EC 1.2.1.50), this enzyme forms a multienzyme fatty acid reductase complex that produces the long-chain aldehyde substrate of the bacterial luciferase enzyme (EC 1.14.14.3). The enzyme activates free long-chain fatty acids, generated by the action of the transferase component, forming a fatty acyl-AMP intermediate, followed by the transfer of the acyl group to an internal L-cysteine residue. It then transfers the acyl group to EC 1.2.1.50, long-chain acyl-protein thioester reductase.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 82657-98-5

References:

1. Riendeau, D., Rodrigues, A. and Meighen, E. Resolution of the fatty acid reductase from Photobacterium phosphoreum into acyl protein synthetase and acyl-CoA reductase activities. Evidence for an enzyme complex. J. Biol. Chem. 257 (1982) 6908-6915. [PMID: 7085612]

2. Rodriguez, A. and Meighen, E. Fatty acyl-AMP as an intermediate in fatty acid reduction to aldehyde in luminescent bacteria. J. Biol. Chem. 260 (1985) 771-774. [PMID: 3968067]

3. Wall, L. and Meighen, E.A. Subunit structure of the fatty-acid reductase complex from Photobacterium phosphoreum. Biochemistry 25 (1986) 4315-4321.

4. Soly, R.R. and Meighen, E.A. Identification of the acyl transfer site of fatty acyl-protein synthetase from bioluminescent bacteria. J. Mol. Biol. 219 (1991) 69-77. [PMID: 2023262]

5. Lin, J.W., Chao, Y.F. and Weng, S.F. Nucleotide sequence and functional analysis of the luxE gene encoding acyl-protein synthetase of the lux operon from Photobacterium leiognathi. Biochem. Biophys. Res. Commun. 228 (1996) 764-773. [PMID: 8941351]

[EC 6.2.1.19 created 1986, modified 2011, modified 2016]

EC 6.2.1.20

Accepted name: long-chain-fatty-acid—[acyl-carrier-protein] ligase

Reaction: ATP + a long-chain fatty acid + an [acyl-carrier protein] = AMP + diphosphate + a long-chain acyl-[acyl-carrier protein]

Other name(s): acyl-[acyl-carrier-protein] synthetase (ambiguous); acyl-ACP synthetase (ambiguous); stearoyl-ACP synthetase; acyl-acyl carrier protein synthetase (ambiguous); long-chain-fatty-acid:[acyl-carrier-protein] ligase (AMP-forming)

Systematic name: long-chain-fatty-acid:[acyl-carrier protein] ligase (AMP-forming)

Comments: The enzyme ligates long chain fatty acids (with aliphatic chain of 13-22 carbons) to an acyl-carrier protein. Not identical with EC 6.2.1.3 long-chain-fatty-acid—CoA ligase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 77322-37-3

References:

1. Ray, T.K. and Cronan, J.E., Jr. Activation of long chain fatty acids with acyl carrier protein: demonstration of a new enzyme, acyl-acyl carrier protein synthetase, in Escherichia coli. Proc. Natl. Acad. Sci. USA 73 (1976) 4374-4378. [PMID: 794875]

2. Kaczmarzyk, D. and Fulda, M. Fatty acid activation in cyanobacteria mediated by acyl-acyl carrier protein synthetase enables fatty acid recycling. Plant Physiol. 152 (2010) 1598-1610. [PMID: 20061450]

[EC 6.2.1.20 created 1986]

[EC 6.2.1.21 Deleted entry: phenylacetate-CoA ligase. Activity covered by EC 6.2.1.30, phenylacetate—CoA ligase (EC 6.2.1.21 created 1986, deleted 2001)]

EC 6.2.1.22

Accepted name: [citrate (pro-3S)-lyase] ligase

Reaction: ATP + acetate + [citrate (pro-3S)-lyase](thiol form) = AMP + diphosphate + [citrate (pro-3S)-lyase](acetyl form)

Glossary
citrate = 2-hydroxypropane-1,2,3-tricarboxylate

Other name(s): citrate lyase ligase; citrate lyase synthetase; acetate: SH-[acyl-carrier-protein] enzyme ligase (AMP); acetate:HS-citrate lyase ligase; acetate:citrate-(pro-3S)-lyase(thiol-form) ligase (AMP-forming)

Systematic name: acetate:[citrate-(pro-3S)-lyase](thiol-form) ligase (AMP-forming)

Comments: Both this enzyme and EC 2.3.1.49, deacetyl-[citrate-(pro-3S)-lyase] S-acetyltransferase, acetylate and activate EC 4.1.3.6, citrate (pro-3S)-lyase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 52660-22-7

References:

1. Antranikian, G. and Gottschalk, G. Copurification of citrate lyase and citrate lyase ligase from Rhodopseudomonas gelatinosa and subsequent separation of the two enzymes. Eur. J. Biochem. 126 (1982) 43-47. [PMID: 7128585]

2. Antranikian, G., Herzberg, C. and Gottschalk, G. Covalent modification of citrate lyase ligase from Clostridium sphenoides by phosphorylation/dephosphorylation. Eur. J. Biochem. 153 (1985) 413-420. [PMID: 3935436]

3. Quentmeier, A. and Antranikian, G. Characterization of citrate lyase from Clostridium sporosphaeroides. Arch. Microbiol. 141 (1985) 85-90. [PMID: 3994485]

4. Schmellenkamp, H. and Eggerer, H. Mechanism of enzymic acetylation of des-acetyl citrate lyase. Proc. Natl. Acad. Sci. USA 71 (1974) 1987-1991. [PMID: 4365579]

[EC 6.2.1.22 created 1989]

EC 6.2.1.23

Accepted name: dicarboxylate—CoA ligase

Reaction: ATP + an α,ω-dicarboxylate + CoA = AMP + diphosphate + an ω-carboxyacyl-CoA

Other name(s): carboxylyl-CoA synthetase; dicarboxylyl-CoA synthetase

Systematic name: ω-dicarboxylate:CoA ligase (AMP-forming)

Comments: Acts on dicarboxylic acids of chain length C5 to C16; the best substrate is dodecanedioic acid.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 99332-77-1

References:

1. Vamecq, J., de Hoffmann, E. and van Hoof, F. The microsomal dicarboxylyl-CoA synthetase. Biochem. J. 230 (1985) 683-693. [PMID: 4062873]

[EC 6.2.1.23 created 1989, modified 2011]

EC 6.2.1.24

Accepted name: phytanate—CoA ligase

Reaction: ATP + phytanate + CoA = AMP + diphosphate + phytanoyl-CoA

Other name(s): phytanoyl-CoA ligase

Systematic name: phytanate:CoA ligase (AMP-forming)

Comments: Not identical with EC 6.2.1.20 long-chain-fatty-acid—[acyl-carrier-protein] ligase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 105238-50-4

References:

1. Muralidharan, F.N. and Muralidharan, V.B. Phytanoyl-CoA ligase activity in rat liver. Biochem. Int. 13 (1986) 123-130. [PMID: 3753503]

[EC 6.2.1.24 created 1989]

EC 6.2.1.25

Accepted name: benzoate—CoA ligase

Reaction: ATP + benzoate + CoA = AMP + diphosphate + benzoyl-CoA

For diagram of reaction click here.

Other name(s): benzoate—coenzyme A ligase; benzoyl-coenzyme A synthetase; benzoyl CoA synthetase (AMP forming)

Systematic name: benzoate:CoA ligase (AMP-forming)

Comments: Also acts on 2-, 3- and 4-fluorobenzoate, but only very slowly on the corresponding chlorobenzoates.

Links to other databases: BRENDA, EXPASY, KEGG, UM-BBD, Metacyc, UM-BBD, CAS registry number: 95329-17-2

References:

1. Hutber, G.N. and Ribbons, D.W. Involvement of coenzyme-A esters in the metabolism of benzoate and cyclohexanecarboxylate by Rhodopseudomonas palustris. J. Gen. Microbiol. 129 (1983) 2413-2420.

2. Schennen, U., Braun, K. and Knackmuss, H.-J. Anaerobic degradation of 2-fluorobenzoate by benzoate-degrading, denitrifying bacteria. J. Bacteriol. 161 (1985) 321-325. [PMID: 2857161]

[EC 6.2.1.25 created 1989]

EC 6.2.1.26

Accepted name: o-succinylbenzoate—CoA ligase

Reaction: ATP + 2-succinylbenzoate + CoA = AMP + diphosphate + 4-(2-carboxyphenyl)-4-oxobutanoyl-CoA

For diagram click here.

Glossary: 2-succinylbenzoate = o-succinylbenzoate = 4-(2-carboxyphenyl)-4-oxobutanoate
2-succinylbenzoyl-CoA = o-succinylbenzoyl-CoA = 4-(2-carboxyphenyl)-4-oxobutanoyl-CoA

Other name(s): 2-succinylbenzoyl-coenzyme A synthetase; 2-succinylbenzoate:CoA ligase (AMP-forming)

Systematic name: 2-succinylbenzoate:CoA ligase (AMP-forming)

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 72506-70-8

References:

1. Heide, L., Arendt, S. and Leistner, E. Enzymatic-synthesis, characterization, and metabolism of the coenzyme-A ester of o-succinylbenzoic acid, an intermediate in menaquinone (vitamin K2) biosynthesis. J. Biol. Chem. 257 (1982) 7396-7400. [PMID: 7045104]

2. Kolkmann, R. and Leistner, E. 4-(2'-Carboxyphenyl)-4-oxobutyryl coenzyme-A ester, an intermediate in vitamin K2 (menaquinone) biosynthesis. Z. Naturforsch. C: Sci. 42 (1987) 1207-1214. [PMID: 2966501]

3. Meganathan, R. and Bentley, R. Menaquinone (vitamin K2) biosynthesis: conversion of o-succinylbenzoic acid to 1,4-dihydroxy-2-naphthoic acid by Mycobacterium phlei enzymes. J. Bacteriol. 140 (1979) 92-98. [PMID: 500558]

[EC 6.2.1.26 created 1992]

EC 6.2.1.27

Accepted name: 4-hydroxybenzoate—CoA ligase

Reaction: ATP + 4-hydroxybenzoate + CoA = AMP + diphosphate + 4-hydroxybenzoyl-CoA

Other name(s): 4-hydroxybenzoate-CoA synthetase; 4-hydroxybenzoate—coenzyme A ligase (AMP-forming); 4-hydroxybenzoyl coenzyme A synthetase; 4-hydroxybenzoyl-CoA ligase

Systematic name: 4-hydroxybenzoate:CoA ligase (AMP-forming)

Links to other databases: BRENDA, EXPASY, KEGG, UM-BBD, Metacyc, UM-BBD, CAS registry number: 119699-80-8

References:

1. Merkel, S.M., Eberhard, A.E., Gibson, J. and Harwood, C.S. Involvement of coenzyme A thioesters in anaerobic metabolism of 4-hydroxybenzoate by Rhodopseudomonas palustris. J. Bacteriol. 171 (1989) 1-7. [PMID: 2914844]

[EC 6.2.1.27 created 1992]

EC 6.2.1.28

Accepted name: 3α,7α-dihydroxy-5β-cholestanate—CoA ligase

Reaction: ATP + (25R)-3α,7α-dihydroxy-5β-cholestan-26-oate + CoA = AMP + diphosphate + (25R)-3α,7α-dihydroxy-5β-cholestanoyl-CoA

For diagram click here.

Other name(s): 3α,7α-dihydroxy-5β-cholestanoyl coenzyme A synthetase; DHCA-CoA ligase; 3α,7α-dihydroxy-5β-cholestanate:CoA ligase (AMP-forming)

Systematic name: (25R)-3α,7α-dihydroxy-5β-cholestan-26-oate:CoA ligase (AMP-forming)

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 118732-03-9

References:

1. Prydz, K., Kase, B.F., Bjoerkhem, I. and Pedersen, J.I. Subcellular localization of 3α,7α-dihydroxy- and 3α,7α,12α-trihydroxy-5β-cholestanoyl-coenzyme A ligase(s) in rat liver. J. Lipid Res. 29 (1988) 997-1004. [PMID: 3183523]

[EC 6.2.1.28 created 1992]

[EC 6.2.1.29 Deleted entry: 3α,7α,12α-trihydroxy-5β-cholestanate—CoA ligase. The enzyme is identical to EC 6.2.1.7, cholate—CoA ligase (EC 6.2.1.29 created 1992, deleted 2005)]

EC 6.2.1.30

Accepted name: phenylacetate—CoA ligase

Reaction: ATP + phenylacetate + CoA = AMP + diphosphate + phenylacetyl-CoA

For diagram of reaction click here.

Other name(s): phenacyl coenzyme A synthetase; phenylacetyl-CoA ligase; PA-CoA ligase; phenylacetyl-CoA ligase (AMP-forming)

Systematic name: phenylacetate:CoA ligase (AMP-forming)

Comments: Also acts, more slowly, on acetate, propanoate and butanoate, but not on hydroxy derivatives of phenylacetate and related compounds.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number: 57219-71-3

References:

1. Martinez-Blanco, H., Reglero, A., Rodriguez-Asparicio, L.B. and Luengo, J.M. Purification and biochemical characterization of phenylacetyl-CoA ligase from Pseudomonas putida. A specific enzyme for the catabolism of phenylacetic acid. J. Biol. Chem. 265 (1990) 7084-7090. [PMID: 2324116]

[EC 6.2.1.30 created 1992 (EC 6.2.1.21 created 1986, incorporated 2001)]

EC 6.2.1.31

Accepted name: 2-furoate—CoA ligase

Reaction: ATP + 2-furoate + CoA = AMP + diphosphate + 2-furoyl-CoA

For diagram of reaction click here.

Glossary
anthranilate = 2-aminobenzoate

Other name(s): 2-furoyl coenzyme A synthetase

Systematic name: 2-furoate:CoA ligase (AMP-forming)

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number: 122320-08-5

References:

1. Koenig, K. and Andreesen, J.R. Molybdenum involvement in aerobic degradation of 2-furoic acid by Pseudomonas putida FU1. Appl. Environ. Microbiol. 55 (1989) 1829-1834.

[EC 6.2.1.31 created 1992]

EC 6.2.1.32

Accepted name: anthranilate—CoA ligase

Reaction: ATP + anthranilate + CoA = AMP + diphosphate + anthraniloyl-CoA

For diagram click here.

Glossary: anthraniloyl-CoA = 2-aminobenzoyl-CoA

Other name(s): anthraniloyl coenzyme A synthetase; 2-aminobenzoate—CoA ligase; 2-aminobenzoate—coenzyme A ligase; 2-aminobenzoate coenzyme A ligase

Systematic name: anthranilate:CoA ligase (AMP-forming)

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number: 112692-58-7

References:

1. Altenschmidt, U., Eckerskorn, C. and Fuchs, G. Evidence that enzymes of a novel aerobic 2-amino-benzoate metabolism in denitrifying Pseudomonas are coded on a small plasmid. Eur. J. Biochem. 194 (1990) 647-653. [PMID: 2176602]

[EC 6.2.1.32 created 1992]

EC 6.2.1.33

Accepted name: 4-chlorobenzoate—CoA ligase

Reaction: 4-chlorobenzoate + CoA + ATP = 4-chlorobenzoyl-CoA + AMP + diphosphate

Systematic name: 4-chlorobenzoate:CoA ligase

Comments: requires Mg2+. This enzyme is part of the bacterial 2,4-dichlorobenzoate degradation pathway.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number: 141583-20-2

References:

1. Dunaway-Mariano, D., Babbitt, P.C. On the origins and functions of the enzymes of the 4-chlorobenzoate to 4-hydroxybenzoate converting pathway. Biodegradation 5 (1994) 259-276. [PMID: 7765837]

2. Loffler, F., Muller, R., Lingens, F. Purification and properties of 4-halobenzoate-coenzyme A ligase from Pseudomonas sp. CBS3. Biol. Chem. Hoppe-Seyler 373 (1992) 1001-1007. [PMID: 1418673]

3. Chang, K.H., Liang, P.H., Beck, W., Scholten, J.D., Dunaway-Mariano, D. Isolation and characterization of the three polypeptide components of 4-chlorobenzoate dehalogenase from Pseudomonas sp. strain CBS-3. Biochemistry 31 (1992) 5605-5610. [PMID: 1610806]

[EC 6.2.1.33 created 1999]

EC 6.2.1.34

Accepted name: trans-feruloyl-CoA synthase

Reaction: ferulic acid + CoA + ATP = feruloyl-CoA + products of ATP breakdown

For diagram of reaction click here.

Other name(s): trans-feruloyl-CoA synthetase; trans-ferulate:CoASH ligase (ATP-hydrolysing); ferulate:CoASH ligase (ATP-hydrolysing)

Systematic name: ferulate:CoA ligase (ATP-hydrolysing)

Comments: Requires Mg2+. It has not yet been established whether AMP + diphosphate or ADP + phosphate are formed in this reaction.

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

References:

1. Narbad, A. and Gasson, M.J. Metabolism of ferulic acid via vanillin using a novel CoA-dependent pathway in a newly-isolated strain of Pseudomonas fluorescens. Microbiology 144 (1998) 1397-1405. [PMID: 9611814]

2. Pometto, A.L. and Crawford, D.L. Whole-cell bioconversion of vanillin to vanillic acid by Streptomyces viridosporus. Appl. Environ. Microbiol. 45 (1983) 1582-1585. [PMID: 6870241]

[EC 6.2.1.34 created 2000]

EC 6.2.1.35

Accepted name: ACP-SH:acetate ligase

Reaction: ATP + acetate + an [acyl-carrier protein] = AMP + diphosphate + an acetyl-[acyl-carrier protein]

For diagram of the reaction click here

Other name(s): HS-acyl-carrier protein:acetate ligase; [acyl-carrier protein]:acetate ligase; MadH

Systematic name: acetate:[acyl-carrier-protein] ligase (AMP-forming)

Comments: This enzyme, from the anaerobic bacterium Malonomonas rubra, is a component of the multienzyme complex EC 4.1.1.89, biotin-dependent malonate decarboxylase. The enzyme uses the energy from hydrolysis of ATP to convert the thiol group of the acyl-carrier-protein-bound 2'-(5-phosphoribosyl)-3'-dephospho-CoA prosthetic group into its acetyl thioester [2].

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

References:

1. Hilbi, H., Dehning, I., Schink, B. and Dimroth, P. Malonate decarboxylase of Malonomonas rubra, a novel type of biotin-containing acetyl enzyme. Eur. J. Biochem. 207 (1992) 117-123. [PMID: 1628643]

2. Berg, M., Hilbi, H. and Dimroth, P. The acyl carrier protein of malonate decarboxylase of Malonomonas rubra contains 2'-(5"-phosphoribosyl)-3'-dephosphocoenzyme A as a prosthetic group. Biochemistry 35 (1996) 4689-4696. [PMID: 8664258]

3. Berg, M., Hilbi, H. and Dimroth, P. Sequence of a gene cluster from Malonomonas rubra encoding components of the malonate decarboxylase Na+ pump and evidence for their function. Eur. J. Biochem. 245 (1997) 103-115. [PMID: 9128730]

4. Dimroth, P. and Hilbi, H. Enzymic and genetic basis for bacterial growth on malonate. Mol. Microbiol. 25 (1997) 3-10. [PMID: 11902724]

[EC 6.2.1.35 created 2008]

EC 6.2.1.36

Accepted name: 3-hydroxypropionyl-CoA synthase

Reaction: 3-hydroxypropanoate + ATP + CoA = 3-hydroxypropanoyl-CoA + AMP + diphosphate

For diagram of reaction click here (another example).

Glossary: 3-hydroxypropanoyl-CoA = 3-hydroxypropionyl-CoA

Other name(s): 3-hydroxypropionyl-CoA synthetase (AMP-forming); 3-hydroxypropionate—CoA ligase; hydroxypropionate:CoA ligase (AMP-forming)

Systematic name: hydroxypropanoate:CoA ligase (AMP-forming)

Comments: Catalyses a step in the 3-hydroxypropanoate/4-hydroxybutanoate cycle, an autotrophic CO2 fixation pathway found in some thermoacidophilic archaea [1,2]. The enzymes from Metallosphaera sedula and Sulfolobus tokodaii can also use propionate, acrylate, acetate, and butanoate as substrates [2], and are thus different from EC 6.2.1.17 (propionate—CoA ligase), which does not accept acetate or butanoate.

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

References:

1. Berg, I.A., Kockelkorn, D., Buckel, W. and Fuchs, G. A 3-hydroxypropionate/4-hydroxybutyrate autotrophic carbon dioxide assimilation pathway in Archaea. Science 318 (2007) 1782-1786. [PMID: 18079405]

2. Alber, B.E., Kung, J.W. and Fuchs, G. 3-Hydroxypropionyl-coenzyme A synthetase from Metallosphaera sedula, an enzyme involved in autotrophic CO2 fixation. J. Bacteriol. 190 (2008) 1383-1389. [PMID: 18165310]

[EC 6.2.1.36 created 2009]

EC 6.2.1.37

Accepted name: 3-hydroxybenzoate—CoA ligase

Reaction: ATP + 3-hydroxybenzoate + CoA = AMP + diphosphate + 3-hydroxybenzoyl-CoA

Other name(s): 3-hydroxybenzoyl-CoA synthetase; 3-hydroxybenzoate—coenzyme A ligase (AMP-forming); 3-hydroxybenzoyl coenzyme A synthetase; 3-hydroxybenzoyl-CoA ligase

Systematic name: 3-hydroxybenzoate:CoA ligase (AMP-forming)

Comments: The enzyme works equally well with 4-hydroxybenzoate but shows low activity towards benzoate, 4-aminobenzoate, 3-aminobenzoate, 3-fluorobenzoate, 4-fluorobenzoate, 3-chlorobenzoate, and 4-chlorobenzoate. There is no activity with 3,4-dihydroxybenzoate, 2,3-dihydroxybenzoate, and 2-hydroxybenzoate as substrates.

References:

1. Laempe, D., Jahn, M., Breese, K., Schägger, H. and Fuchs, G. Anaerobic metabolism of 3-hydroxybenzoate by the denitrifying bacterium Thauera aromatica. J. Bacteriol. 183 (2001) 968-979. [PMID: 11208796]

[EC 6.2.1.37 created 2011]

EC 6.2.1.38

Accepted name: (2,2,3-trimethyl-5-oxocyclopent-3-enyl)acetyl-CoA synthase

Reaction: [(1R)-2,2,3-trimethyl-5-oxocyclopent-3-enyl]acetate + ATP + CoA = AMP + diphosphate + [(1R)-2,2,3-trimethyl-5-oxocyclopent-3-enyl]acetyl-CoA

For diagram of reaction click here.

Other name(s): 2-oxo-Δ3-4,5,5-trimethylcyclopentenylacetyl-CoA synthetase

Systematic name: [(1R)-2,2,3-trimethyl-5-oxocyclopent-3-enyl]acetate:CoA ligase (AMP-forming)

Comments: Isolated from Pseudomonas putida. Forms part of the pathway of camphor catabolism.

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

References:

1. Ougham, H.J., Taylor, D.G. and Trudgill, P.W. Camphor revisited: involvement of a unique monooxygenase in metabolism of 2-oxo-Δ3-4,5,5-trimethylcyclopentenylacetic acid by Pseudomonas putida. J. Bacteriol. 153 (1983) 140-152. [PMID: 6848481]

[EC 6.2.1.38 created 2012]

EC 6.2.1.39

Accepted name: [butirosin acyl-carrier protein]—L-glutamate ligase

Reaction: (1) ATP + L-glutamate + BtrI acyl-carrier protein = ADP + phosphate + L-glutamyl-[BtrI acyl-carrier protein]
(2) ATP + L-glutamate + 4-amino butanoyl-[BtrI acyl-carrier protein] = ADP + phosphate + 4-(L-γ-glutamylamino)butanoyl-[BtrI acyl-carrier protein]

Other name(s): [BtrI acyl-carrier protein]—L-glutamate ligase; BtrJ

Systematic name: [BtrI acyl-carrier protein]:L-glutamate ligase (ADP-forming)

Comments: Catalyses two steps in the biosynthesis of the side chain of the aminoglycoside antibiotics of the butirosin family. The enzyme adds one molecule of L-glutamate to a dedicated acyl-carrier protein, and following decarboxylation of the product by EC 4.1.1.95, L-glutamyl-[BtrI acyl-carrier protein] decarboxylase, adds a second L-glutamate molecule. Requires Mg2+ or Mn2+, and activity is enhanced in the presence of Mn2+.

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

References:

1. Li, Y., Llewellyn, N.M., Giri, R., Huang, F. and Spencer, J.B. Biosynthesis of the unique amino acid side chain of butirosin: possible protective-group chemistry in an acyl carrier protein-mediated pathway. Chem. Biol. 12 (2005) 665-675. [PMID: 15975512]

[EC 6.2.1.39 created 2012]

EC 6.2.1.40

Accepted name: 4-hydroxybutyrate—CoA ligase

Reaction: ATP + 4-hydroxybutanoate + CoA = AMP + diphosphate + 4-hydroxybutanoyl-CoA

For diagram of reaction click here.

Other name(s): 4-hydroxybutyrate-CoA synthetase; 4-hydroxybutyrate:CoA ligase (AMP formimg)

Systematic name: 4-hydroxybutanoate:CoA ligase (AMP-forming)

Comments: Isolated from the archaeon Metallosphaera sedula. Involved in the 3-hydroxypropanoate/4-hydroxybutanoate cycle.

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

References:

1. Ramos-Vera, W.H., Weiss, M., Strittmatter, E., Kockelkorn, D. and Fuchs, G. Identification of missing genes and enzymes for autotrophic carbon fixation in crenarchaeota. J. Bacteriol. 193 (2011) 1201-1211. [PMID: 21169482]

2. Hawkins, A.S., Han, Y., Bennett, R.K., Adams, M.W. and Kelly, R.M. Role of 4-hydroxybutyrate-CoA synthetase in the CO2 fixation cycle in thermoacidophilic archaea. J. Biol. Chem. 288 (2013) 4012-4022. [PMID: 23258541]

[EC 6.2.1.40 created 2014]

EC 6.2.1.41

Accepted name: 3-[(3aS,4S,7aS)-7a-methyl-1,5-dioxo-octahydro-1H-inden-4-yl]propanoate—CoA ligase

Reaction: ATP + 3-[(3aS,4S,7aS)-7a-methyl-1,5-dioxo-octahydro-1H-inden-4-yl]propanoate + CoA = AMP + diphosphate + 3-[(3aS,4S,7aS)-7a-methyl-1,5-dioxo-octahydro-1H-inden-4-yl]propanoyl-CoA

For diagram of reaction click here.

Glossary: 3-[(3aS,4S,7aS)-7a-methyl-1,5-dioxo-octahydro-1H-inden-4-yl]propanoate = HIP

Other name(s): fadD3 (gene name); HIP—CoA ligase

Systematic name: 3-[(3aS,4S,7aS)-7a-methyl-1,5-dioxo-octahydro-1H-inden-4-yl]propanoate:CoA ligase (AMP-forming)

Comments: The enzyme, characterized from actinobacterium Mycobacterium tuberculosis, catalyses a step in the degradation of cholesterol and cholate. The enzyme is very specific for its substrate, and requires that the side chain at C17 is completely removed.

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

References:

1. Horinouchi, M., Hayashi, T., Koshino, H. and Kudo, T. ORF18-disrupted mutant of Comamonas testosteroni TA441 accumulates significant amounts of 9,17-dioxo-1,2,3,4,10,19-hexanorandrostan-5-oic acid and its derivatives after incubation with steroids. J. Steroid Biochem. Mol. Biol. 101 (2006) 78-84. [PMID: 16891113]

2. Casabon, I., Crowe, A.M., Liu, J. and Eltis, L.D. FadD3 is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. Mol. Microbiol. 87 (2013) 269-283. [PMID: 23146019]

[EC 6.2.1.41 created 2014]

EC 6.2.1.42

Accepted name: 3-oxocholest-4-en-26-oate—CoA ligase

Reaction: ATP + (25S)-3-oxocholest-4-en-26-oate + CoA = AMP + diphosphate + (25S)-3-oxocholest-4-en-26-oyl-CoA

For diagram of reaction click here.

Other name(s): fadD19 (gene name)

Systematic name: (25S)-3-oxocholest-4-en-26-oate:CoA ligase (AMP-forming)

Comments: The enzyme, characterized from actinobacterium Mycobacterium tuberculosis, catalyses a step in the degradation of cholesterol. It is responsible for the activation of the C8 side chain. 3β-hydroxycholest-5-en-26-oate can also be used as substrate.

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

References:

1. Wilbrink, M.H., Petrusma, M., Dijkhuizen, L. and van der Geize, R. FadD19 of Rhodococcus rhodochrous-DSM43269, a steroid-coenzyme A ligase essential for degradation of C-24 branched sterol side chains. Appl. Environ. Microbiol. 77 (2011) 4455-4464. [PMID: 21602385]

2. Casabon, I., Swain, K., Crowe, A.M., Eltis, L.D. and Mohn, W.W. Actinobacterial acyl coenzyme a synthetases involved in steroid side-chain catabolism. J. Bacteriol. 196 (2014) 579-587. [PMID: 24244004]

[EC 6.2.1.42 created 2014]

EC 6.2.1.43

Accepted name: 2-hydroxy-7-methoxy-5-methyl-1-naphthoate—CoA ligase

Reaction: ATP + 2-hydroxy-7-methoxy-5-methyl-1-naphthoate + CoA = AMP + diphosphate + 2-hydroxy-7-methoxy-5-methyl-1-naphthoyl-CoA

For diagram of reaction click here.

Other name(s): NcsB2

Systematic name: 2-hydroxy-7-methoxy-5-methyl-1-naphthoate:CoA ligase

Comments: The enzyme from the bacterium Streptomyces carzinostaticus is involved in the attachment of the 2-hydroxy-7-methoxy-5-methyl-1-naphthoate moiety of the antibiotic neocarzinostatin. In vitro the enzyme also catalyses the activation of other 1-naphthoic acid analogues, e.g. 2-hydroxy-5-methyl-1-naphthoate or 2,7-dihydroxy-5-methyl-1-naphthoate.

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

References:

1. Cooke, H.A., Zhang, J., Griffin, M.A., Nonaka, K., Van Lanen, S.G., Shen, B. and Bruner, S.D. Characterization of NcsB2 as a promiscuous naphthoic acid/coenzyme A ligase integral to the biosynthesis of the enediyne antitumor antibiotic neocarzinostatin. J. Am. Chem. Soc. 129 (2007) 7728-7729. [PMID: 17539640]

[EC 6.2.1.43 created 2014]

EC 6.2.1.44

Accepted name: 3-(methylthio)propionyl—CoA ligase

Reaction: ATP + 3-(methylthio)propanoate + CoA = AMP + diphosphate + 3-(methylthio)propanoyl-CoA

For diagram of reaction click here.

Other name(s): DmdB; MMPA-CoA ligase; methylmercaptopropionate-coenzyme A ligase; 3-methylmercaptopropionyl-CoA ligase

Systematic name: 3-(methylthio)propanoate:CoA ligase (AMP-forming)

Comments: The enzyme is part of a dimethylsulfoniopropanoate demethylation pathway in the marine bacteria Ruegeria pomeroyi and Pelagibacter ubique. It also occurs in some nonmarine bacteria capable of metabolizing dimethylsulfoniopropionate (e.g. Burkholderia thailandensis, Pseudomonas aeruginosa, and Silicibacter lacuscaerulensis). It requires Mg2+ [2].

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

References:

1. Reisch, C.R., Stoudemayer, M.J., Varaljay, V.A., Amster, I.J., Moran, M.A. and Whitman, W.B. Novel pathway for assimilation of dimethylsulphoniopropionate widespread in marine bacteria. Nature 473 (2011) 208-211. [PMID: 21562561]

2. Bullock, H.A., Reisch, C.R., Burns, A.S., Moran, M.A. and Whitman, W.B. Regulatory and functional diversity of methylmercaptopropionate coenzyme A ligases from the dimethylsulfoniopropionate demethylation pathway in Ruegeria pomeroyi DSS-3 and other proteobacteria. J. Bacteriol. 196 (2014) 1275-1285. [PMID: 24443527]

[EC 6.2.1.44 created 2014]

EC 6.2.1.45

Accepted name: E1 ubiquitin-activating enzyme

Reaction: ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine = AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine

Other name(s): ubiquitin activating enzyme; E1; ubiquitin-activating enzyme E1

Systematic name: ubiquitin:[E1 ubiquitin-activating enzyme] ligase (AMP-forming)

Comments: Catalyses the ATP-dependent activation of ubiquitin through the formation of a thioester bond between the C-terminal glycine of ubiquitin and the sulfhydryl side group of a cysteine residue in the E1 protein. The two-step reaction consists of the ATP-dependent formation of an E1-ubiquitin adenylate intermediate in which the C-terminal glycine of ubiquitin is bound to AMP via an acyl-phosphate linkage, then followed by the conversion to an E1-ubiquitin thioester bond via the cysteine residue on E1 in the second step.

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

References:

1. Haas, A.L., Warms, J.V., Hershko, A. and Rose, I.A. Ubiquitin-activating enzyme. Mechanism and role in protein-ubiquitin conjugation. J. Biol. Chem. 257 (1982) 2543-2548. [PMID: 6277905]

2. Huzil, J.T., Pannu, R., Ptak, C., Garen, G. and Ellison, M.J. Direct catalysis of lysine 48-linked polyubiquitin chains by the ubiquitin-activating enzyme. J. Biol. Chem. 282 (2007) 37454-37460. [PMID: 17951259]

3. Zheng, M., Liu, J., Yang, Z., Gu, X., Li, F., Lou, T., Ji, C. and Mao, Y. Expression, purification and characterization of human ubiquitin-activating enzyme, UBE1. Mol. Biol. Rep. 37 (2010) 1413-1419. [PMID: 19343538]

4. Carvalho, A.F., Pinto, M.P., Grou, C.P., Vitorino, R., Domingues, P., Yamao, F., Sa-Miranda, C. and Azevedo, J.E. High-yield expression in Escherichia coli and purification of mouse ubiquitin-activating enzyme E1. Mol Biotechnol 51 (2012) 254-261. [PMID: 22012022]

[EC 6.2.1.45 created 2015]

EC 6.2.1.46

Accepted name: L-allo-isoleucine:holo-[CmaA peptidyl-carrier protein] ligase

Reaction: ATP + L-allo-isoleucine + holo-[CmaA peptidyl-carrier protein] = AMP + diphosphate + L-allo-isoleucyl-S-[CmaA peptidyl-carrier protein]

Other name(s): CmaA

Systematic name: L-allo-isoleucine:holo-[CmaA peptidyl-carrier protein] ligase (AMP-forming)

Comments: This two-domain protein from the bacterium Pseudomonas syringae contains an adenylation domain (A domain) and a thiolation domain (T domain). It catalyses the adenylation of L-allo-isoleucine and its attachment to the T domain. The enzyme is involved in the biosynthesis of the toxin coronatine, which mimics the plant hormone jasmonic acid isoleucine. Coronatine promotes opening of the plant stomata allowing bacterial invasion, which is followed by bacterial growth in the apoplast, systemic susceptibility, and disease.

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

References:

1. Couch, R., O'Connor, S.E., Seidle, H., Walsh, C.T. and Parry, R. Characterization of CmaA, an adenylation-thiolation didomain enzyme involved in the biosynthesis of coronatine. J. Bacteriol. 186 (2004) 35-42. [PMID: 14679222]

[EC 6.2.1.46 created 2015]

EC 6.2.1.47

Accepted name: medium-chain-fatty-acid—[acyl-carrier-protein] ligase

Reaction: ATP + a medium-chain fatty acid + a holo-[acyl-carrier protein] = AMP + diphosphate + a medium-chain acyl-[acyl-carrier protein]

Other name(s): jamA (gene name)

Systematic name: medium-chain-fatty-acid:[acyl-carrier protein] ligase (AMP-forming)

Comments: The enzyme ligates medium chain fatty acids (with aliphatic chain of 6-12 carbons) to an acyl-carrier protein.

References:

1. Edwards, D.J., Marquez, B.L., Nogle, L.M., McPhail, K., Goeger, D.E., Roberts, M.A. and Gerwick, W.H. Structure and biosynthesis of the jamaicamides, new mixed polyketide-peptide neurotoxins from the marine cyanobacterium Lyngbya majuscula. Chem. Biol. 11 (2004) 817-833. [PMID: 15217615]

2. Zhu, X., Liu, J. and Zhang, W. De novo biosynthesis of terminal alkyne-labeled natural products. Nat. Chem. Biol. 11 (2015) 115-120. [PMID: 25531891]

[EC 6.2.1.47 created 2016]


Continued with EC 6.3.1 to EC 6.3.2
Return to EC 6 home page
Return to Enzymes home page
Return to IUBMB Biochemical Nomenclature home page