Continued from EC 6.1.1
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.
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]
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]
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.
Accepted name: succinate—CoA ligase (ADP-forming)
Reaction: ATP + succinate + CoA = ADP + phosphate + succinyl-CoA
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.
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.
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]
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]
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.
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]
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.
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]
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]
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.
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]
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]
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]
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]
Accepted name: long-chain-fatty-acid—luciferin-component ligase
Reaction: ATP + a long-chain fatty acid + protein = AMP + diphosphate + an acyl-protein thioester
Other name(s): acyl-protein synthetase
Systematic name: long-chain-fatty-acid:protein ligase (AMP-forming)
Comments: Together with EC 1.2.1.50 long-chain-fatty-acyl-CoA reductase, enzyme forms a fatty acid reductase system that produces the substrate of EC 1.14.14.3 alkanal monooxygenase (FMN-linked), thus being a component of the bacterial luciferase system.
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. Wall, L. and Meighen, E.A. Subunit structure of the fatty-acid reductase complex from Photobacterium phosphoreum. Biochemistry 25 (1986) 4315-4321.
Accepted name: long-chain-fatty-acid—[acyl-carrier-protein] ligase
Reaction: ATP + an acid + an [acyl-carrier protein] = AMP + diphosphate + an acyl-[acyl-carrier protein]
Other name(s): acyl-[acyl-carrier-protein] synthetase; acyl-[acyl carrier protein] synthetase; acyl-ACP synthetase; acyl-[acyl-carrier-protein]synthetase; stearoyl-ACP synthetase; acyl-acyl carrier protein synthetase
Systematic name: long-chain-fatty-acid:[acyl-carrier protein] ligase (AMP-forming)
Comments: 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]
[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)]
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]
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]
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]
Accepted name: benzoate—CoA ligase
Reaction: ATP + benzoate + CoA = AMP + diphosphate + benzoyl-CoA
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]
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]
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]
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 6.2.1.29 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)]
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]
Accepted name: 2-furoate—CoA ligase
Reaction: ATP + 2-furoate + CoA = AMP + diphosphate + 2-furoyl-CoA
For diagram of reaction click here.
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.
Accepted name: anthranilate—CoA ligase
Reaction: ATP + anthranilate + CoA = AMP + diphosphate + anthranilyl-CoA
For diagram click here.
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]
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]
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]
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]
Accepted name: 3-hydroxypropionyl-CoA synthase
Reaction: 3-hydroxypropionate + ATP + CoA = 3-hydroxypropionyl-CoA + AMP + diphosphate
Glossary: 3-hydroxypropionyl-CoA = 3-hydroxypropanoyl-CoA
Other name(s): 3-hydroxypropionyl-CoA synthetase (AMP-forming); 3-hydroxypropionate—CoA ligase
Systematic name: hydroxypropionate:CoA ligase (AMP-forming)
Comments: Catalyses a step in the 3-hydroxypropionate/4-hydroxybutyrate 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]
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]
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]
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]