EC |
1.3.8.1 |
Accepted name: |
short-chain acyl-CoA dehydrogenase |
Reaction: |
a short-chain acyl-CoA + electron-transfer flavoprotein = a short-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein |
Glossary: |
a short-chain acyl-CoA = an acyl-CoA thioester where the acyl chain contains less than 6 carbon atoms. |
Other name(s): |
butyryl-CoA dehydrogenase; butanoyl-CoA dehydrogenase; butyryl dehydrogenase; unsaturated acyl-CoA reductase; ethylene reductase; enoyl-coenzyme A reductase; unsaturated acyl coenzyme A reductase; butyryl coenzyme A dehydrogenase; short-chain acyl CoA dehydrogenase; short-chain acyl-coenzyme A dehydrogenase; 3-hydroxyacyl CoA reductase; butanoyl-CoA:(acceptor) 2,3-oxidoreductase; ACADS (gene name). |
Systematic name: |
short-chain acyl-CoA:electron-transfer flavoprotein 2,3-oxidoreductase |
Comments: |
Contains a tightly-bound FAD cofactor. One of several enzymes that catalyse the first step in fatty acids β-oxidation. The enzyme catalyses the oxidation of saturated short-chain acyl-CoA thioesters to give a trans 2,3-unsaturated product by removal of the two pro-R-hydrogen atoms. The enzyme from beef liver accepts substrates with acyl chain lengths of 3 to 8 carbon atoms. The highest activity was reported with either butanoyl-CoA [2] or pentanoyl-CoA [4]. The enzyme from rat has only 10% activity with hexanoyl-CoA (compared to butanoyl-CoA) and no activity with octanoyl-CoA [6]. cf. EC 1.3.8.7, medium-chain acyl-CoA dehydrogenase, EC 1.3.8.8, long-chain acyl-CoA dehydrogenase, and EC 1.3.8.9, very-long-chain acyl-CoA dehydrogenase. |
Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9027-88-7 |
References: |
1. |
Mahler, H.R. Studies on the fatty acid oxidizing system of animal tissue. IV. The prosthetic group of butyryl coenzyme A dehydrogenase. J. Biol. Chem. 206 (1954) 13–26. [PMID: 13130522] |
2. |
Green, D.E., Mii, S., Mahler, H.R. and Bock, R.M. Studies on the fatty acid oxidizing system of animal tissue. III. Butyryl coenzyme A dehydrogenase. J. Biol. Chem. 206 (1954) 1–12. [PMID: 13130521] |
3. |
Beinert, H. Acyl coenzyme A dehydrogenase. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 7, Academic Press, New York, 1963, pp. 447–466. |
4. |
Shaw, L. and Engel, P.C. The purification and properties of ox liver short-chain acyl-CoA dehydrogenase. Biochem. J. 218 (1984) 511–520. [PMID: 6712627] |
5. |
Thorpe, C. and Kim, J.J. Structure and mechanism of action of the acyl-CoA dehydrogenases. FASEB J. 9 (1995) 718–725. [PMID: 7601336] |
6. |
Ikeda, Y., Ikeda, K.O. and Tanaka, K. Purification and characterization of short-chain, medium-chain, and long-chain acyl-CoA dehydrogenases from rat liver mitochondria. Isolation of the holo- and apoenzymes and conversion of the apoenzyme to the holoenzyme. J. Biol. Chem. 260 (1985) 1311–1325. [PMID: 3968063] |
7. |
McMahon, B., Gallagher, M.E. and Mayhew, S.G. The protein coded by the PP2216 gene of Pseudomonas putida KT2440 is an acyl-CoA dehydrogenase that oxidises only short-chain aliphatic substrates. FEMS Microbiol. Lett. 250 (2005) 121–127. [DOI] [PMID: 16024185] |
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[EC 1.3.8.1 created 1961 as EC 1.3.2.1, transferred 1964 to EC 1.3.99.2, transferred 2011 to EC 1.3.8.1, modified 2012] |
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EC |
1.3.8.7 |
Accepted name: |
medium-chain acyl-CoA dehydrogenase |
Reaction: |
a medium-chain acyl-CoA + electron-transfer flavoprotein = a medium-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein |
Glossary: |
a medium-chain acyl-CoA = an acyl-CoA thioester where the acyl chain contains 6 to 12 carbon atoms. |
Other name(s): |
fatty acyl coenzyme A dehydrogenase (ambiguous); acyl coenzyme A dehydrogenase (ambiguous); acyl dehydrogenase (ambiguous); fatty-acyl-CoA dehydrogenase (ambiguous); acyl CoA dehydrogenase (ambiguous); general acyl CoA dehydrogenase (ambiguous); medium-chain acyl-coenzyme A dehydrogenase; acyl-CoA:(acceptor) 2,3-oxidoreductase (ambiguous); ACADM (gene name). |
Systematic name: |
medium-chain acyl-CoA:electron-transfer flavoprotein 2,3-oxidoreductase |
Comments: |
Contains a tightly-bound FAD cofactor. One of several enzymes that catalyse the first step in fatty acids β-oxidation. The enzyme from pig liver can accept substrates with acyl chain lengths of 4 to 16 carbon atoms, but is most active with C8 to C12 compounds [2]. The enzyme from rat does not accept C16 at all and is most active with C6-C8 compounds [4]. cf. EC 1.3.8.1, short-chain acyl-CoA dehydrogenase, EC 1.3.8.8, long-chain acyl-CoA dehydrogenase, and EC 1.3.8.9, very-long-chain acyl-CoA dehydrogenase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Crane, F.L., Hauge, J.G. and Beinert, H. Flavoproteins involved in the first oxidative step of the fatty acid cycle. Biochim. Biophys. Acta 17 (1955) 292–294. [DOI] [PMID: 13239683] |
2. |
Crane, F.L., Mii, S., Hauge, J.G., Green, D.E. and Beinert, H. On the mechanism of dehydrogenation of fatty acyl derivatives of coenzyme A. I. The general fatty acyl coenzyme A dehydrogenase. J. Biol. Chem. 218 (1956) 701–716. [PMID: 13295224] |
3. |
Beinert, H. Acyl coenzyme A dehydrogenase. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 7, Academic Press, New York, 1963, pp. 447–466. |
4. |
Ikeda, Y., Ikeda, K.O. and Tanaka, K. Purification and characterization of short-chain, medium-chain, and long-chain acyl-CoA dehydrogenases from rat liver mitochondria. Isolation of the holo- and apoenzymes and conversion of the apoenzyme to the holoenzyme. J. Biol. Chem. 260 (1985) 1311–1325. [PMID: 3968063] |
5. |
Thorpe, C. and Kim, J.J. Structure and mechanism of action of the acyl-CoA dehydrogenases. FASEB J. 9 (1995) 718–725. [PMID: 7601336] |
6. |
Kim, J.J., Wang, M. and Paschke, R. Crystal structures of medium-chain acyl-CoA dehydrogenase from pig liver mitochondria with and without substrate. Proc. Natl. Acad. Sci. USA 90 (1993) 7523–7527. [DOI] [PMID: 8356049] |
7. |
Peterson, K.L., Sergienko, E.E., Wu, Y., Kumar, N.R., Strauss, A.W., Oleson, A.E., Muhonen, W.W., Shabb, J.B. and Srivastava, D.K. Recombinant human liver medium-chain acyl-CoA dehydrogenase: purification, characterization, and the mechanism of interactions with functionally diverse C8-CoA molecules. Biochemistry 34 (1995) 14942–14953. [PMID: 7578106] |
8. |
Toogood, H.S., van Thiel, A., Basran, J., Sutcliffe, M.J., Scrutton, N.S. and Leys, D. Extensive domain motion and electron transfer in the human electron transferring flavoprotein.medium chain Acyl-CoA dehydrogenase complex. J. Biol. Chem. 279 (2004) 32904–32912. [DOI] [PMID: 15159392] |
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[EC 1.3.8.7 created 1961 as EC 1.3.2.2, transferred 1964 to EC 1.3.99.3, part transferred 2012 to EC 1.3.8.7] |
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EC |
1.3.8.8 |
Accepted name: |
long-chain acyl-CoA dehydrogenase |
Reaction: |
a long-chain acyl-CoA + electron-transfer flavoprotein = a long-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein |
Glossary: |
a long-chain acyl-CoA = an acyl-CoA thioester where the acyl chain contains 13 to 22 carbon atoms. |
Other name(s): |
palmitoyl-CoA dehydrogenase; palmitoyl-coenzyme A dehydrogenase; long-chain acyl-coenzyme A dehydrogenase; long-chain-acyl-CoA:(acceptor) 2,3-oxidoreductase; ACADL (gene name). |
Systematic name: |
long-chain acyl-CoA:electron-transfer flavoprotein 2,3-oxidoreductase |
Comments: |
Contains a tightly-bound FAD cofactor. One of several enzymes that catalyse the first step in fatty acids β-oxidation. The enzyme from pig liver can accept substrates with acyl chain lengths of 6 to at least 16 carbon atoms. The highest activity was found with C12, and the rates with C8 and C16 were 80 and 70%, respectively [2]. The enzyme from rat can accept substrates with C8-C22. It is most active with C14 and C16, and has no activity with C4, C6 or C24 [4]. cf. EC 1.3.8.1, short-chain acyl-CoA dehydrogenase, EC 1.3.8.8, medium-chain acyl-CoA dehydrogenase, and EC 1.3.8.9, very-long-chain acyl-CoA dehydrogenase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 59536-74-2 |
References: |
1. |
Crane, F.L., Hauge, J.G. and Beinert, H. Flavoproteins involved in the first oxidative step of the fatty acid cycle. Biochim. Biophys. Acta 17 (1955) 292–294. [DOI] [PMID: 13239683] |
2. |
Hauge, J.G., Crane, F.L. and Beinert, H. On the mechanism of dehydrogenation of fatty acyl derivatives of coenzyme A. III. Palmityl CoA dehydrogenase. J. Biol. Chem. 219 (1956) 727–733. [PMID: 13319294] |
3. |
Hall, C.L., Heijkenkjold, L., Bartfai, T., Ernster, L. and Kamin, H. Acyl coenzyme A dehydrogenases and electron-transferring flavoprotein from beef heart mitochondria. Arch. Biochem. Biophys. 177 (1976) 402–414. [DOI] [PMID: 1015826] |
4. |
Ikeda, Y., Ikeda, K.O. and Tanaka, K. Purification and characterization of short-chain, medium-chain, and long-chain acyl-CoA dehydrogenases from rat liver mitochondria. Isolation of the holo- and apoenzymes and conversion of the apoenzyme to the holoenzyme. J. Biol. Chem. 260 (1985) 1311–1325. [PMID: 3968063] |
5. |
Djordjevic, S., Dong, Y., Paschke, R., Frerman, F.E., Strauss, A.W. and Kim, J.J. Identification of the catalytic base in long chain acyl-CoA dehydrogenase. Biochemistry 33 (1994) 4258–4264. [PMID: 8155643] |
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[EC 1.3.8.8 created 1989 as EC 1.3.99.13, part transferred 2012 to EC 1.3.8.8] |
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EC |
1.3.8.9 |
Accepted name: |
very-long-chain acyl-CoA dehydrogenase |
Reaction: |
a very-long-chain acyl-CoA + electron-transfer flavoprotein = a very-long-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein |
Glossary: |
a very-long-chain acyl-CoA = an acyl-CoA thioester where the acyl chain contains 23 or more carbon atoms. |
Other name(s): |
ACADVL (gene name). |
Systematic name: |
very-long-chain acyl-CoA:electron-transfer flavoprotein 2,3-oxidoreductase |
Comments: |
Contains a tightly-bound FAD cofactor. One of several enzymes that catalyse the first step in fatty acids β-oxidation. The enzyme is most active toward long-chain acyl-CoAs such as C14, C16 and C18, but is also active with very-long-chain acyl-CoAs up to 24 carbons. It shows no activity for substrates of less than 12 carbons. Its specific activity towards palmitoyl-CoA is more than 10-fold that of the long-chain acyl-CoA dehydrogenase [1]. cf. EC 1.3.8.1, short-chain acyl-CoA dehydrogenase, EC 1.3.8.7, medium-chain acyl-CoA dehydrogenase, and EC 1.3.8.8, long-chain acyl-CoA dehydrogenase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Izai, K., Uchida, Y., Orii, T., Yamamoto, S. and Hashimoto, T. Novel fatty acid β-oxidation enzymes in rat liver mitochondria. I. Purification and properties of very-long-chain acyl-coenzyme A dehydrogenase. J. Biol. Chem. 267 (1992) 1027–1033. [PMID: 1730632] |
2. |
Aoyama, T., Souri, M., Ushikubo, S., Kamijo, T., Yamaguchi, S., Kelley, R.I., Rhead, W.J., Uetake, K., Tanaka, K. and Hashimoto, T. Purification of human very-long-chain acyl-coenzyme A dehydrogenase and characterization of its deficiency in seven patients. J. Clin. Invest. 95 (1995) 2465–2473. [DOI] [PMID: 7769092] |
3. |
McAndrew, R.P., Wang, Y., Mohsen, A.W., He, M., Vockley, J. and Kim, J.J. Structural basis for substrate fatty acyl chain specificity: crystal structure of human very-long-chain acyl-CoA dehydrogenase. J. Biol. Chem. 283 (2008) 9435–9443. [DOI] [PMID: 18227065] |
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[EC 1.3.8.9 created 1961 as EC 1.3.2.2, transferred 1964 to EC 1.3.99.3, part transferred 2012 to EC 1.3.8.9] |
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EC
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1.3.99.3
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Transferred entry: | acyl-CoA dehydrogenase, now EC 1.3.8.7, medium-chain acyl-CoA dehydrogenase, EC 1.3.8.8, long-chain acyl-CoA dehydrogenase and EC 1.3.8.9, very-long-chain acyl-CoA dehydrogenase
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[EC 1.3.99.3 created 1961 as EC 1.3.2.2, transferred 1964 to EC 1.3.99.3, deleted 2012] |
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EC
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1.3.99.12
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Transferred entry: | 2-methylacyl-CoA dehydrogenase. Now classified as EC 1.3.8.5, 2-methyl-branched-chain-enoyl-CoA reductase.
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[EC 1.3.99.12 created 1986, deleted 2020] |
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EC |
2.3.1.295 |
Accepted name: |
mycoketide-CoA synthase |
Reaction: |
a medium-chain acyl-CoA + 5 malonyl-CoA + 5 (S)-methylmalonyl-CoA + 22 NADPH + 22 H+ = a mycoketide-CoA + 10 CO2 + 10 CoA + 22 NADP+ + 11 H2O |
Glossary: |
a mycoketide-CoA = a 4,8,12,16,20-pentamethyl-(long-chain fatty acyl)-CoA |
Other name(s): |
pks12 (gene name) |
Systematic name: |
malonyl-CoA/(S)-methylmalonyl-CoA:heptanoyl-CoA malonyltransferase (mycoketide-CoA-forming) |
Comments: |
The enzyme, found in mycobacteria, is involved in the synthesis of β-D-mannosyl phosphomycoketides. It is a very large polyketide synthase that contains two complete sets of FAS-like fatty acid synthase modules. It binds an acyl-CoA with 5-9 carbons as a starter unit, and extends it by five rounds of alternative additions of malonyl-CoA and methylmalonyl-CoA extender units. Depending on the starter unit, the enzyme forms mycoketide-CoAs of different lengths. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Matsunaga, I., Bhatt, A., Young, D.C., Cheng, T.Y., Eyles, S.J., Besra, G.S., Briken, V., Porcelli, S.A., Costello, C.E., Jacobs, W.R., Jr. and Moody, D.B. Mycobacterium tuberculosis pks12 produces a novel polyketide presented by CD1c to T cells. J. Exp. Med. 200 (2004) 1559–1569. [PMID: 15611286] |
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[EC 2.3.1.295 created 2019] |
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EC |
3.1.2.18 |
Accepted name: |
ADP-dependent short-chain-acyl-CoA hydrolase |
Reaction: |
acyl-CoA + H2O = CoA + a carboxylate |
Other name(s): |
short-chain acyl coenzyme A hydrolase; propionyl coenzyme A hydrolase; propionyl-CoA hydrolase; propionyl-CoA thioesterase; short-chain acyl-CoA hydrolase; short-chain acyl-CoA thioesterase |
Systematic name: |
ADP-dependent-short-chain-acyl-CoA hydrolase |
Comments: |
Requires ADP; inhibited by NADH. Maximum activity is shown with propanoyl-CoA. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 117698-16-5 |
References: |
1. |
Alexson, S.E.H. and Nedergaard, J. A novel type of short- and medium-chain acyl-CoA hydrolases in brown adipose tissue mitochondria. J. Biol. Chem. 263 (1988) 13564–13571. [PMID: 2901416] |
2. |
Alexson, S.E.H., Svensson, L.T. and Nedergaard, J. NADH-sensitive propionyl-CoA hydrolase in brown-adipose-tissue mitochondria of the rat. Biochim. Biophys. Acta 1005 (1989) 13–19. [DOI] [PMID: 2570608] |
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[EC 3.1.2.18 created 1992] |
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EC |
3.1.2.19 |
Accepted name: |
ADP-dependent medium-chain-acyl-CoA hydrolase |
Reaction: |
acyl-CoA + H2O = CoA + a carboxylate |
Other name(s): |
medium-chain acyl coenzyme A hydrolase; medium-chain acyl-CoA hydrolase; medium-chain acyl-thioester hydrolase; medium-chain hydrolase; myristoyl-CoA thioesterase |
Systematic name: |
ADP-dependent-medium-chain-acyl-CoA hydrolase |
Comments: |
Requires ADP; inhibited by NADH. Maximum activity is shown with nonanoyl-CoA. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 63363-75-7 |
References: |
1. |
Alexson, S.E.H. and Nedergaard, J. A novel type of short- and medium-chain acyl-CoA hydrolases in brown adipose tissue mitochondria. J. Biol. Chem. 263 (1988) 13564–13571. [PMID: 2901416] |
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[EC 3.1.2.19 created 1992] |
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EC |
4.2.1.74 |
Accepted name: |
medium-chain-enoyl-CoA hydratase |
Reaction: |
a medium-chain (3S)-3-hydroxyacyl-CoA = a medium-chain trans-2-enoyl-CoA + H2O |
Glossary: |
a medium-chain acyl-CoA = an acyl-CoA thioester where the acyl chain contains 6 to 12 carbon atoms. |
Other name(s): |
long-chain enoyl coenzyme A hydratase (incorrect); long-chain-enoyl-CoA hydratase (incorrect); long-chain-(3S)-3-hydroxyacyl-CoA hydro-lyase (incorrect) |
Systematic name: |
medium-chain-(3S)-3-hydroxyacyl-CoA hydro-lyase |
Comments: |
Acts in the reverse direction. The best substrate for the porcine enzyme is oct-2-enoyl-CoA. Unlike EC 4.2.1.17 enoyl-CoA hydratase, it does not act on crotonoyl-CoA. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 62009-81-8 |
References: |
1. |
Fong, J.C. and Schulz, H. Purification and properties of pig heart crotonase and the presence of short chain and long chain enoyl coenzyme A hydratases in pig and guinea pig tissues. J. Biol. Chem. 252 (1977) 542–547. [PMID: 833142] |
2. |
Schulz, H. Long chain enoyl coenzyme A hydratase from pig heart. J. Biol. Chem. 249 (1974) 2704–2709. [PMID: 4828315] |
3. |
Arent, S., Christensen, C.E., Pye, V.E., Norgaard, A. and Henriksen, A. The multifunctional protein in peroxisomal β-oxidation: structure and substrate specificity of the Arabidopsis thaliana protein MFP2. J. Biol. Chem. 285 (2010) 24066–24077. [DOI] [PMID: 20463021] |
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[EC 4.2.1.74 created 1981, modified 2022] |
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EC |
6.2.1.2 |
Accepted name: |
medium-chain acyl-CoA ligase |
Reaction: |
ATP + a medium-chain fatty acid + CoA = AMP + diphosphate + a medium-chain acyl-CoA |
Other name(s): |
fadK (gene name); lvaE (gene name); butyryl-CoA synthetase; fatty acid thiokinase (medium chain); acyl-activating enzyme; fatty acid elongase; fatty acid activating enzyme; fatty acyl coenzyme A synthetase; butyrate—CoA ligase; butyryl-coenzyme A synthetase; L-(+)-3-hydroxybutyryl CoA ligase; short-chain acyl-CoA synthetase; medium-chain acyl-CoA synthetase; butanoate:CoA ligase (AMP-forming) |
Systematic name: |
medium-chain fatty acid:CoA ligase (AMP-forming) |
Comments: |
Acts on fatty acids from C4 to C11 and on the corresponding 3-hydroxy and 2,3- or 3,4-unsaturated acids. The enzyme from the bacterium Pseudomonas putida also acts on 4-oxo and 4-hydroxy derivatives. |
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] |
4. |
Morgan-Kiss, R.M. and Cronan, J.E. The Escherichia coli fadK (ydiD) gene encodes an anerobically regulated short chain acyl-CoA synthetase. J. Biol. Chem. 279 (2004) 37324–37333. [PMID: 15213221] |
5. |
Rand, J.M., Pisithkul, T., Clark, R.L., Thiede, J.M., Mehrer, C.R., Agnew, D.E., Campbell, C.E., Markley, A.L., Price, M.N., Ray, J., Wetmore, K.M., Suh, Y., Arkin, A.P., Deutschbauer, A.M., Amador-Noguez, D. and Pfleger, B.F. A metabolic pathway for catabolizing levulinic acid in bacteria. Nat Microbiol 2 (2017) 1624–1634. [PMID: 28947739] |
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[EC 6.2.1.2 created 1961, modified 2011, modified 2018] |
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