EC 1 - Oxidoreductases
EC 1.3 - Acting on the CH-CH group of donors
EC 1.3.8 - With a flavin as acceptor
EC 1.3.8.1 - Short-chain acyl-CoA dehydrogenase
IntEnz Enzyme Nomenclature
EC 1.3.8.1
Names
butyryl coenzyme A dehydrogenase
butyryl dehydrogenase
enoyl-coenzyme A reductase
ethylene reductase
butyryl-CoA dehydrogenase
short-chain acyl-coenzyme A dehydrogenase
unsaturated acyl coenzyme A reductase
unsaturated acyl-CoA reductase
short-chain acyl CoA dehydrogenase
butanoyl-CoA:(acceptor) 2,3-oxidoreductase
butanoyl-CoA dehydrogenase
ACADS (gene name)
Reactions
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butanoyl-CoAName origin: UniProt - CHECKED (C)Formula: C25H38N7O17P3S
Charge: -4ChEBI compound status: CHECKED (C)H+Name origin: UniProt - CHECKED (C)Formula: H
Charge: 1ChEBI compound status: CHECKED (C)oxidized [electron-transfer flavoprotein]GENERIC:10685Is ROOT: no
ROOT compound: GENERIC:10684Number of residues: 1=(2E)-butenoyl-CoAName origin: UniProt - CHECKED (C)Formula: C25H36N7O17P3S
Charge: -4ChEBI compound status: CHECKED (C) -
47196 [IUBMB]a short-chain 2,3-saturated fatty acyl-CoAName origin: UniProt - CHECKED (C)Formula: C24H35N7O17P3SR
Charge: -4ChEBI compound status: CHECKED (C)H+Name origin: UniProt - CHECKED (C)Formula: H
Charge: 1ChEBI compound status: CHECKED (C)oxidized [electron-transfer flavoprotein]GENERIC:10685Is ROOT: no
ROOT compound: GENERIC:10684Number of residues: 1=a short-chain (2E)-enoyl-CoAName origin: UniProt - CHECKED (C)Formula: C24H33N7O17P3SR
Charge: -4ChEBI compound status: CHECKED (C)
Cofactor
Comments:
Contains FAD as prosthetic group. 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
References
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Studies on the fatty acid oxidizing system of animal tissues. IV. The prosthetic group of butyryl coenzyme A dehydrogenase.J. Biol. Chem. 206 : 13-26 (1954). [PMID: 13130522]
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Studies on the fatty acid oxidizing system of animal tissue. III. Butyryl coenzyme A dehydrogenase.J. Biol. Chem. 206 : 1-12 (1954). [PMID: 13130521]
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Acyl coenzyme A dehydrogenase.In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.) The Enzymes , 2nd ed. vol. 7 , Academic Press , New York , 1963 , 447-466
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The purification and properties of ox liver short-chain acyl-CoA dehydrogenase.Biochem. J. 218 : 511-520 (1984). [PMID: 6712627]
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Structure and mechanism of action of the acyl-CoA dehydrogenases.FASEB J. 9 : 718-725 (1995). [PMID: 7601336]
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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 : 1311-1325 (1985). [PMID: 3968063]
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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 : 121-127 (2005). [PMID: 16024185]
[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]