| Entry |
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| Name |
short-chain acyl-CoA dehydrogenase;
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).
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| Class |
Oxidoreductases;
Acting on the CH-CH group of donors;
With a flavin as acceptor
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| Sysname |
short-chain acyl-CoA:electron-transfer flavoprotein 2,3-oxidoreductase
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| Reaction(IUBMB) |
a short-chain acyl-CoA + electron-transfer flavoprotein = a short-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein [RN: R01178]
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| Reaction(KEGG) |
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| Substrate |
short-chain acyl-CoA [CPD: C20675];
electron-transfer flavoprotein [CPD: C04253]
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| Product |
short-chain trans-2,3-dehydroacyl-CoA [CPD: C20676];
reduced electron-transfer flavoprotein [CPD: C04570]
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| Comment |
Contains FAD as prosthetic group. One of several enzymes that catalyse the first step in fatty acids beta-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.
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| History |
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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| Pathway |
| ec00280 | Valine, leucine and isoleucine degradation |
| ec01110 | Biosynthesis of secondary metabolites |
| ec01120 | Microbial metabolism in diverse environments |
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| Orthology |
| K00248 | butyryl-CoA dehydrogenase |
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| Genes |
» show all
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| Reference |
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| Authors |
MAHLER HR. |
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| Title |
Studies on the fatty acid oxidizing system of animal tissues. IV. The prosthetic group of butyryl coenzyme A dehydrogenase. |
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| Journal |
J Biol Chem 206:13-26 (1954) |
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| Reference |
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| Authors |
GREEN DE, MII S, MAHLER HR, BOCK RM |
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| Title |
Studies on the fatty acid oxidizing system of animal tissues. III. Butyryl coenzyme A dehydrogenase. |
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| Journal |
J Biol Chem 206:1-12 (1954) |
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| Reference |
3 |
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| Authors |
Beinert, H. |
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| Title |
Acyl coenzyme A dehydrogenase. |
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| Journal |
In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd ed., vol. 7, Academic Press, New York, 1963, p. 447-466. |
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| Reference |
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| Authors |
Shaw L, Engel PC |
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| Title |
The purification and properties of ox liver short-chain acyl-CoA dehydrogenase. |
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| Journal |
Biochem J 218:511-20 (1984) |
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| Reference |
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| Authors |
Thorpe C, Kim JJ |
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| Title |
Structure and mechanism of action of the acyl-CoA dehydrogenases. |
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| Journal |
FASEB J 9:718-25 (1995) |
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| Reference |
|
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| Authors |
Ikeda Y, Okamura-Ikeda K, Tanaka K. |
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| Title |
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. |
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| Journal |
J Biol Chem 260:1311-25 (1985) |
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| Sequence |
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| Reference |
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| Authors |
McMahon B, Gallagher ME, Mayhew SG |
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| Title |
The protein coded by the PP2216 gene of Pseudomonas putida KT2440 is an acyl-CoA dehydrogenase that oxidises only short-chain aliphatic substrates. |
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| Journal |
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| Other DBs |
| ExplorEnz - The Enzyme Database: | 1.3.8.1 |
| ExPASy - ENZYME nomenclature database: | 1.3.8.1 |
| UM-BBD (Biocatalysis/Biodegradation Database): | 1.3.8.1 |
| BRENDA, the Enzyme Database: | 1.3.8.1 |
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