| Entry |
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| Name |
medium-chain acyl-CoA dehydrogenase;
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).
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| Class |
Oxidoreductases;
Acting on the CH-CH group of donors;
With a flavin as acceptor
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| Sysname |
medium-chain acyl-CoA:electron-transfer flavoprotein 2,3-oxidoreductase
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| Reaction(IUBMB) |
a medium-chain acyl-CoA + electron-transfer flavoprotein = a medium-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein [RN: R00392]
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| Reaction(KEGG) |
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| Substrate |
medium-chain acyl-CoA [CPD: C21926];
electron-transfer flavoprotein [CPD: C04253]
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| Product |
medium-chain trans-2,3-dehydroacyl-CoA;
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 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.
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| History |
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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| Pathway |
| ec00280 | Valine, leucine and isoleucine degradation |
| ec01110 | Biosynthesis of secondary metabolites |
| ec01130 | Biosynthesis of antibiotics |
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| Orthology |
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| Genes |
» show all
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| Reference |
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| Authors |
CRANE FL, HAUGE JG, BEINERT H |
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| Title |
Flavoproteins involved in the first oxidative step of the fatty acid cycle. |
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| Journal |
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| Reference |
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| Authors |
CRANE FL, MII S, HAUGE JG, GREEN DE, BEINERT H. |
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| Title |
On the mechanism of dehydrogenation of fatty acyl derivatives of coenzyme A. I. The general fatty acyl coenzyme A dehydrogenase. |
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| Journal |
J Biol Chem 218:701-6 (1956) |
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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 |
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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| 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 |
Kim JJ, Wang M, Paschke R |
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| Title |
Crystal structures of medium-chain acyl-CoA dehydrogenase from pig liver mitochondria with and without substrate. |
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| Journal |
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| Sequence |
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| Reference |
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| Authors |
Peterson KL, Sergienko EE, Wu Y, Kumar NR, Strauss AW, Oleson AE, Muhonen WW, Shabb JB, Srivastava DK |
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| Title |
Recombinant human liver medium-chain acyl-CoA dehydrogenase: purification, characterization, and the mechanism of interactions with functionally diverse C8-CoA molecules. |
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| Journal |
Biochemistry 34:14942-53 (1995) |
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| Reference |
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| Authors |
Toogood HS, van Thiel A, Basran J, Sutcliffe MJ, Scrutton NS, Leys D |
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| Title |
Extensive domain motion and electron transfer in the human electron transferring flavoprotein.medium chain Acyl-CoA dehydrogenase complex. |
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| Journal |
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| Sequence |
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| Other DBs |
| ExplorEnz - The Enzyme Database: | 1.3.8.7 |
| ExPASy - ENZYME nomenclature database: | 1.3.8.7 |
| BRENDA, the Enzyme Database: | 1.3.8.7 |
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