Medium-chain acyl-CoA dehydrogenase

Medium-chain acyl-CoA dehydrogenase (EC 1.3.8.7, 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).) is an enzyme with systematic name medium-chain acyl-CoA:electron-transfer flavoprotein 2,3-oxidoreductase.^[1]^[2]^[3]^[4]^[5]^[6]^[7]^[8] This enzyme catalyses the following chemical reaction

a medium-chain acyl-CoA + electron-transfer flavoprotein

\rightleftharpoons

a medium-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein

This enzyme contains FAD as prosthetic group.

References

↑ Crane, F.L., Hauge, J.G. and Beinert, H. (1955). "Flavoproteins involved in the first oxidative step of the fatty acid cycle". Biochim. Biophys. Acta 17 (2): 292–294. doi:10.1016/0006-3002(55)90374-7. PMID 13239683.
↑ Crane, F.L., Mii, S., Hauge, J.G., Green, D.E. and Beinert, H. (1956). "On the mechanism of dehydrogenation of fatty acyl derivatives of coenzyme A. I. The general fatty acyl coenzyme A dehydrogenase". J. Biol. Chem. 218 (2): 701–716. PMID 13295224.
↑ Beinert, H. (1963). "Acyl coenzyme A dehydrogenase". In Boyer, P.D., Lardy, H. and Myrbäck, K. The Enzymes 7 (2nd ed.). New York: Academic Press. pp. 447–466.
↑ Ikeda, Y., Ikeda, K.O. and Tanaka, K. (1985). "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 (2): 1311–1325. PMID 3968063.
↑ Thorpe, C. and Kim, J.J. (1995). "Structure and mechanism of action of the acyl-CoA dehydrogenases". FASEB J. 9 (9): 718–725. PMID 7601336.
↑ Kim, J.J., Wang, M. and Paschke, R. (1993). "Crystal structures of medium-chain acyl-CoA dehydrogenase from pig liver mitochondria with and without substrate". Proc. Natl. Acad. Sci. USA 90: 7523–7527. doi:10.1073/pnas.90.16.7523. PMC 47174. PMID 8356049.
↑ 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. (1995). "Recombinant human liver medium-chain acyl-CoA dehydrogenase: purification, characterization, and the mechanism of interactions with functionally diverse C₈-CoA molecules". Biochemistry 34 (45): 14942–14953. doi:10.1021/bi00045a039. PMID 7578106.
↑ Toogood, H.S., van Thiel, A., Basran, J., Sutcliffe, M.J., Scrutton, N.S. and Leys, D. (2004). "Extensive domain motion and electron transfer in the human electron transferring flavoprotein.medium chain Acyl-CoA dehydrogenase complex". J. Biol. Chem. 279 (31): 32904–32912. doi:10.1074/jbc.M404884200. PMID 15159392.

External links

Medium-chain acyl-CoA dehydrogenase at the US National Library of Medicine Medical Subject Headings (MeSH)

Oxidoreductases: CH–CH oxidoreductases (EC 1.3)

1.3.1: NAD/NADP acceptor	Enoyl-acyl carrier protein reductase/Enoyl ACP reductase 7-Dehydrocholesterol reductase Biliverdin reductase 2,4 Dienoyl-CoA reductase Dihydroxymethyloxo-tetrahydroquinoline dehydrogenase

1.3.3: Oxygen acceptor	Dihydroorotate dehydrogenase Coproporphyrinogen III oxidase Protoporphyrinogen oxidase Bilirubin oxidase Acyl-CoA oxidase Dihydrouracil oxidase Tetrahydroberberine oxidase Secologanin synthase Tryptophan alpha,beta-oxidase Pyrroloquinoline-quinone synthase L-galactonolactone oxidase

1.3.5: Quinone	Succinate dehydrogenase SDHA SDHB SDHC SDHD

1.3.99: Other acceptors	Fumarate reductase Butyryl-CoA dehydrogenase Acyl CoA dehydrogenase ACADSB ACADS 5α-reductase SRD5A1 SRD5A2 SRD5A3 Glutaryl-CoA dehydrogenase Isovaleryl coenzyme A dehydrogenase 3-oxo-5beta-steroid 4-dehydrogenase

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases(list) EC2 Transferases(list) EC3 Hydrolases(list) EC4 Lyases(list) EC5 Isomerases(list) EC6 Ligases(list)

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