Long-chain acyl-CoA dehydrogenase

Long-chain acyl-CoA dehydrogenase (EC 1.3.8.8, palmitoyl-CoA dehydrogenase, palmitoyl-coenzyme A dehydrogenase, long-chain acyl-coenzyme A dehydrogenase, long-chain-acyl-CoA:(acceptor) 2,3-oxidoreductase, ACADL (gene).) is an enzyme with systematic name long-chain acyl-CoA:electron-transfer flavoprotein 2,3-oxidoreductase.^[1]^[2]^[3]^[4]^[5] This enzyme catalyses the following chemical reaction

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

\rightleftharpoons

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

This enzyme contains FAD as prosthetic group and participates in fatty acid metabolism and PPAR signaling pathway. Mitochondrial mutations in this enzyme may be associated with some forms of dilated cardiomyopathy.

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: 292–294. doi:10.1016/0006-3002(55)90374-7. PMID 13239683.
↑ Hauge, J.G., Crane, F.L. and Beinert, H. (1956). "On the mechanism of dehydrogenation of fatty acyl derivatives of coenzyme A. III. Palmityl CoA dehydrogenase". J. Biol. Chem. 219: 727–733. PMID 13319294.
↑ Hall, C.L., Heijkenkjold, L., Bartfai, T., Ernster, L. and Kamin, H. (1976). "Acyl coenzyme A dehydrogenases and electron-transferring flavoprotein from beef heart mitochondria". Arch. Biochem. Biophys. 177: 402–414. doi:10.1016/0003-9861(76)90453-7. PMID 1015826.
↑ 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: 1311–1325. PMID 3968063.
↑ Djordjevic, S., Dong, Y., Paschke, R., Frerman, F.E., Strauss, A.W. and Kim, J.J. (1994). "Identification of the catalytic base in long chain acyl-CoA dehydrogenase". Biochemistry 33: 4258–4264. doi:10.1021/bi00180a021. PMID 8155643.

External links

Long-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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