Short-chain acyl-CoA dehydrogenase

Short-chain acyl-CoA dehydrogenase (EC 1.3.8.1, 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).) is an enzyme with systematic name short-chain acyl-CoA:electron-transfer flavoprotein 2,3-oxidoreductase.^[1]^[2]^[3]^[4]^[5]^[6]^[7] This enzyme catalyses the following chemical reaction

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

\rightleftharpoons

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

This enzyime contains FAD as prosthetic group.

References

↑ Mahler, H.R. (1954). "Studies on the fatty acid oxidizing system of animal tissue. IV. The prosthetic group of butyryl coenzyme A dehydrogenase". J. Biol. Chem. 206 (1): 13–26. PMID 13130522.
↑ Green, D.E.; Mii, S.; Mahler, H.R.; Bock, R.M. (1954). "Studies on the fatty acid oxidizing system of animal tissue. III. Butyryl coenzyme A dehydrogenase". J. Biol. Chem. 206 (1): 1–12. PMID 13130521.
↑ Beinert, H.; Lardy, H.; Myrbäck, K. (1963). "Acyl coenzyme A dehydrogenase". In Boyer, P.D. The Enzymes. 7 (2nd ed.). New York: Academic Press. pp. 447–466.
↑ Shaw, L.; Engel, P.C. (1984). "The purification and properties of ox liver short-chain acyl-CoA dehydrogenase". Biochem. J. 218 (2): 511–520. PMC 1153367. PMID 6712627.
↑ Thorpe, C.; Kim, J.J. (1995). "Structure and mechanism of action of the acyl-CoA dehydrogenases". FASEB J. 9 (9): 718–725. PMID 7601336.
↑ Ikeda, Y.; Ikeda, K.O.; 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.
↑ McMahon, B.; Gallagher, M.E.; Mayhew, S.G. (2005). "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 (1): 121–127. doi:10.1016/j.femsle.2005.06.049. PMID 16024185.

External links

Short-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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