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. 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 and participates in fatty acid metabolism and PPAR signaling pathway.

References

Crane FL, Hauge JG, Beinert H (June 1955). "Flavoproteins involved in the first oxidative step of the fatty acid cycle". Biochimica et Biophysica Acta. 17 (2): 292–4. doi:10.1016/0006-3002(55)90374-7. PMID 13239683.
Crane FL, Mii S, Hauge JG, Green DE, Beinert H (February 1956). "On the mechanism of dehydrogenation of fatty acyl derivatives of coenzyme A. I. The general fatty acyl coenzyme A dehydrogenase". The Journal of Biological Chemistry. 218 (2): 701–6. doi:10.1016/S0021-9258(18)65836-3. PMID 13295224.
Beinert, H. (1963). "Acyl coenzyme A dehydrogenase". In Boyer, P.D.; Lardy, H.; Myrbäck, K. (eds.). The Enzymes. Vol. 7 (2nd ed.). New York: Academic Press. pp. 447–466.
Ikeda Y, Okamura-Ikeda K, Tanaka K (January 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". The Journal of Biological Chemistry. 260 (2): 1311–25. doi:10.1016/S0021-9258(20)71245-7. PMID 3968063.
Thorpe C, Kim JJ (June 1995). "Structure and mechanism of action of the acyl-CoA dehydrogenases". FASEB Journal. 9 (9): 718–25. doi:10.1096/fasebj.9.9.7601336. PMID 7601336. S2CID 42549744.
Kim JJ, Wang M, Paschke R (August 1993). "Crystal structures of medium-chain acyl-CoA dehydrogenase from pig liver mitochondria with and without substrate". Proceedings of the National Academy of Sciences of the United States of America. 90 (16): 7523–7. Bibcode:1993PNAS...90.7523K. doi:10.1073/pnas.90.16.7523. PMC 47174. PMID 8356049.
Peterson KL, Sergienko EE, Wu Y, Kumar NR, Strauss AW, Oleson AE, Muhonen WW, Shabb JB, Srivastava DK (November 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): 14942–53. doi:10.1021/bi00045a039. PMID 7578106.
Toogood HS, van Thiel A, Basran J, Sutcliffe MJ, Scrutton NS, Leys D (July 2004). "Extensive domain motion and electron transfer in the human electron transferring flavoprotein.medium chain Acyl-CoA dehydrogenase complex". The Journal of Biological Chemistry. 279 (31): 32904–12. doi:10.1074/jbc.M404884200. PMID 15159392.
Ezzeddini R, Taghikhani M, Salek Farrokhi A, Somi MH, Samadi N, Esfahani A, Rasaee, MJ (May 2021). "Downregulation of fatty acid oxidation by involvement of HIF-1α and PPARγ in human gastric adenocarcinoma and its related clinical significance". Journal of Physiology and Biochemistry. 77 (2): 249–260. doi:10.1007/s13105-021-00791-3. PMID 33730333. S2CID 232300877.

External links

Medium-chain+acyl-CoA+dehydrogenase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

v t e 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

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

Portal:

Biology

Category:

EC 1.3.8