Medium-chain acyl-CoA dehydrogenase

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Medium-chain acyl-CoA dehydrogenase
Medium-chain acyl-CoA dehydrogenase tetramer, Human
EC number1.3.8.7
IntEnzIntEnz view
ExPASyNiceZyme view
MetaCycmetabolic pathway
PDB structuresRCSB PDB PDBe PDBsum

Medium-chain acyl-CoA dehydrogenase (EC, 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 a medium-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein

This enzyme contains FAD as prosthetic group.


  1. ^ Crane, F.L.; Hauge, J.G.; 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.
  2. ^ Crane, F.L.; Mii, S.; Hauge, J.G.; Green, D.E.; 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.
  3. ^ Beinert, H. (1963). "Acyl coenzyme A dehydrogenase". In Boyer, P.D.; Lardy, H.; Myrbäck, K. The Enzymes. 7 (2nd ed.). New York: Academic Press. pp. 447–466.
  4. ^ 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.
  5. ^ Thorpe, C.; Kim, J.J. (1995). "Structure and mechanism of action of the acyl-CoA dehydrogenases". FASEB J. 9 (9): 718–725. PMID 7601336.
  6. ^ Kim, J.J.; Wang, M.; 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.
  7. ^ Peterson, K.L.; Sergienko, E.E.; Wu, Y.; Kumar, N.R.; Strauss, A.W.; Oleson, A.E.; Muhonen, W.W.; Shabb, J.B.; 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.
  8. ^ Toogood, H.S.; van Thiel, A.; Basran, J.; Sutcliffe, M.J.; Scrutton, N.S.; 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.

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