Medium-chain acyl-CoA dehydrogenase

Medium-chain acyl-CoA dehydrogenase

Medium-chain acyl-CoA dehydrogenase tetramer, Human
Identifiers
EC number 1.3.8.7
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

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

This enzyme contains FAD as prosthetic group.

References

  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 47174Freely accessible. 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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