EC 1.3.8.7 - Medium-chain acyl-CoA dehydrogenase

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IntEnz Enzyme Nomenclature
EC 1.3.8.7

Names

Accepted name:
medium-chain acyl-CoA dehydrogenase
Other names:
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)
Systematic name:
medium-chain acyl-CoA:electron-transfer flavoprotein 2,3-oxidoreductase

Reaction

Comments:

Contains FAD as prosthetic group. One of several enzymes that catalyse the first step in fatty acids β-oxidation. The enzyme from pig liver can accept substrates with acyl chain lengths of 4 to 16 carbon atoms, but is most active with C8 to C12 compounds [2]. The enzyme from rat does not accept C16 at all and is most active with C6-C8 compounds [4]. cf. EC 1.3.8.1, short-chain acyl-CoA dehydrogenase, EC 1.3.8.8, long-chain acyl-CoA dehydrogenase, and EC 1.3.8.9, very-long-chain acyl-CoA dehydrogenase.

One of several enzymes that catalyse the first step in fatty acids β-oxidation. The enzyme from pig liver can accept substrates with acyl chain lengths of 4 to 16 carbon atoms, but is most active with C8 to C12 compounds. The enzyme from rat does not accept C16 at all and is most active with C6-C8 compounds. cf. EC 1.3.8.1, EC 1.3.8.8 and EC 1.3.8.9. Formerly EC 1.3.2.2 and EC 1.3.99.3.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot: (11) [show] [UniProt]

References

  1. Crane, F.L., Hauge, J.G., Beinert, H.
    Flavoproteins involved in the first oxidative step of the fatty acid cycle.
    Biochim. Biophys. Acta 17: 292-294 (1955). [PMID: 13239683]
  2. Crane, F.L., Mii, S., Hauge, J.G., Green, D.E., Beinert, H.
    On the mechanism of dehydrogenation of fatty acyl derivatives of coenzyme A. I. The general fatty acyl coenzyme A dehydrogenase.
    J. Biol. Chem. 218: 701-706 (1956). [PMID: 13295224]
  3. Beinert, H.
    Acyl coenzyme A dehydrogenase.
    In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.) The Enzymes, 2nd ed. vol. 7, Academic Press, 1963, 447-466
  4. Ikeda, Y., Okamura-Ikeda, K., Tanaka, K.
    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 (1985). [PMID: 3968063]
  5. Thorpe, C., Kim, J. J.
    Structure and mechanism of action of the acyl-CoA dehydrogenases.
    FASEB J. 9: 718-725 (1995). [PMID: 7601336]
  6. Kim, J. J., Wang, M., Paschke, R.
    Crystal structures of medium-chain acyl-CoA dehydrogenase from pig liver mitochondria with and without substrate.
    Proc. Natl. Acad. Sci. U.S.A. 90: 7523-7527 (1993). [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.
    Recombinant human liver medium-chain acyl-CoA dehydrogenase: purification, characterization, and the mechanism of interactions with functionally diverse C8-CoA molecules.
    Biochemistry 34: 14942-14953 (1995). [PMID: 7578106]
  8. Toogood, H. S., van Thiel, A., Basran, J., Sutcliffe, M. J., Scrutton, N. S., Leys, D.
    Extensive domain motion and electron transfer in the human electron transferring flavoprotein.medium chain Acyl-CoA dehydrogenase complex.
    J. Biol. Chem. 279: 32904-32912 (2004). [PMID: 15159392]

[EC 1.3.8.7 created 1961 as EC 1.3.2.2, transferred 1964 to EC 1.3.99.3, part transferred 2012 to EC 1.3.8.7]