EC 1.3.8.8 - Long-chain-acyl-CoA dehydrogenase

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IntEnz Enzyme Nomenclature
EC 1.3.8.8

Names

Accepted name:
long-chain-acyl-CoA dehydrogenase
Other names:
long-chain acyl-coenzyme A dehydrogenase
palmitoyl-CoA dehydrogenase
palmitoyl-coenzyme A dehydrogenase
long-chain-acyl-CoA:(acceptor) 2,3-oxidoreductase
ACADL (gene name)
Systematic name:
long-chain-acyl-CoA:electron-transfer flavoprotein 2,3-oxidoreductase

Reaction

Cofactor

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 6 to at least 16 carbon atoms. The highest activity was found with C12, and the rates with C8 and C16 were 80% and 70%, respectively [2]. The enzyme from rat can accept substrates with C8-C22. It is most active with C14 and C16, and has no activity with C4, C6 or C24 [4]. cf. EC 1.3.8.1, short-chain acyl-CoA dehydrogenase, EC 1.3.8.8, medium-chain acyl-CoA dehydrogenase, and EC 1.3.8.9, very-long-chain acyl-CoA dehydrogenase.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00070
Structural data: CSA , EC2PDB
Gene Ontology: GO:0004466
CAS Registry Number: 59536-74-2
UniProtKB/Swiss-Prot: (12) [show] [UniProt]

References

  1. Hall, C.L., Heijkenkjold, L., Bartfai, T., Ernster, L. and Kamin, H.
    Acyl coenzyme A dehydrogenases and electron-transferring flavoprotein from beef heart mitochondria.
    Arch. Biochem. Biophys. 177 : 402-414 (1976). [PMID: 1015826]
  2. Hauge, J.G., Crane, F.L. and Beinert, H.
    On the mechanism of dehydrogenation of fatty acyl derivatives of coenzyme A. III. Palmityl CoA dehydrogenase.
    J. Biol. Chem. 219 : 727-733 (1956). [PMID: 13319294]
  3. Ikeda, Y., Ikeda, K.O. and 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]
  4. 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]
  5. Djordjevic, S., Dong, Y., Paschke, R., Frerman, F. E., Strauss, A. W., Kim, J. J.
    Identification of the catalytic base in long chain acyl-CoA dehydrogenase.
    Biochemistry 33 : 4258-4264 (1994). [PMID: 8155643]

[EC 1.3.8.8 created 1989 as EC 1.3.99.13, part transferred 2012 to EC 1.3.8.8]