EC 1.3.8.1 - Short-chain acyl-CoA dehydrogenase

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IntEnz Enzyme Nomenclature
EC 1.3.8.1

Names

Accepted name:
short-chain acyl-CoA dehydrogenase
Other names:
3-hydroxyacyl CoA reductase
butyryl coenzyme A dehydrogenase
butyryl dehydrogenase
enoyl-coenzyme A reductase
ethylene reductase
butyryl-CoA dehydrogenase
short-chain acyl-coenzyme A dehydrogenase
unsaturated acyl coenzyme A reductase
unsaturated acyl-CoA reductase
short-chain acyl CoA dehydrogenase
butanoyl-CoA:(acceptor) 2,3-oxidoreductase
butanoyl-CoA dehydrogenase
ACADS (gene name)
Systematic name:
short-chain acyl-CoA:electron-transfer flavoprotein 2,3-oxidoreductase

Reactions

Cofactor

Comments:

Contains FAD as prosthetic group. One of several enzymes that catalyse the first step in fatty acids β-oxidation. The enzyme catalyses the oxidation of saturated short-chain acyl-CoA thioesters to give a trans 2,3-unsaturated product by removal of the two pro-R hydrogen atoms. The enzyme from beef liver accepts substrates with acyl chain lengths of 3 to 8 carbon atoms. The highest activity was reported with either butanoyl-CoA [2] or pentanoyl-CoA [4]. The enzyme from rat has only 10% activity with hexanoyl-CoA (compared to butanoyl-CoA) and no activity with octanoyl-CoA [6]. cf. EC 1.3.8.7, medium-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.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , NIST 74 , UM-BBD , UniPathway
Protein domains and families: PROSITE:PDOC00070
Structural data: CSA , EC2PDB
Gene Ontology: GO:0004085
CAS Registry Number: 9027-88-7
UniProtKB/Swiss-Prot: (10) [show] [UniProt]

References

  1. Mahler, H.R.
    Studies on the fatty acid oxidizing system of animal tissues. IV. The prosthetic group of butyryl coenzyme A dehydrogenase.
    J. Biol. Chem. 206: 13-26 (1954). [PMID: 13130522]
  2. Green, D.E., Mii, S., Mahler, H.R. and Bock, R.M.
    Studies on the fatty acid oxidizing system of animal tissue. III. Butyryl coenzyme A dehydrogenase.
    J. Biol. Chem. 206: 1-12 (1954). [PMID: 13130521]
  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, New York, 1963, 447-466
  4. Shaw, L., Engel, P. C.
    The purification and properties of ox liver short-chain acyl-CoA dehydrogenase.
    Biochem. J. 218: 511-520 (1984). [PMID: 6712627]
  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. 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]
  7. McMahon, B., Gallagher, M. E., Mayhew, S. G.
    The protein coded by the PP2216 gene of Pseudomonas putida KT2440 is an acyl-CoA dehydrogenase that oxidises only short-chain aliphatic substrates.
    FEMS Microbiol. Lett. 250: 121-127 (2005). [PMID: 16024185]

[EC 1.3.8.1 created 1961 as EC 1.3.2.1, transferred 1964 to EC 1.3.99.2, transferred 2011 to EC 1.3.8.1, modified 2012]