PROSITE documentation PDOC00070

Acyl-CoA dehydrogenases signatures




Description

Acyl-CoA dehydrogenases [1,2,3] are enzymes that catalyze the α,β-dehydrogenation of acyl-CoA esters and transfer electrons to ETF, the electron transfer protein. Acyl-CoA dehydrogenases are FAD flavoproteins. This family currently includes:

  • Five eukaryotic isozymes that catalyze the first step of the β-oxidation cycles for fatty acids with various chain lengths. These are short (SCAD) (EC 1.3.99.2), medium (MCAD) (EC 1.3.99.3), long (LCAD) (EC 1.3.99.13), very-long (VLCAD) and short/branched (SBCAD) chain acyl-CoA dehydrogenases. These enzymes are located in the mitochondrion. They are all homotetrameric proteins of about 400 amino acid residues except VLCAD which is a dimer and which contains, in its mature form, about 600 residues.
  • Glutaryl-CoA dehydrogenase (EC 1.3.99.7) (GCDH), which is involved in the catabolism of lysine, hydroxylysine and tryptophan.
  • Isovaleryl-CoA dehydrogenase (EC 1.3.99.10) (IVD), involved in the catabolism of leucine.
  • Acyl-coA dehydrogenases acdA and mmgC from Bacillus subtilis.
  • Butyryl-CoA dehydrogenase (EC 1.3.99.2) from Clostridium acetobutylicum.
  • Escherichia coli protein caiA [4].
  • Escherichia coli protein aidB.

We have selected two conserved regions as signature patterns. The first is located in the center of these enzymes, the second in the C-terminal section.

Last update:

December 2004 / Pattern and text revised.

Technical section

PROSITE methods (with tools and information) covered by this documentation:

ACYL_COA_DH_1, PS00072; Acyl-CoA dehydrogenases signature 1  (PATTERN)

ACYL_COA_DH_2, PS00073; Acyl-CoA dehydrogenases signature 2  (PATTERN)


References

1AuthorsTanaka K., Ikeda Y., Matsubara Y., Hyman D.B.
TitleMolecular basis of isovaleric acidemia and medium-chain acyl-CoA dehydrogenase deficiency.
SourceEnzyme 38:91-107(1987).
PubMed ID3326738

2AuthorsMatsubara Y., Indo Y., Naito E., Ozasa H., Glassberg R., Vockley J., Ikeda Y., Kraus J., Tanaka K.
TitleMolecular cloning and nucleotide sequence of cDNAs encoding the precursors of rat long chain acyl-coenzyme A, short chain acyl-coenzyme A, and isovaleryl-coenzyme A dehydrogenases. Sequence homology of four enzymes of the acyl-CoA dehydrogenase family.
SourceJ. Biol. Chem. 264:16321-16331(1989).
PubMed ID2777793

3AuthorsAoyama T., Ueno I., Kamijo T., Hashimoto T.
TitleRat very-long-chain acyl-CoA dehydrogenase, a novel mitochondrial acyl-CoA dehydrogenase gene product, is a rate-limiting enzyme in long-chain fatty acid beta-oxidation system. cDNA and deduced amino acid sequence and distinct specificities of the cDNA-expressed protein.
SourceJ. Biol. Chem. 269:19088-19094(1994).
PubMed ID8034667

4AuthorsEichler K., Bourgis F., Buchet A., Kleber H.-P., Mandrand-Berthelot M.-A.
TitleMolecular characterization of the cai operon necessary for carnitine metabolism in Escherichia coli.
SourceMol. Microbiol. 13:775-786(1994).
PubMed ID7815937



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