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PROSITE documentation PDOC00070 |
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:
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.
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PROSITE methods (with tools and information) covered by this documentation:
1 | Authors | Tanaka K. Ikeda Y. Matsubara Y. Hyman D.B. |
Title | Molecular basis of isovaleric acidemia and medium-chain acyl-CoA dehydrogenase deficiency. | |
Source | Enzyme 38:91-107(1987). | |
PubMed ID | 3326738 |
2 | Authors | Matsubara Y. Indo Y. Naito E. Ozasa H. Glassberg R. Vockley J. Ikeda Y. Kraus J. Tanaka K. |
Title | Molecular 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. | |
Source | J. Biol. Chem. 264:16321-16331(1989). | |
PubMed ID | 2777793 |
3 | Authors | Aoyama T. Ueno I. Kamijo T. Hashimoto T. |
Title | Rat 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. | |
Source | J. Biol. Chem. 269:19088-19094(1994). | |
PubMed ID | 8034667 |
4 | Authors | Eichler K. Bourgis F. Buchet A. Kleber H.-P. Mandrand-Berthelot M.-A. |
Title | Molecular characterization of the cai operon necessary for carnitine metabolism in Escherichia coli. | |
Source | Mol. Microbiol. 13:775-786(1994). | |
PubMed ID | 7815937 |