To improve security and privacy, we are moving our web pages and services from HTTP to HTTPS. To give users of web services time to transition to HTTPS, we will support separate HTTP and HTTPS services until the end of 2017. From January 2018 most HTTP traffic will be automatically redirected to HTTPS. [more...] View this page in https
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
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 18.104.22.168), medium (MCAD) (EC 22.214.171.124), long (LCAD) (EC 126.96.36.199),
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 188.8.131.52) (GCDH), which is involved in the
catabolism of lysine, hydroxylysine and tryptophan.
Isovaleryl-CoA dehydrogenase (EC 184.108.40.206) (IVD), involved in the
catabolism of leucine.
Acyl-coA dehydrogenases acdA and mmgC from Bacillus subtilis.
Butyryl-CoA dehydrogenase (EC 220.127.116.11) from Clostridium acetobutylicum.
Matsubara Y., Indo Y., Naito E., Ozasa H., Glassberg R., Vockley J., Ikeda Y., Kraus J., Tanaka K.
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.
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.
PROSITE is copyright. It is produced by the SIB Swiss Institute
Bioinformatics. There are no restrictions on its use by non-profit
institutions as long as its content is in no way modified. Usage by and
for commercial entities requires a license agreement. For information
about the licensing scheme send an email to
or see: prosite_license.html.