<p>Mammalian Co-A dehydrogenases (<db_xref db="EC" dbkey="1.3.99.3"/>) are enzymes that catalyse the first step in each cycle of beta-oxidation in mitochondion. Acyl-CoA dehydrogenases [<cite idref="PUB00001328"/>, <cite idref="PUB00002511"/>, <cite idref="PUB00002861"/>] catalyze the alpha,beta-dehydrogenation of acyl-CoA thioesters to the corresponding trans 2,3-enoyl CoA-products with concommitant reduction of enzyme-bound FAD. Reoxidation of the flavin involves transfer of electrons to ETF (electron transfering flavoprotein). These enzymes are homodimers containing one molecule of FAD.</p> <p> The monomeric enzyme is folded into three domains of approximately equal size. The N-terminal and the C-terminal are mainly alpha-helices packed together, and the middle domain consists of two orthogonal beta-sheets. The flavin ring is buried in the crevise between two alpha-helical domains and the beta-sheet of one subunit, and the adenosine pyrophosphate moiety is stretched into the subunit junction with one formed by two C-terminal domains [<cite idref="PUB00007933"/>]. The C-terminal domain of Acyl-CoA dehydrogenase is an all-alpha, four helical up-and-down bundle.</p> Acyl-CoA oxidase/dehydrogenase, type 1