Isovaleryl-CoA dehydrogenase
In enzymology, an isovaleryl-CoA dehydrogenase () is an enzyme that catalyzes the chemical reaction Thus, the two substrates of this enzyme are 3-methylbutanoyl-CoA and acceptor, whereas its two products are 3-methylbut-2-enoyl-CoA and reduced acceptor. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with other acceptors. The systematic name of this enzyme class is 3-methylbutanoyl-CoA:acceptor oxidoreductase. Other names in common use include isovaleryl-coenzyme A dehydrogenase, isovaleroyl-coenzyme A dehydrogenase, and 3-methylbutanoyl-CoA:(acceptor) oxidoreductase. This enzyme participates in valine , leucine and isoleucine degradation. It employs one cofactor, FAD. Structural studies. As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code . It was created by a group containing K.A.Tiffany, D.L.Roberts, M.Wang, R.Paschke, A.-W.A.Mohsen, J.Vockley, and J.J.P.Kim. The structure was released on May 20th, 1998.