In enzymology, an isovaleryl-CoA dehydrogenase () is an enzyme that catalysis, catalyzes the chemical reaction
:3-methylbutanoyl-CoA + acceptor
3-methylbut-2-enoyl-CoA + reduced acceptor
Thus, the two substrate (biochemistry), substrates of this enzyme are 3-methylbutanoyl-CoA and Electron acceptor, acceptor, whereas its two product (chemistry), 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 List of enzymes, 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 (biochemistry), cofactor, flavin adenine dinucleotide, FAD.
Structural studies
As of late 2007, only one tertiary structure, structure has been solved for this class of enzymes, with the Protein Data Bank, 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.
Leucine metabolism
References
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EC 1.3.8
Flavoproteins
Enzymes of known structure
Mitochondrial proteins