Butyryl-Coa Dehydrogenase, subunit A; domain 1
Butyryl-CoA Dehydrogenase, subunit A; domain 2
Butyryl-CoA Dehydrogenase, subunit A; domain 3
3-methylbutanoyl-CoA:(acceptor) oxidoreductase
Valine, leucine and isoleucine degradation
Reduced electron-transferring flavoprotein
Identification of the active site catalytic residue in human isovaleryl-CoA dehydrogenase.
Cerebral energy metabolism in isovaleric acidaemia.
Mechanism-based inhibitor discrimination in the acyl-CoA dehydrogenases.
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 35-421.
Structure of human isovaleryl-CoA dehydrogenase at 2.6 A resolution: structural basis for substrate specificity,.
Characterization of molecular defects in isovaleryl-CoA dehydrogenase in patients with isovaleric acidemia.
Mitochondrial import and processing of wild type and type III mutant isovaleryl-CoA dehydrogenase.
Identification of Caenorhabditis elegans isovaleryl-CoA dehydrogenase and structural comparison with other acyl-CoA dehydrogenases.
Arginine 387 of human isovaleryl-CoA dehydrogenase plays a crucial role in substrate/product binding.
This enzyme belongs to the acyl-CoA dehydrogenase family.