title: CoA-persulphide: a possible in vivo inhibitor of mammalian short-chain acyl-CoA dehydrogenase.
abstract: The characteristic green colour of native short-chain acyl-CoA dehydrogenases (EC 1.3.99.2) results from a charge transfer complex between the FAD prosthetic group and a tightly bound molecule of CoA-persulphide. The native enzyme from ox liver mitochondria was found to have about 60% of its FAD cofactor liganded with CoA-persulphide. When artificially fully liganded with CoA-persulphide, this enzyme was inhibited by 90% in comparison to unliganded enzyme. Enzymic activity could be slowly restored by displacing the CoA-persulphide with high concentrations of butyryl-CoA, the enzyme's physiological substrate. The results show that CoA-persulphide is a potent inhibitor of short-chain acyl-CoA dehydrogenase and may have a physiological role in the regulation of beta-oxidation.
mesh_terms: D042964:Acyl-CoA Dehydrogenase; D044944:Acyl-CoA Dehydrogenases / Q000037:antagonists & inhibitors* / Q000378:metabolism; D000818:Animals; D001665:Binding Sites; D002417:Cattle; D003065:Coenzyme A / Q000378:metabolism / Q000494:pharmacology*; D008099:Liver / Q000201:enzymology; D013053:Spectrophotometry
chemical_list: C052650:coenzyme A persulfide; D044944:Acyl-CoA Dehydrogenases; D042964:Acyl-CoA Dehydrogenase; D003065:Coenzyme A