The role of the available sulphydryl group in liver butyryl-coenzyme A synthetase.
Butyryl-CoA synthetase from acetone-dried ox liver mitochondria can be activated up to 80% by low concentrations of iodoacetate with the concomitant modification of one available enzyme thiol group. The relative molecular mass of the carboxymethylated enzyme was unchanged, and there were no major changes in the complex kinetic properties of the enzyme. Extraction experiments on liver mitochondria indicate that in vivo the enzyme is linked to a mitochondrial membrane by a bond cleavable by disulphide bond reducing agents.
D000818:Animals; D002417:Cattle; D003066:Coenzyme A Ligases / Q000378:metabolism*; D004789:Enzyme Activation / Q000187:drug effects; D007425:Intracellular Membranes / Q000201:enzymology; D007461:Iodoacetates / Q000494:pharmacology; D019807:Iodoacetic Acid; D007700:Kinetics; D008623:Mercaptoethanol / Q000494:pharmacology; D008930:Mitochondria, Liver / Q000201:enzymology*; D008970:Molecular Weight; D012995:Solubility; D013438:Sulfhydryl Compounds / Q000378:metabolism*
D007461:Iodoacetates; D013438:Sulfhydryl Compounds; D008623:Mercaptoethanol; D003066:Coenzyme A Ligases; C019805:butyryl-CoA synthetase; D019807:Iodoacetic Acid