Decreased dissociation of the 3-methylcrotonyl-CoA carboxylase complex from Achromobacter in the presence of 3-methylcrotonyl-CoA. A possible regulatory mechanism for the intracellular degradation of the enzyme.
By inactivation of different concentrations of 3-methylcrotonyl-CoA carboxylase from Achromobacter IVS with a fixed concentration of iodoacetamide, it was demonstrated that the degree of dissociation of the complex is considerably lower in the presence of 3-methylcrotonyl-CoA. ATP did not produce this effect. This property could serve to regulate the intracellular degradation of the enzyme, if the dissociated subunits were attacked preferentially.
D000421:Alcaligenes / Q000201:enzymology*; D001665:Binding Sites; D001710:Biotin; D002087:Butyrates; D003065:Coenzyme A / Q000494:pharmacology; D003437:Crotonates / Q000494:pharmacology; D007460:Iodoacetamide; D008025:Ligases / Q000378:metabolism; D046911:Macromolecular Substances; D011485:Protein Binding
D002087:Butyrates; D003437:Crotonates; D046911:Macromolecular Substances; D001710:Biotin; D008025:Ligases; D003065:Coenzyme A; D007460:Iodoacetamide