Magnesium and magnesium adenosine triphosphate activation of human propionyl CoA carboxylase and beta-methylcrotonyl CoA carboxylase.
Free magnesium and MgATP2- are required for activation of the mitochondrial enzymes pyruvate carboxylase, propionyl CoA carboxylase and beta-methylcrotonyl CoA carboxylase. Previous studies have demonstrated that free Mg2+ interacts with either a Mg2+- binding site or one of the two MgATP2- sites that are required for the allosteric activation of pyruvate carboxylase. We have shown that similar Mg2+ and MgATP2- interactions occur to activate propionyl CoA carboxylase and beta-methylcrotonyl CoA carboxylase. Thus, Mg2+ and MgATP2- activation, because it is common to structurally similar carboxylases, may constitute a general mode of carboxylase activation.
D000255:Adenosine Triphosphate / Q000494:pharmacology*; D001665:Binding Sites; D019735:Carbon-Carbon Ligases; D004789:Enzyme Activation; D005347:Fibroblasts / Q000201:enzymology; D006801:Humans; D007700:Kinetics; D008025:Ligases / Q000378:metabolism*; D008099:Liver / Q000201:enzymology; D008274:Magnesium / Q000494:pharmacology*
D000255:Adenosine Triphosphate; D008025:Ligases; D019735:Carbon-Carbon Ligases; C022458:propionyl CoA carboxylase (ATP-hydrolyzing); C021573:methylcrotonoyl-CoA carboxylase; D008274:Magnesium