Metabolism of glycerate-2,3-P2--IV. Effect of Hg2+ on the enzymes involved in the metabolism of glycerate-2,3-P2 in pig skeletal muscle.
Type M phosphoglycerate mutase and skeletal muscle bisphosphoglycerate synthase-phosphatase from pig are similarly affected by Hg2+. Both enzymes lose the phosphoglycerate mutase and the glycerate-2,3-P2 synthase activities, and increase the glycerate-2,3-P2 phosphatase activity upon Hg2+-treatment. In contrast, bisphosphoglycerate phosphatase from pig skeletal muscle is inactivated by Hg2+. These results confirm the similarity between phosphoglycerate mutase and bisphosphoglycerate synthase-phosphatase. In addition they support the existence of separate binding sites for monophosphoglycerates and for bisphosphoglycerates at the phosphoglycerate mutase active site.
D019794:2,3-Diphosphoglycerate; D000818:Animals; D004163:Diphosphoglyceric Acids / Q000378:metabolism*; D004229:Dithiothreitol / Q000494:pharmacology; D004789:Enzyme Activation / Q000187:drug effects; D004793:Enzyme Reactivators; D008628:Mercury / Q000494:pharmacology*; D009132:Muscles / Q000201:enzymology*; D010736:Phosphoglycerate Mutase / Q000378:metabolism*; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism*; D010770:Phosphotransferases / Q000378:metabolism*; D013552:Swine
D004163:Diphosphoglyceric Acids; D004793:Enzyme Reactivators; C019794:bisphosphoglycerate phosphatase; D019794:2,3-Diphosphoglycerate; D010770:Phosphotransferases; D010744:Phosphoric Monoester Hydrolases; D010736:Phosphoglycerate Mutase; D008628:Mercury; D004229:Dithiothreitol