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Metabolism of glycerate 2 3 di phosphate 5. histidine specific reagents inactivate the phospho glycerate mutase glycerate 2 3 di phosphate synthase and glycerate 2 3 di phosphate phosphatase activities of rabbit muscle phospho glycerate mutase



Metabolism of glycerate 2 3 di phosphate 5. histidine specific reagents inactivate the phospho glycerate mutase glycerate 2 3 di phosphate synthase and glycerate 2 3 di phosphate phosphatase activities of rabbit muscle phospho glycerate mutase



Comparative Biochemistry and Physiology B 76(4): 795-800



Both treatment with diethylpyrocarbonate and photooxidation with rose bengal produces the loss of the 3 enzymatic activites of rabbit muscle phosphoglcyerate mutase: phosphoglycerate mutase, glycerate-2,3-P2 synthase and glycerate-2,3-P2 phosphatase. The synthase and the phosphatase activities are less affected than the mutase activity. Glycerate-2,3-P2 and glycerate-3-P protect against diethylpyrocarbonate inactivation, but do not protect against inactivation produced by photo-oxidation. Hydroxylamine reactivates the diethylpyrocarbonate-treated enzyme. Chemical modification of phosphoglycerate mutase markedly reduces its ability to form the functionally active phosphoenzyme. Evidence of the intrinsic characters of the 3 enzymatic activities of phosphoglycerate mutase was provided. The existence of 2 separate binding sites for monophosphoglycerates and for bisphosphoglycerates were supported.

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