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Metabolism of glycerate 2 3 di phosphate 3. arginine 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 3. arginine 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(1): 9-14



Treatment of rabbit muscle phosphoglycerate mutase with diketones (2,3-butanedione and 1,2-cyclohexanedione) and with glyoxal derivatives (methylglyoxal and phenylglyoxal) produces the loss of the 3 activities of the enzyme: phosphoglycerate mutase, glycerate-2,3-P2 synthase and glycerate-2,3-P2 phosphatase. Hydroxylamine reactivates all the activities of the modified enzyme. Inactivated phosphoglycerate mutase is unable to form the functionally active phosphoenzyme when mixed with glycerate-2,3-P2. Both substrate and cofactor protect against inactivation. These results provide additional evidence of the intrinsic character of the 3 enzymatic activities of phosphoglycerate mutase and favor their location at the same active site. Evidently, arginine is involved in the binding of the cofactor to the enzyme.

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