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Metabolism of 2 3 bisphosphoglycerate xi. essential amino acids of pig phosphoglycerate mutase isozymes


, : Metabolism of 2 3 bisphosphoglycerate xi. essential amino acids of pig phosphoglycerate mutase isozymes. Comparative Biochemistry and Physiology B 86(3): 547-554

Phosphoglycerate mutase isozymes (types M, B and MB) from pig tissues are inactivated upon treatment with reagents specific for histidyl, arginyl and lysyl residues. Their mutase, 2,3-biphosphoglycerate synthase and 2,3-bisphosphoglycerate phosphatase activities are concurrently lost, although some differences exist in the rate of inactivation. No significant differences are observed between the isozymes. 3. The reversion of the modifying reactions reactivates the three activities. 4. Substrates and cofactors protect against inactivation, the protective effects varying with the modifying reagent. 5. Titration with pCMB shows the existence of two essential thiol groups per subunit type M. 6. These results provide evidence of the intrinsic character o fthe three enzymatic activities, favor their location at the same active site and suggest the existence of separate binding sites for monophosphoglycerates and bisphophoglycerates. 7. Both type M and B subunit from pig phosphoglycerate mutase are similar to type M subunit from rabbit and to the enzyme from yeast.

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