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Phosphoglucomutase

II. PREPARATION AND PROPERTIES OF PHOSPHOGLUCOMUTASES FROM MICROCOCCUS LYSODEIKTICUS AND BACILLUS CEREUS

From the ¹ From the Department of Biochemistry, Duke University Medical Center, Durham, North Carolina 27706

Procedures are described for the preparation of phosphoglucomutases from Bacillus cereus and Micrococcus lysodeikticus. Both require Mg⁺⁺ and glucose 1,6-diphosphate for activity which is optimal at pH 8.3 and 8.5, respectively; both enzymes rapidly equilibrate ³²P among -d-glucose-1-P, glucose-6-P, and glucose-1,6-di-P. In contrast to rabbit muscle and Escherichia coli P-glucomutases, neither of these bacterial enzymes could be shown to form a stable phosphoenzyme by reaction with glucose-1,6-di-P. Correspondingly, the rabbit muscle and E. coli enzymes exhibited "shuttle" kinetics whereas Lineweaver-Burk plots with the B. cereus and M. lysodeikticus enzymes yielded families of converging lines, suggesting a metathetical reaction between glucose-1,6-di-P and glucose-1-P on the enzyme surface. p-Chloromercuribenzoate partially inhibits the rabbit enzyme, completely inhibits the E. coli enzyme, activates and then deactivates the shark enzyme, activates and then inhibits the M. lysodeikticus enzyme, and is without effect on the B. cereus enzyme.

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