Multifunctional properties of beef liver phosphoglucomutase.

Abstract
Liver phosphoglucomutase was found to catalyze also the reaction of Glc-1, 6-P2 formation from Glc-1-P and Fru-1, 6-P2 or Glc-1-P and glycerate-1, 3-P2. The specific activity of Glc-1, 6-P2 formation from Glc-1-P and Fru-1, 6-P2 was 1/9200 of that of the mutase activity. The activity of Glc-1, 6-P2 formation from Glc-1-P and glycerate-1, 3-P2 was 1/122, 000 of the mutase activity. From the results of the kinetics and the thermal inactivation experiments, the reaction of the mutase and Glc-1, 6-P2 synthesis were strongly suggested to occur at the same active site of liver phosphoglucomutase. Liver phosphoglucomutase exhibited the Glc-1, 6-P2 phosphatase activity only in the presence of xylose 1-phosphate. The specific activity of phosphatase was only 1/154, 000 of that of the mutase activity.

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