The hydrolysis of glucose monophosphates by a phosphatase preparation from pea seeds

Abstract

A phosphatase from pea seeds that hydrolyzed both glucose 1 -phosphate and glucose 6-phosphate was purified approximately 20-fold. Glucose 1-phosphate was hydrolyzed directly and not by way of glucose 6-phosphate. The effects of pH, substrate concentration and inhibitors on the hydrolysis of the glucose monophosphates were studied. The hydrolysis of other phosphoric compounds by the enzyme preparation was examined. Low concentrations of inorganic phosphate competitively inhibited the hydrolysis of both glucose 1-phosphate and glucose 6-phosphate. The possible metabolic significance of this inhibition has been discussed.