Kinetics of Phosphoglucomutase Action*

The mechanism of activation of the phosphoglucomutase reaction by the coenzyme, cu-glucose 1,6-diphosphate, was studied by Leloir et al. (1)) Sutherland et al. (2)) and Jagannathan and Luck (3). In 1954, Najjar and Pullman (4) showed that the active, phosphorylated form of the enzyme interacted with glucose l-phosphate to form the coenzyme and the inactive, dephosphorylated enzyme, and that these latter products could also interact to form glucose-6-P and the active, phosphorylated enzyme. The reverse reaction, glucose-6-P -+ glucose-l-P, was formulated similarly. The purpose of the present study is to examine the kinetics for further insight into the details of this reaction. Data are submitted on the relationship between the reaction velocity and the concentration of the substrate, glucose-l-P, and the influences on this relationship of various concentrations of the coenzyme and of the reaction product, glucose-6-P.