| Abstract
| - The chemical and catalytic properties of potato phosphoglucomutase [EC 2.7.5.1] were studied using various enzyme species (Peaks la, Ib, Ic, and II; Takamiya, S. & Fukui, T. (1978) Plant Cell Physiol. 19, 319-328). The molecular weights of the species are all approximately 60,000. No indication of the presence of subunit structure was obtained under various conditions. The amino acid composition of Peak Ia is generally similar to those of the enzymes from other sources, though it has some peculiarities. The Peak Ia and Peak II enzymes both absolutely require α-D-glucose 1,6-bisphosphate and Mg2+ for activity, and appear to have a “ping-pong” mechanism. A low concentration of Be2+ inhibits their action, the inhibition being retarded either by Mg2+ or EDTA. Although the inhibition patterns by various metabolites are similar for Peaks Ia and II, they differ in their kinetic parameters and optimal pH values.
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