The Appearance and Disappearance of Uridine Diphosphate Glucose Pyrophosphorylase Activity during Differentiation of the Cellular Slime Mold Dictyostelium discoideum

Abstract Uridine diphosphate glucose pyrophosphorylase (EC 2.7.7.9) from the cellular slime mold, Dictyostelium discoideum, has been characterized. The specific enzyme activity increases 10-fold during the course of morphogenesis. This increase is sensitive to coincident inhibition of protein synthesis by actidione and prior inhibition of ribonucleic acid synthesis by actinomycin D. A new method of assay was developed which can be applied generally to nucleoside diphosphate-sugar pyrophosphorylase reactions.