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Abstract
The distribution and some properties of polyphosphate kinase, that catalyzes the formation of polyphosphate from ATP, were investigated. High enzyme activity was found in Alcaligenes faecalis, Brevibacterium ammoniagenes, Escherichia coli, Micrococuss lysodeikticus and Pseudomonas aeruginosa. The enzyme required Mg2+ for maximum activity and was activated by basic proteins, polyamines and phosphate polymers of low molecular weight. The enzyme from E. coli B could catalyze the reverse reaction, and generated ATP from ADP and metaphosphate. The feasibility of the generation of ATP by the E. coli B enzyme was confirmed by means of the coupled reactions of polyphosphate kinase and hexokinase, which produces glucose-6-phosphate.