Summary: Cell-free extracts of strains Pi and T960 (CX8) (serovars 6 and 8, respectively) metabolized inorganic pyrophosphate (PP). The inorganic pyrophosphatase (PPase) activity was greatest with Mg as cofactor, but Mn acted as a poor substitute. The PPases of the two serovars differed electrophoretically. Although the highest PPase activity was obtained using PP as substrate, the enzyme could also utilize to a lesser degree both tripolyphosphate and trimetaphosphate. No activity was observed against β-glycerophosphate, naphthyl phosphates, glucose 6-phosphate, fructose 6-phosphate, fructose 1,6-bisphosphate, thiamin pyrophosphate, phosphoribosylpyrophosphate, ADP or ATP. Acid- and alkaline-phosphatase activities were observed with naphthyl phosphates as substrates, but they did not have the same electrophoretic mobility on gels as the PPase activity. PPase was inhibited by oxidized glutathione, 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide, phenyl-glyoxal, -chloromercuribenzoic acid, Mn, Zn and Ca. Neither reduced glutathione, -cysteine nor Co enhanced activity. PP can act as a substrate or regulator of certain metabolic reactions, and PP metabolism can function in bacterial bioenergetics; its role in ureaplasmas is presently unclear.


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