PHOSPHATASES OF ACINETOBACTER-LWOFFI LOCALIZATION AND REGULATION OF SYNTHESIS BY ORTHOPHOSPHATE

Several phosphomonoesterases and diesterases with various pH optima have been observed in Acinetobacter lwofi JW11. The osmotic shock fluids contained only those with an alkaline pH optimum. The synthesis of these phosphatases was regulated by external Pi concentrations. The shock fluids were fractionated by chromatography, yielding three fractions, two of which had hydrophobic properties. One of these contained an alkaline phosphatase that specifically required Ca2+ for activity. The diesterases required various divalent cations for their function. Mutants that lack phosphomonoesterase or both phosphomonoesterase and phosphodiesterase activities were isolated. © 1990 Springer-Verlag New York Inc.