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. 1984 Apr;47(4):693–698. doi: 10.1128/aem.47.4.693-698.1984

Production of two phosphatases by Lysobacter enzymogenes and purification and characterization of the extracellular enzyme.

R G von Tigerstrom
PMCID: PMC239750  PMID: 6426386

Abstract

Lysobacter enzymogenes produces an extracellular phosphatase (EC. 3.1.3.1) during the stationary phase of growth. The cells also produce a cell-associated alkaline phosphatase. This enzyme is found in the particulate fraction of cell extracts and may be membrane bound. The production of both phosphatases, especially the extracellular enzyme, is reduced by inorganic phosphate. The extracellular phosphatase was purified to a specific activity of 270 U/mg primarily by chromatography on carboxymethyl cellulose and gel filtration. The enzyme is stable under normal storage conditions but is rapidly inactivated above 70 degrees. It consists of one polypeptide with an approximate molecular weight of 25,000. The pH optimum is 7.5, and the Km for p-nitrophenylphosphate is 2.2 X 10(-4) M. The enzyme degrades a number of other phosphomonoesters but at a reduced rate compared with the rate obtained with p-nitrophenylphosphate. Phosphate and arsenate inhibit the enzyme, but EDTA and other chelating agents have no effect. The lack of a metal ion requirement for activity, the lower molecular weight, the soluble nature of the enzyme, and the lower pH optimum clearly distinguish the extracellular phosphatase from the cell-associated phosphatase and from other bacterial phosphatases.

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Selected References

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