The cell surface associated phosphatase activity of Mycobacterium bovis BCG is not regulated by environmental inorganic phosphate.
Non-specific phosphomonoesterase activities (alkaline phosphatase (EC 3.1.3.1) and acid phosphatase (EC 3.1.3.2)) were examined at the cell surface of Mycobacterium bovis BCG. Using p-nitrophenylphosphate as the substrate, peaks of phosphatase activity were detected at pH 6.0, pH 10.0 and pH 12.0, suggesting the presence of one acid phosphatase and two alkaline phosphatases with distinct optimum pH values. Contrary to the situation observed in several other microorganisms, the expression of these enzymes is not regulated by the environmental inorganic phosphate concentration.
Braibant
M
M
Institut Pasteur, Département de Virologie, rue Engeland 642, B-1180 Bruxelles, Belgium. braibant@tours.inra.fr
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D000135:Acid Phosphatase / Q000096:biosynthesis / Q000378:metabolism*; D000469:Alkaline Phosphatase / Q000096:biosynthesis / Q000378:metabolism*; D002462:Cell Membrane / Q000201:enzymology; D003470:Culture Media; D004790:Enzyme Induction; D006863:Hydrogen-Ion Concentration; D009163:Mycobacterium bovis / Q000201:enzymology* / Q000254:growth & development; D010710:Phosphates / Q000378:metabolism*
D003470:Culture Media; D010710:Phosphates; D000469:Alkaline Phosphatase; D000135:Acid Phosphatase