Feb 17, 2001

The cell surface associated phosphatase activity of Mycobacterium bovis BCG is not regulated by environmental inorganic phosphate

FEMS Microbiology Letters
Martine Braibant, Jean Content

Abstract

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.

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Mentioned in this Paper

Acid Phosphatase
Alkaline Phosphatase
Mycobacterium bovis
Enzyme Induction
Orthophosphate
Hydrogen-Ion Concentration
ALPI
Plasma Membrane

About this Paper

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