Open AccessThe cell surface associated phosphatase activity of Mycobacterium bovis BCG is not regulated by environmental inorganic phosphate
Author(s) -
Braibant Martine,
Content Jean
Publication year - 2001
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2001.tb10508.x
Subject(s) - phosphomonoesterase , phosphatase , alkaline phosphatase , phosphate , acid phosphatase , biochemistry , inorganic phosphate , chemistry , mycobacterium bovis , enzyme , phosphoric monoester hydrolases , substrate (aquarium) , mycobacterium , bacteria , microbiology and biotechnology , biology , mycobacterium tuberculosis , ecology , genetics , medicine , tuberculosis , pathology
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.