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

Citation
M. Braibant et J. Content, The cell surface associated phosphatase activity of Mycobacterium bovis BCG is not regulated by environmental inorganic phosphate, FEMS MICROB, 195(2), 2001, pp. 121-126
Citations number
21
Categorie Soggetti
Microbiology
Journal title
FEMS MICROBIOLOGY LETTERS
ISSN journal
03781097 → ACNP
Volume
195
Issue
2
Year of publication
2001
Pages
121 - 126
Database
ISI
SICI code
0378-1097(20010220)195:2<121:TCSAPA>2.0.ZU;2-R
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, pea ks of phosphatase activity were detected at pH 6.0, pH 10.0 and pH 12.0, su ggesting the presence of one acid phosphatase and two alkaline phosphatases with distinct optimum pH values. Contrary to the situation observed in sev eral other microorganisms. the expression of these enzymes is not regulated by the environmental inorganic phosphate concentration. (C) 2001 Federatio n of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.