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Properties of two sugar phosphate phosphatases from Streptococcus bovis and their potential involvement in inducer expulsion
Author(s) -
Gregory M. Cook,
Jing Jing Ye,
James B. Russell,
Milton H. Saier
Publication year - 1995
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.177.23.7007-7009.1995
Subject(s) - biology , streptococcus bovis , pep group translocation , inducer , phosphatase , biochemistry , enzyme , sugar , lactose , phosphate , microbiology and biotechnology , rumen , phosphoenolpyruvate carboxykinase , fermentation , gene
Streptococcus bovis possesses two sugar phosphate phosphatases (Pases). Pase I is a soluble enzyme that is inhibited by the membrane fractions from lactose-grown cells and is insensitive to activation by S46D HPr, an analog of HPr(ser-P) of the sugar phosphotransferase system. Pase II is a membrane-associated enzyme that can be activated 10-fold by S46D HPr, and it appears to play a role in inducer expulsion.

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