Properties of two sugar phosphate phosphatases from Streptococcus bovis and their potential involvement in inducer expulsion

J Bacteriol. 1995 Dec;177(23):7007-9. doi: 10.1128/jb.177.23.7007-7009.1995.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Bacterial Proteins*
  • Cell Fractionation
  • Enzyme Activation
  • Methylgalactosides / metabolism*
  • Phosphoenolpyruvate Sugar Phosphotransferase System / metabolism
  • Phosphoric Monoester Hydrolases / isolation & purification
  • Phosphoric Monoester Hydrolases / metabolism*
  • Streptococcus bovis / enzymology*
  • Streptococcus bovis / metabolism
  • Sugar Phosphates / metabolism*
  • Thiogalactosides / metabolism*

Substances

  • Bacterial Proteins
  • Methylgalactosides
  • Sugar Phosphates
  • Thiogalactosides
  • thiomethylgalactoside
  • Phosphoenolpyruvate Sugar Phosphotransferase System
  • phosphocarrier protein HPr
  • Phosphoric Monoester Hydrolases