Identification and properties of distinct sucrose and glucose phosphotransferase enzyme II activities in Streptococcus mutans 6715g.
نویسندگان
چکیده
We investigated phosphoenolpyruvate-dependent phosphotransferase system enzyme II activities for sucrose and glucose in Streptococcus mutans 6715g. Two integral membrane proteins, enzyme IIscr and enzyme IIglc, each specific for its sugar substrate, sucrose or glucose, were identified by their abilities to catalyze specific sugar:sugar-phosphate exchange reactions. Some of the properties of these two transport proteins are also presented.
منابع مشابه
Characterization of a phosphoenolpyruvate-dependent sucrose phosphotransferase system in Streptococcus mutans.
A phosphoenolpyruvate-dependent sucrose phosphotransferase system has been identified in Streptococcus mutans. Sucrose phosphotransferase activity was inducible by sucrose and had an apparent Km for sucrose of 70 microM. The product of the sucrose phosphotransferase reaction was isolated and identified as sucrose phosphate. Additional analysis revealed that the phosphate group was on the glucos...
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The growth of Streptococcus mutants Ingbritt in continuous culture at low pH or high growth rates repressed the biosynthesis of the components of the phosphoenolpyruvate:sugar phosphotransferase system (PTS). The cellular concentrations of the soluble components HPr, enzyme I (EI), and EIII for mannose (IIIman) and EII activity for glucose, mannose, 2-deoxyglucose (2DG), and fructose were deter...
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ورودعنوان ژورنال:
- Infection and immunity
دوره 46 3 شماره
صفحات -
تاریخ انتشار 1984