Stereochemical course of the reactions catalyzed by the bacterial phosphoenolpyruvate:mannitol phosphotransferase system
β Scribed by Mueller, Eugene G.; Khandekar, Sanjay S.; Knowles, Jeremy R.; Jacobson, Gary R.
- Book ID
- 125981060
- Publisher
- American Chemical Society
- Year
- 1990
- Tongue
- English
- Weight
- 676 KB
- Volume
- 29
- Category
- Article
- ISSN
- 0006-2960
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The kinetic mechanisms by which the glucose, glucitol, N-acetylglucosamine, and mannitol enzymes I1 catalyze sugar phosphorylation have been investigated in vitro. Lineweaver-Burk analyses indicate that the glucose and glucitol enzymes I1 catalyze sugar phosphorylation by a sequential mechanism when
The phosphoenolpyruvate: sugar phosphotransferase system (PTS) found in enteric bacteria is a complex enzyme system consisting of a non-sugar-specific phosphotransfer protein called Enzyme I, two small non-sugar-specific phosphocarrier substrates of Enzyme I, designated HPr and FPr, and at least 11