Escherichia coli phosphoenolpyruvate-dependent phosphotransferase system. Evidence that the dimer is the active form of enzyme I
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00546a009
Reference16 articles.
1. Sugar Transport
2. Escherichia coli phosphoenolpyruvate dependent phosphotransferase system. Copurification of HPr and .alpha.1-6 glucan
3. Escherichia coli phosphoenolpyruvate dependent phosphotransferase system. NMR studies of the conformation of HPr and P-HPr and the mechanism of energy coupling
4. Enzymology of Carbohydrate Transport in Bacteria
5. Molecular interactions in the bacterial phosphoenolpyruvate-phosphotransferase system (PTS)
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3. The bacterial phosphoenolpyruvate: sugar phosphotransferase system (PTS): an interface between energy and signal transduction;Journal of the Iranian Chemical Society;2012-12-18
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