Involvement of the carboxy-terminal residue in the active site of the histidine-containing protein, HPr, of the phosphoenolpyruvate:sugar phosphotransferase system of Escherichia coli-Reference-Cited by-同舟云学术

Involvement of the carboxy-terminal residue in the active site of the histidine-containing protein, HPr, of the phosphoenolpyruvate:sugar phosphotransferase system of Escherichia coli

Published:1991-10-08 Issue:40 Volume:30 Page:9601-9607
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Anderson J. William,Bhanot Pradeep,Georges Fawzey,Klevit Rachel E.,Waygood E. Bruce

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi00104a006

Reference43 articles.

1. Sugar Transport

2. Sugar transport by the bacterial phosphotransferase system. Isolation and characterization of a phosphocarrier protein HPr from wild type and mutants of Salmonella typhimurium.

3. 716. The reactions of organic phosphates. Part I. The hydrolysis of methyl dihydrogen phosphate

4. 717. The reactions of organic phosphates. Part II. The hydrolysis of α-D-glucose 1-(dihydrogen phosphate)

5. Escherichia coli phosphoenolpyruvate dependent phosphotransferase system. NMR studies of the conformation of HPr and P-HPr and the mechanism of energy coupling

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3. Identification of Histidine Phosphorylations in Proteins Using Mass Spectrometry and Affinity‐Based Techniques;Methods in Enzymology;2007

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