Impact of Phosphorylation on Structure and Thermodynamics of the Interaction between the N-terminal Domain of Enzyme I and the Histidine Phosphocarrier Protein of the Bacterial Phosphotransferase System-Reference-Cited by-同舟云学术

Impact of Phosphorylation on Structure and Thermodynamics of the Interaction between the N-terminal Domain of Enzyme I and the Histidine Phosphocarrier Protein of the Bacterial Phosphotransferase System

Published:2008-07 Issue:27 Volume:283 Page:18980-18989
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Suh Jeong-Yong,Cai Mengli,Clore G. Marius

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference44 articles.

1. THE BACTERIAL PHOSPHOENOL-PYRUVATE: GLYCOSE PHOSPHOTRANSFERASE SYSTEM

2. Structure/function studies on the bacterial carbohydrate transporters, enzymes II, of the phosphoenolpyruvate-dependent phosphotransferase system

3. Carbohydrate transporters of the bacterial phosphoenolpyruvate: sugar phosphotransferase system (PTS)

4. How Phosphotransferase System-Related Protein Phosphorylation Regulates Carbohydrate Metabolism in Bacteria

5. Sugar transport by the bacterial phosphotransferase system. Phosphoryl transfer reactions catalyzed by enzyme I of Salmonella typhimurium.

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