Stability and binding of the phosphorylated species of the N-terminal domain of enzyme I and the histidine phosphocarrier protein from the Streptomyces coelicolor phosphoenolpyruvate:sugar phosphotransferase system-Reference-Cited by-同舟云学术

Stability and binding of the phosphorylated species of the N-terminal domain of enzyme I and the histidine phosphocarrier protein from the Streptomyces coelicolor phosphoenolpyruvate:sugar phosphotransferase system

Published:2012-10 Issue:1 Volume:526 Page:44-53
ISSN:0003-9861
Container-title:Archives of Biochemistry and Biophysics
language:en
Short-container-title:Archives of Biochemistry and Biophysics

Author:

Doménech Rosa,Martínez-Gómez Ana Isabel,Aguado-Llera David,Martínez-Rodríguez Sergio,Clemente-Jiménez Josefa María,Velázquez-Campoy Adrián,Neira José L.

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics

Reference49 articles.

1. Carbon catabolite repression in bacteria: many ways to make the most out of nutrients

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

3. The mechanisms of carbon catabolite repression in bacteria

4. Bacterial PEP-Dependent Carbohydrate: Phosphotransferase Systems Couple Sensing and Global Control Mechanisms

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

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