Structural Analysis of the Bacterial HPr Kinase/Phosphorylase V267F Mutant Gives Insights into the Allosteric Regulation Mechanism of This Bifunctional Enzyme-Reference-Cited by-同舟云学术

Structural Analysis of the Bacterial HPr Kinase/Phosphorylase V267F Mutant Gives Insights into the Allosteric Regulation Mechanism of This Bifunctional Enzyme

Published:2007-11 Issue:48 Volume:282 Page:34952-34957
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Chaptal Vincent,Vincent Fanny,Gueguen-Chaignon Virginie,Monedero Vicente,Poncet Sandrine,Deutscher Josef,Nessler Sylvie,Morera Solange

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference38 articles.

1. Phosphorylation of HPr and Crh by HprK, Early Steps in the Catabolite Repression Signalling Pathway for the Bacillus subtilis Levanase Operon

2. Specific recognition of the Bacillus subtilis gnt cis-acting catabolite-responsive element by a protein complex formed between CcpA and seryl-phosphorylated HPr

3. Binding of the Catabolite Repressor Protein CcpA to Its DNA Target Is Regulated by Phosphorylation of its Corepressor HPr

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

5. Transcription Regulators Potentially Controlled by HPr Kinase/Phosphorylase in Gram-Negative Bacteria

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