The HPr Kinase from Bacillus subtilis Is a Homo-oligomeric Enzyme Which Exhibits Strong Positive Cooperativity for Nucleotide and Fructose 1,6-Bisphosphate Binding-Reference-Cited by-同舟云学术

The HPr Kinase from Bacillus subtilis Is a Homo-oligomeric Enzyme Which Exhibits Strong Positive Cooperativity for Nucleotide and Fructose 1,6-Bisphosphate Binding

Published:2000-01 Issue:3 Volume:275 Page:1773-1780
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Jault Jean-Michel,Fieulaine Sonia,Nessler Sylvie,Gonzalo Philippe,Di Pietro Attilio,Deutscher Josef,Galinier Anne

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference52 articles.

1. PHOSPHATE BOUND TO HISTIDINE IN A PROTEIN AS AN INTERMEDIATE IN A NOVEL PHOSPHO-TRANSFERASE SYSTEM

2. The Phosphoenolpyruvate-Dependent Phosphotransferase System of Staphylococcus aureus. 2. 1H and 31P Nuclear-Magnetic-Resonance Studies on the Phosphocarrier Protein HPr, Phosphohistidines and Phosphorylated HPr

3. Purification and characterization of an ATP-dependent protein kinase fromStreptococcus faecalis

4. Properties of ATP-dependent protein kinase from Streptococcus pyogenes that phosphorylates a seryl residue in HPr, a phosphocarrier protein of the phosphotransferase system

5. New protein kinase and protein phosphatase families mediate signal transduction in bacterial catabolite repression

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