A New Family of Phosphotransferases with a P-loop Motif
Open Access
- 1 March 2002
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 277 (13) , 11362-11367
- https://doi.org/10.1074/jbc.m109527200
Abstract
No abstract availableKeywords
This publication has 31 references indexed in Scilit:
- Catabolite repression mediated by the CcpA protein in Bacillus subtilis: novel modes of regulation revealed by whole‐genome analysesMolecular Microbiology, 2001
- Characterization of an HPr Kinase Mutant of Staphylococcus xylosusJournal of Bacteriology, 2000
- The HPr Kinase from Bacillus subtilis Is a Homo-oligomeric Enzyme Which Exhibits Strong Positive Cooperativity for Nucleotide and Fructose 1,6-Bisphosphate BindingPublished by Elsevier ,2000
- The hprK gene of Enterococcus faecalis encodes a novel bifunctional enzyme: the HPr kinase/phosphataseMolecular Microbiology, 1999
- A novel protein kinase that controls carbon catabolite repression in bacteriaMolecular Microbiology, 1998
- New protein kinase and protein phosphatase families mediate signal transduction in bacterial catabolite repressionProceedings of the National Academy of Sciences, 1998
- The Bacillus subtilis crh gene encodes a HPr-like protein involved in carbon catabolite repressionProceedings of the National Academy of Sciences, 1997
- Protein phosphorylation and regulation of carbon metabolism in Gram-negative versus Gram-positive bacteriaTrends in Biochemical Sciences, 1995
- Protein kinase‐dependent HPr/CcpA interaction links glycolytic activity to carbon catabolite repression in Gram‐positive bacteriaMolecular Microbiology, 1995
- The P-loop — a common motif in ATP- and GTP-binding proteinsTrends in Biochemical Sciences, 1990