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| | <pubmed>12837773 9570401 9465101 12123463 18757537 12359880 11483496 12055300 10636874 12411438 11796714 12009882 12779331 11904409 12589763 12359875 15084125, </pubmed> | | <pubmed>12837773 9570401 9465101 12123463 18757537 12359880 11483496 12055300 10636874 12411438 11796714 12009882 12779331 11904409 12589763 12359875 15084125, </pubmed> |
| | '''review''' | | '''review''' |
| − | # Nessler S, Fieulaine S, Poncet S, Galinier A, Deutscher J, Janin J (2003) HPr kinase/phosphorylase, the sensor enzyme of catabolite repression in Gram-positive bacteria: structural aspects of the enzyme and the complex with its protein substrate. J Bacteriol 185:4003-4010. [http://www.ncbi.nlm.nih.gov/sites/entrez/12837773 PubMed]
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| | '''general/ physiology''' | | '''general/ physiology''' |
| − | # Reizer, J., Hoischen, C., Titgemeyer, F., Rivolta, C., Rabus, R., Stülke, J., Karamata, D., Saier, M. H., Jr., & Hillen, W. (1998) A novel bacterial protein kinase that controls carbon catabolite repression. Mol. Microbiol. 27: 1157-1169. [http://www.ncbi.nlm.nih.gov/sites/entrez/9570401 PubMed]
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| − | # Galinier A, Kravanja M, Engelmann R, Hengstenberg W, Kilhoffer MC, Deutscher J, Haiech J (1998) New protein kinase and protein phosphatase families mediate signal transduction in bacterial catabolite repression. Proc Natl Acad Sci USA 95:1823-1828. [http://www.ncbi.nlm.nih.gov/sites/entrez/9465101 PubMed]
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| − | # Ludwig, H., Rebhan, N., Blencke, H.-M., Merzbacher, M. & Stülke, J. (2002) Control of the glycolytic gapA operon by the catabolite control protein A in Bacillus subtilis: a novel mechanism of CcpA-mediated regulation. Mol. Microbiol. 45: 543-553. [http://www.ncbi.nlm.nih.gov/sites/entrez/12123463 PubMed]
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| − | # Singh, K. D., Schmalisch, M. H., Stülke, J. & Görke, B. (2008) Carbon catabolite repression in Bacillus subtilis: A quantitative analysis of repression exerted by different carbon sources. J. Bacteriol. 190: 7275-7284. [http://www.ncbi.nlm.nih.gov/sites/entrez/18757537 PubMed]
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| | | | |
| | '''enzymatic properties, mutation analysis''' | | '''enzymatic properties, mutation analysis''' |
| − | # Mijakovic I, Poncet S, Galiner A, Monedero V, Fieulaine S, Janin J, Nessler S, Marquez JA, Scheffzek K, Hasenbein S, Hengstenberg W, Deutscher J: Pyrophosphate-producing protein dephosphorylation by HPr kinase/ phosphorylase: a relic of early life? Proc Natl Acad Sci USA 2002, 99:13442-13447. [http://www.ncbi.nlm.nih.gov/sites/entrez/12359880 PubMed]
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| − | # Monedero V, Poncet S, Mijakovic I, Fieulaine S, Dossonet V, Martin-Verstraete I, Nessler S, Deutscher J (2001) Mutations lowering the phosphatase activity of HPr kinase/phosphatase switch off carbon metabolism. EMBO J 20:3928-3937. [http://www.ncbi.nlm.nih.gov/sites/entrez/11483496 PubMed]
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| − | # Hanson K. G., Steinhauer, K., Reizer, J., Hillen, W. & Stülke, J. (2002) HPr kinase/phosphatase of Bacillus subtilis: Expression of the gene and effects of mutations on enzyme activity, growth, and carbon catabolite repression. Microbiology 148: 1805-1811. [http://www.ncbi.nlm.nih.gov/sites/entrez/12055300 PubMed]
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| − | # Jault J M, Fieulaine S, Nessler S, Gonzalo P, Di Pietro A, Deutscher J, Galinier A (2000) The HPr kinase from Bacillus subtilis is a homo-oligomeric enzyme which exhibits strong positive cooperativity for nucleotide and fructose 1,6-bisphosphate binding. J Biol Chem 275:1773-1780. [http://www.ncbi.nlm.nih.gov/sites/entrez/10636874 PubMed]
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| − | # Ramström H, Sanglier S, Leize-Wagner E, Philippe C, van Dorsselaer A, Haiech J (2003) Properties and regulation of the bifunctional enzyme HPr kinase/phosphatase in Bacillus subtilis. J Biol Chem 278:1174-1185. [http://www.ncbi.nlm.nih.gov/sites/entrez/12411438 PubMed]
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| − | # Galinier, A., Lavergne, J.-P., Geourjon, C., Fieulaine, S., Nessler, S. & Jault, J.-M. (2002) A new family of phosphotransferases with a P-loop motif. J. Biol. Chem. 277, 11362-11367. [http://www.ncbi.nlm.nih.gov/sites/entrez/11796714 PubMed]
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| − | # Lavergne, J.-P., Jault, J.-M. & Galinier, A. (2002) Insights into the functioning of ''Bacillus subtilis'' HPr kinase/phosphatase: affinity for its protein substrates and role of cations and phosphate. Biochemistry 41, 6218-6225. [http://www.ncbi.nlm.nih.gov/sites/entrez/12009882 PubMed]
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| − | # Pompeo, F., Granet, Y., Lavergne, J.-P., Grangeasse, C., Nessler, S., Jault, J.-M. & Galinier, A. (2003) Regulation and mutational analysis of the HPr kinase/phosphorylase from ''Bacillus subtilis''. Biochemistry 42, 6762-6771. [http://www.ncbi.nlm.nih.gov/sites/entrez/12779331 PubMed]
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| | '''structure analysis''' | | '''structure analysis''' |
| − | # Márquez, J. A., Hasenbein, S., Koch, B., Fieulaine, S., Nessler, S., Russell, R. B., Hengstenberg, W. & Scheffzek, K. (2002) Structure of the full-length HPr kinase/phosphatase from ''Staphylococcus xylosus'' at 1.95 Å resolution: mimicking the product/substrate of the phosphotransfer reactions. Proc. Natl. Acad. Sci. USA 99, 3458-3463. [http://www.ncbi.nlm.nih.gov/sites/entrez/11904409 PubMed]
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| − | # Allen, G.S., Steinhauer, K., Hillen, W., Stülke, J. & Brennan, R.G. (2003) Crystal structure of HPr kinase/phosphatase from ''Mycoplasma pneumoniae''. J. Mol. Biol. 326, 1203-1217. [http://www.ncbi.nlm.nih.gov/sites/entrez/12589763 PubMed]
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| − | # Fieulaine, S., Morera, S., Poncet, S., Mijakovic, I., Galinier, A., Janin, J., Deutscher, J., and Nessler, S. (2002) X-ray structure of a bifunctional protein kinase in complex with its protein substrate HPr. Proc Natl Acad Sci U S A 99: 13437-13441. [http://www.ncbi.nlm.nih.gov/sites/entrez/12359875 PubMed]
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| | '''HprK as target for antimicrobial compounds''' | | '''HprK as target for antimicrobial compounds''' |
| − | # Ramström, H. et al. (2004) Heterocylic bis-cations as starting hits for design of inhibitors of the bifunctional enzyme histidine-containing protein kinase/ phosphatase from ''Bacillus subtilis''. J. Med. Chem. 47, 2264-2275. [http://www.ncbi.nlm.nih.gov/sites/entrez/15084125 PubMed]
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| − | # Author1, Author2 & Author3 (year) Title ''Journal'' '''volume:''' page-page. [http://www.ncbi.nlm.nih.gov/sites/entrez/PMID PubMed]
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