- ATP + protein L-histidine ADP + protein N-phospho-L-histidine
This enzyme belongs to the family of transferases, specifically those transferring a phosphate group to the sidechain of histidine residues in proteins (protein-histidine kinases). The systematic name of this enzyme class is ATP:protein-L-histidine N-phosphotransferase. Other names in common use include EnvZ, histidine kinase (ambiguous), histidine protein kinase (ambiguous), protein histidine kinase (ambiguous), protein kinase (histidine) (ambiguous), HK1, HP165, and Sln1p. This enzyme participates in 4 metabolic pathways: two-component system - general, bacterial chemotaxis - general, bacterial chemotaxis - organism-specific, and type ii secretion system.
- IUBMB entry for 18.104.22.168
- BRENDA references for 22.214.171.124 (Recommended.)
- PubMed references for 126.96.36.199
- PubMed Central references for 188.8.131.52
- Google Scholar references for 184.108.40.206
- Kowluru A (2002). "Identification and characterization of a novel protein histidine kinase in the islet beta cell: evidence for its regulation by mastoparan, an activator of G-proteins and insulin secretion". Biochem. Pharmacol. 63: 2091&ndash, 100. PMID 12110368.
- Yoshimi A, Tsuda M, Tanaka C (2004). "Cloning and characterization of the histidine kinase gene Dic1 from Cochliobolus heterostrophus that confers dicarboximide resistance and osmotic adaptation". Mol. Genet. Genomics. 271: 228&ndash, 36. PMID 14752661.
- Beier D, Frank R (2000). "Molecular characterization of two-component systems of Helicobacter pylori". J. Bacteriol. 182: 2068&ndash, 76. PMID 10735847.
- Pflock M, Dietz P, Schar J, Beier D (2004). "Genetic evidence for histidine kinase HP165 being an acid sensor of Helicobacter pylori". FEMS. Microbiol. Lett. 234: 51&ndash, 61. PMID 15109719.
- Roberts DL, Bennett DW, Forst SA (1994). "Identification of the site of phosphorylation on the osmosensor, EnvZ, of Escherichia coli". J. Biol. Chem. 269: 8728&ndash, 33. PMID 8132603.
Gene Ontology (GO) codes
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