Autocatalytic rate kcat for various histidine kinases (from different bacteria)

Range Table - link sec^-1
Organism bacteria
Reference Bitbol AF, Wingreen NS. Fundamental constraints on the abundances of chemotaxis proteins. Biophys J. 2015 Mar 10 108(5):1293-305. doi: 10.1016/j.bpj.2015.01.024. Supporting information p.10 Table S3PubMed ID25762341
Primary Source See refs beneath table
Comments P.1300 left column bottom paragraph: "Several other features of the chemotaxis pathway reflect a pressure toward rapidity. First, the existence of a dedicated phosphatase for the response regulator CheY, which is uncommon for two-component systems, suggests the importance of fast turnover of the CheY-P pool. Second, CheA is an extremely fast histidine kinase: when incorporated in signaling complexes containing chemoreceptors and CheW, the autocatalytic rate of CheA is kcatA=20/s for E. coli (refs 52, 53 and 54) and Salmonella typhimurium (primary source 29), which makes it four to five orders of magnitude faster than other kinases in two-component systems (Table S3)." See note above table
Entered by Uri M
ID 112524