kcat of p38α (MAPK14) protein kinase with EGFR as substrate

Value 31.6 sec^-1 Range: ±1.1 sec^-1
Organism Bacteria Escherichia coli
Reference Zhang YY, Mei ZQ, Wu JW, Wang ZX. Enzymatic activity and substrate specificity of mitogen-activated protein kinase p38alpha in different phosphorylation states. J Biol Chem. 2008 Sep 26 283(39):26591-601. doi: 10.1074/jbc.M801703200. p.26596 left column 3rd paragraph & p.26597 table 2PubMed ID18669639
Method "To determine the kinetic parameters of p38a kinase activity, [researchers] selected a synthetic peptide derived from the EGF receptor (residues 661–681 EGFR peptide) and the transcription factor ATF2?109 (residues 1–109) as p38a substrates... All steady-state kinetic studies were performed at pH 7.0 and 25°C."
Comments "By fitting the Michaelis-Menten equation to the experimental data, the values of kcat and Km were determined to be 31.6±1.1 s^-1 and 656±62µM, respectively."
Entered by Uri M
ID 110568