| 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 |