| Value |
0.562
sec^-1
Range: ±0.007 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 2nd paragraph & p.26597 table 1PubMed ID18669639
|
| Method |
"To characterize the biochemical properties
of various forms of p38a, [researchers] first measured the ATPase
and kinase activities of p38a in various phosphorylation states
using an enzyme-coupled spectrophotometric assay (refs 29, 30).
All steady-state kinetic studies were performed at pH 7.0 and
25 °C." |
| Comments |
"Direct curve
fitting of the data to the Michaelis-Menten equation yielded kcat
and Km values, which were 0.562±0.007 s^-1 and 212±12.6µM, respectively, for the p38a/pTpY (p38a phosphorylated on
both Thr-180 and Tyr-182)-catalyzed ATP hydrolysis." |
| Entered by |
Uri M |
| ID |
110567 |