EC Number |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
---|
3.1.3.48 | -999 |
- |
more |
kinetic analyses of the effects of D92A and G129E mutations on the phospholipid and phosphoprotein phosphatase activities of PTEN |
714323 |
3.1.3.48 | -999 |
- |
more |
kinetic isotope effects. In the Stp reaction protonation of the leaving group lags behind P-O bond cleavage, evidenced by the small normal 15(V/K) values indicating a partial negative charge on the leaving group, as well as the more normal 18(V/K)bridge KIEs. The active form of the substrate is the dianion |
749953 |
3.1.3.48 | -999 |
- |
more |
kinetic isotope effects. In the VHZ reaction protonation of the leaving group lags behind P-O bond cleavage, evidenced by the small normal 15(V/K) values indicating a partial negative charge on the leaving group, as well as the more normal 18(V/K)bridge KIEs. The active form of the substrate is the dianion |
749953 |
3.1.3.48 | -999 |
- |
more |
kinetic isotope effects. The active form of the substrate is the dianion |
749953 |
3.1.3.48 | -999 |
- |
more |
kinetics of WPD loop insertion cysteine mutants, overview |
707476 |
3.1.3.48 | -999 |
- |
more |
Michaelis-Menten and Lineweaver-Burk kinetics |
751599 |
3.1.3.48 | -999 |
- |
more |
Michaelis-Menten kinetic modeling |
749934 |
3.1.3.48 | -999 |
- |
more |
Michaelis-Menten kinetics |
749850, 750047, 750465, 750490, 751508, 752091 |
3.1.3.48 | -999 |
- |
more |
Michaelis-Menten steady state kinetics with PTP pseudo-substrate 4-nitrophenyl phosphate |
714058 |
3.1.3.48 | -999 |
- |
more |
steady-state kinetic study, Lineweaver-Burk plots |
751130 |