EC Number   |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
|---|
   2.7.4.22 | -999 |
- |
more |
MPK exhibited Michaelis-Menten kinetics |
692284 |
| 2.7.4.22 | -999 |
- |
more |
reaction kinetics |
698858 |
| 2.7.4.22 | -999 |
- |
more |
steady-state kinetics, velocity curves for the enzyme fit to a steady state random Bi Bi mechanism or ordered Bi Bi mechanism. Data fits both models equally well |
737591 |
| 2.7.4.22 | -999 |
- |
more |
with ATP as the variable substrate, the kinetic curves show a detectable deviation from Michaelis-Menten kinetics, especially at low substrate concentrations, the best fit is therefore to the Hill equation, giving an n value of 1.54 +/- 0.10, demonstrating positive cooperativity with ATP, coupled spectrophotometric assay |
692284 |
| 2.7.4.22 | 0.0023 |
- |
UMP |
mutant enzyme P139H, at pH 7.4 and 30°C |
723289 |
| 2.7.4.22 | 0.00276 |
- |
UMP |
purified enzyme, in 50 mM Tris-HCl pH 7.4, at 30°C |
723708 |
| 2.7.4.22 | 0.00281 |
- |
UMP |
crude cytosolic extract, in 50 mM Tris-HCl pH 7.4, at 30°C |
723708 |
| 2.7.4.22 | 0.0034 |
- |
UMP |
mutant enzyme F81W/S96A, at pH 7.4 and 30°C |
723289 |
| 2.7.4.22 | 0.0061 |
- |
UMP |
mutant enzyme P139W, at pH 7.4 and 30°C |
723289 |
| 2.7.4.22 | 0.0066 |
- |
UMP |
mutant enzyme P139A, at pH 7.4 and 30°C |
723289 |
