EC Number |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
---|
5.4.99.5 | -999 |
- |
Chorismic acid |
Competetive inhibition by I IV Structur: increase the Km |
672622 |
5.4.99.5 | -999 |
- |
more |
A lower Km of 0.5 +/-0.05 mM is obtained with a 27.5 nM protein concentration (11 pmol) whereas a Km of 0.67 +/-0.05 nM is obtained with a 8 nM protein concentration (3.2 pmol) |
674312 |
5.4.99.5 | -999 |
- |
more |
due to instability of chorismate at higher temperature, a Km value is not determined |
692260 |
5.4.99.5 | -999 |
- |
more |
Michaelis-Menten kinetics |
747259, 749355 |
5.4.99.5 | -999 |
- |
more |
Michaelis-Menten steady-state kinetics |
747032 |
5.4.99.5 | -999 |
- |
more |
sigmoid substrate saturation curve with S0.5: 16.7 mM for chorismate at 37°C and S0.5: 12 mM for chorismate at 37°C in presence of 0.1 mM tyrosine |
651660 |
5.4.99.5 | -999 |
- |
more |
steady-state kinetics, isozyme AtCM1 shows Michaelis-Menten kinetics. Effect of aromatic amino acids on wild-type and mutant AtCM1, overview |
748178 |
5.4.99.5 | -999 |
- |
more |
steady-state kinetics, isozyme AtCM2, shows Michaelis-Menten kinetics |
748178 |
5.4.99.5 | -999 |
- |
more |
steady-state kinetics, isozyme AtCM3 displays positive cooperativity with a Hill coefficient of 2.1, indicating that substrate binding at one active site of the homodimer enhanced interaction at the second active site |
748178 |
5.4.99.5 | -999 |
- |
more |
The Km of the active complementations (position 7, 32, 35, 48, 81 and 85) is shown |
672268 |