EC Number   |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
|---|
    2.1.3.2 | -999 |
- |
more |
- |
485872 |
| 2.1.3.2 | -999 |
- |
more |
allosteric mechanism with metal ion involvement, overview |
718943 |
| 2.1.3.2 | -999 |
- |
more |
aspartate transcarbamoylase is an allosteric enzyme, quaternary structural changes during the allosteric transition, and kinetics of the allosteric transition, overview |
718699 |
| 2.1.3.2 | -999 |
- |
more |
enzyme exhibits Michaelis-Menten kinetics for both of its substrates |
485872 |
| 2.1.3.2 | -999 |
- |
more |
Michaelis-Menten kinetics |
737205 |
| 2.1.3.2 | -999 |
- |
more |
sigmoidal saturation curve for aspartate |
485879, 485881 |
| 2.1.3.2 | -999 |
- |
more |
sigmoidal saturation curve for carbamoylphosphate and aspartate |
485869 |
| 2.1.3.2 | -999 |
- |
more |
study of enzyme kinetics under high pressure, in presence of low concentration of L-aspartate, pressure promotes the transition to R-state |
661450 |
| 2.1.3.2 | -999 |
- |
more |
the allosteric enzyme shows homotropic cooperative interactions between the catalytic sites for the binding of aspartate, neuron scattering, protein dynamics, overview |
672392 |
| 2.1.3.2 | -999 |
- |
more |
the saturation curve is cooperative exhibiting a pH dependent Hill coefficient, cooperative kinetics, modeling with the enzyme being in a dynamic equilibrium between a low-activity, low-affinity T state and a high-activity, high-affinity R state |
718458 |
