EC Number   |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
|---|
    3.5.1.1 | -999 |
- |
L-asparagine |
kcat/Km: 66.41 1/mM*s, pH7.5, 37°C |
696012 |
| 3.5.1.1 | -999 |
- |
L-glutamine |
kcat/Km: 0.48 1/mM*s, pH7.5, 37°C |
696012 |
| 3.5.1.1 | -999 |
- |
more |
- |
208953, 208954 |
| 3.5.1.1 | -999 |
- |
more |
kinetic parameters of wild-type and chimeric ASPGA1 and -B1, overview |
720793 |
| 3.5.1.1 | -999 |
- |
more |
kinetics |
669561 |
| 3.5.1.1 | -999 |
- |
more |
Lineweaver-Burk and Michaelis-Menten kinetic analysis of activity, overview. Thiol compounds reduce the Km and increase the Vmax vlaues |
719379 |
| 3.5.1.1 | -999 |
- |
more |
Michaelis-Menten steady-state kinetics, overview |
720205 |
| 3.5.1.1 | -999 |
- |
more |
steady-state enzyme kinetics at different conditions of wild-type and mutant enzymes, overview |
719439 |
| 3.5.1.1 | -999 |
- |
more |
the Km of the immobilized enzyme is 8fold lower compared to the free enzyme |
667907 |
| 3.5.1.1 | -999 |
- |
more |
thermodynamic analysis, kinetic study and molecular modelling |
669556 |
