EC Number |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
---|
6.3.5.4 | -999 |
- |
more |
- |
1673 |
6.3.5.4 | -999 |
- |
more |
biphasic kinetic, linear portion near 0.5 |
861 |
6.3.5.4 | -999 |
- |
more |
kinetic mechanism, kinetic model |
649482 |
6.3.5.4 | -999 |
- |
more |
Km-values of a number of site-specific mutant enzymes |
1701 |
6.3.5.4 | -999 |
- |
more |
Km-values of mutant enzymes R30A, R30K, N74A, N74Q, and N79A |
1700 |
6.3.5.4 | -999 |
- |
more |
regulation: coregulation by light of the activities of three crucial enzymes of NH4+ assimilation and transport |
1704 |
6.3.5.4 | -999 |
- |
more |
steady-state kinetics |
746172 |
6.3.5.4 | -999 |
- |
more |
the AsnS isozymes are kinetically distinct with substantial differences in Km (Gln) and Vmax values, overview. None of the enzymes has cooperative enzyme kinetics |
716573 |
6.3.5.4 | 0.013 |
- |
ATP |
mutant E348D, glutamine-dependent activity, pH 8.0, 37°C |
714228 |
6.3.5.4 | 0.013 |
- |
ATP |
mutant E348D, synthetase activity, glutamine-dependent activity, 20 mM L-Gln, pH 8.0, 37°C |
714228 |