EC Number |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
---|
2.7.7.18 | -999 |
- |
more |
4.82 Vmax/KM NMN |
676525 |
2.7.7.18 | -999 |
- |
more |
7.16 Vmax/KM NaMN |
676525 |
2.7.7.18 | -999 |
- |
more |
Michaelis-Menten kinetics are observed for NMN and ATP, but saturation is not accomplished with NAMN, implying low affinity yet detectable activity with this substrate. Double-reciprocal plots show no cooperativity for this enzyme |
737783 |
2.7.7.18 | -999 |
- |
more |
steady-state kinetic analysis, sequential kinetic mechanism, bisubstrate enzyme kinetics, overview |
738672 |
2.7.7.18 | 0.0017 |
- |
ATP |
- |
703814 |
2.7.7.18 | 0.0045 |
- |
deamido-NAD+ |
37°C, pH 7.5 |
642778 |
2.7.7.18 | 0.006 |
- |
ATP |
pH 7.5, 37°C, recombinant mutant K47A |
738672 |
2.7.7.18 | 0.0068 |
- |
deamido-NAD+ |
37°C, pH 7.4 |
642935 |
2.7.7.18 | 0.011 |
- |
ATP |
pH 7.5, 37°C, recombinant mutant T86A |
738672 |
2.7.7.18 | 0.011 |
- |
ATP |
pH 7.5, 37°C, recombinant mutant W45A |
738672 |