EC Number |
Turnover Number Minimum [1/s] |
Turnover Number Maximum [1/s] |
Substrate |
Reference |
---|
2.4.2.12 | 0.0003 |
- |
ATP |
ATPase activity is decreased in simultaneous presence of 1 mM of substrates of forward and reverse NAMPT reaction |
690900 |
2.4.2.12 | 0.00137 |
- |
nicotinamide |
+/-0.00002, KM/kcat = 1600 1/M*s, pH 7.5, 100 microM PRPP, 88 nM NAMPT |
690900 |
2.4.2.12 | 0.00142 |
- |
nicotinamide |
+/-0.00002, in presence of 2 mM phosphate, KM/kcat = 6100 1/M*s, pH 7.5, 100 microM PRPP, 88 nM NAMPT |
690900 |
2.4.2.12 | 0.00183 |
- |
ATP |
ATPase (ATP hydrolysis) activity of the free NAMPT, 2 mM ATP |
690900 |
2.4.2.12 | 0.00617 |
- |
ATP |
ATPase activity is enhanced in presence of 1 mM nicotinamide, 2 mM ATP |
690900 |
2.4.2.12 | 0.00767 |
- |
nicotinamide |
+/-0.00150, in presence of 2 mM ATP the catalytic efficiency (KM/kcat = 1800000 1/M*s) is improved 1100-fold, pH 7.5, 100 microM PRPP, 88 nM NAMPT |
690900 |
2.4.2.12 | 0.015 |
- |
ATP |
ADP-ATP radiolabel exchange in absence of other reactants (without NMN synthesis), formation or hydrolysis of phospho-NAMPT may be rate limiting for overall NMN synthesis reaction in presence of ATP |
690900 |
2.4.2.12 | 0.0183 |
- |
ATP |
ATPase activity is enhanced in presence of 1 mM diphosphate, presence of PRPP and/or nicotinamide reverses stimulation by diphosphate, 2 mM ATP |
690900 |
2.4.2.12 | 0.02 |
- |
nicotinamide |
pH 7.4, 37°C, recombinant enzyme |
662306 |
2.4.2.12 | 0.0433 |
- |
ATP |
ATPase activity in presence of 1 mM imidodiphosphate (PNP) is higher than in presence of pyophosphate, 2 mM ATP |
690900 |