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Results 1 - 10 of 10
EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.120.0003 - ATP ATPase activity is decreased in simultaneous presence of 1 mM of substrates of forward and reverse NAMPT reaction 690900
Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.120.00137 - nicotinamide +/-0.00002, KM/kcat = 1600 1/M*s, pH 7.5, 100 microM PRPP, 88 nM NAMPT 690900
Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.120.00142 - 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
Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.120.00183 - ATP ATPase (ATP hydrolysis) activity of the free NAMPT, 2 mM ATP 690900
Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.120.00617 - ATP ATPase activity is enhanced in presence of 1 mM nicotinamide, 2 mM ATP 690900
Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.120.00767 - 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
Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.120.015 - 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
Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.120.0183 - 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
Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.120.02 - nicotinamide pH 7.4, 37°C, recombinant enzyme 662306
Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.120.0433 - ATP ATPase activity in presence of 1 mM imidodiphosphate (PNP) is higher than in presence of pyophosphate, 2 mM ATP 690900
Results 1 - 10 of 10