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Results 1 - 10 of 74 > >>
EC Number KM Value [mM] KM Value Maximum [mM] Substrate Commentary Reference
Show all pathways known for 2.7.7.18Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.18-999 - more 4.82 Vmax/KM NMN 676525
Show all pathways known for 2.7.7.18Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.18-999 - more 7.16 Vmax/KM NaMN 676525
Show all pathways known for 2.7.7.18Display the word mapDisplay the reaction diagram Show all sequences 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
Show all pathways known for 2.7.7.18Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.18-999 - more steady-state kinetic analysis, sequential kinetic mechanism, bisubstrate enzyme kinetics, overview 738672
Show all pathways known for 2.7.7.18Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.180.0017 - ATP - 703814
Show all pathways known for 2.7.7.18Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.180.0045 - deamido-NAD+ 37┬░C, pH 7.5 642778
Show all pathways known for 2.7.7.18Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.180.006 - ATP pH 7.5, 37┬░C, recombinant mutant K47A 738672
Show all pathways known for 2.7.7.18Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.180.0068 - deamido-NAD+ 37┬░C, pH 7.4 642935
Show all pathways known for 2.7.7.18Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.180.011 - ATP pH 7.5, 37┬░C, recombinant mutant T86A 738672
Show all pathways known for 2.7.7.18Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.180.011 - ATP pH 7.5, 37┬░C, recombinant mutant W45A 738672
Results 1 - 10 of 74 > >>