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Results 1 - 10 of 25 > >>
EC Number KM Value [mM] KM Value Maximum [mM] Substrate Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 7.5.2.6-999 - more kinetics of the conformational change from ATP-bound T561C to the dynamic equilibrium during continuous ATP hydrolysis (in MgATP) by stopped flow measurements, kinetics of the conformational changes of mutant enzymes 751037
Display the word mapDisplay the reaction diagram Show all sequences 7.5.2.6-999 - more ligand binding kinetics 696114
Display the word mapDisplay the reaction diagram Show all sequences 7.5.2.6-999 - more lipid binding kinetics, overview 698746
Display the word mapDisplay the reaction diagram Show all sequences 7.5.2.6-999 - more Michaelis-Menten kinetics of MsbA ATPase activity 751020
Display the word mapDisplay the reaction diagram Show all sequences 7.5.2.60.002 - ATP pH 7.0, 37°C, mutant H537A 718898
Display the word mapDisplay the reaction diagram Show all sequences 7.5.2.60.005 - ATP pH 7.0, 37°C, mutant S423C/E506Q 718898
Display the word mapDisplay the reaction diagram Show all sequences 7.5.2.60.005 - ATP pH 7.0, 37°C, mutant S423C/H537A 718898
Display the word mapDisplay the reaction diagram Show all sequences 7.5.2.60.0064 - lipid A pH 7.5, 37°C, recombinant His-tagged enzyme 698746
Display the word mapDisplay the reaction diagram Show all sequences 7.5.2.60.012 - ATP pH 7.0, 37°C, mutant E506Q 718898
Display the word mapDisplay the reaction diagram Show all sequences 7.5.2.60.048 0.05 lipopolysaccharide pH 7.5, 37°C, recombinant His-tagged enzyme 698746
Results 1 - 10 of 25 > >>