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Results 1 - 10 of 39 > >>
EC Number KM Value [mM] KM Value Maximum [mM] Substrate Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.7-999 - more free energy profiles for reactions of wild-type and mutated enzymes, and steady-state kinetic analysis, overview 719505
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.7-999 - more kinetic mechanism for transglucosylation to external acceptors catalyzed by sucrose phosphorylase under conditions in which the natural acceptor substrate phosphate is absent, overview 720267
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.7-999 - more kinetics 680980
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.7-999 - more kinetics of recombinant wild-type and mutant enzymes, overview 686739
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.7-999 - more kinetics, calculated Km of D-glucose 1-phosphate formation and release of D-fructose are 3.88 mM and 5.56 mM 704230
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.7-999 - more Michaelis-Menten kinetics 735804
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.7-999 - more steady-state kinetic analysis, ping-pong kinetics 703198
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.7-999 - more steady-state kinetics of wild-type and mutant E237Q enzymes 684969
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.7-999 - more the enzyme exhibits Michaelis-Menten kinetics, overview 721112
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.72 - phosphate - 637844
Results 1 - 10 of 39 > >>