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Results 1 - 10 of 44 > >>
EC Number KM Value [mM] KM Value Maximum [mM] Substrate Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.20-999 - more - 486497
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.20-999 - more acyl-CoA substrate binding kinetics of the recombinant N-terminal fragment, overview 672791
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.20-999 - more isozyme BnaC.DGAT1.a exhibits positive cooperativity. The folded section of the enzyme is important to maintain high acyl-CoA affinity at the active site and activity. Kinetics of wild-type and enzyme mutants, Michaelis-Menten kinetic model 758047
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.20-999 - more kinetic analysis of lipidated BnaDGAT1. BnaDGAT1 exhibits cooperative substrate binding behavior with oleoyl-CoA 758018
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.20-999 - more kinetics of wax synthase activity, overview 756245
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.20-999 - more Michaelis-Menten kinetics 757051, 757183
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.20-999 - more Michaelis-Menten or allosteric sigmoidal kinetics 757545
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.20-999 - more the flux control coefficient is 0.12 in oil palm 673535
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.20-999 - more the flux control coefficient is 0.74 in olive 673535
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.20-999 - more the N-terminal regions of Brassica napus DGAT1 enzymes binds acyl-CoA in a sigmoidal fashion, suggesting positive cooperative binding 757544
Results 1 - 10 of 44 > >>