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Results 1 - 10 of 107 > >>
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Reference
-999
-
Chorismic acid
Competetive inhibition by I – IV Structur: increase the Km
-999
-
more
A lower Km of 0.5 +/-0.05 mM is obtained with a 27.5 nM protein concentration (11 pmol) whereas a Km of 0.67 +/-0.05 nM is obtained with a 8 nM protein concentration (3.2 pmol)
-999
-
more
due to instability of chorismate at higher temperature, a Km value is not determined
-999
-
more
Michaelis-Menten kinetics
-999
-
more
Michaelis-Menten kinetics; Michaelis-Menten kinetics
-999
-
more
Michaelis-Menten steady-state kinetics
-999
-
more
Michaelis-Menten steady-state kinetics; Michaelis-Menten steady-state kinetics
-999
-
more
sigmoid substrate saturation curve with S0.5: 16.7 mM for chorismate at 37°C and S0.5: 12 mM for chorismate at 37°C in presence of 0.1 mM tyrosine
-999
-
more
steady-state kinetics, isozyme AtCM1 shows Michaelis-Menten kinetics. Effect of aromatic amino acids on wild-type and mutant AtCM1, overview; steady-state kinetics, isozyme AtCM2, shows Michaelis-Menten kinetics; steady-state kinetics, isozyme AtCM3 displays positive cooperativity with a Hill coefficient of 2.1, indicating that substrate binding at one active site of the homodimer enhanced interaction at the second active site
-999
-
more
The Km of the active complementations (position 7, 32, 35, 48, 81 and 85) is shown
Results 1 - 10 of 107 > >>