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Results 1 - 10 of 357 > >>
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Reference
-999
-
more
assay methods for both directions of reaction
-999
-
more
lower Km of the Thermotoga maritima acetate kinase for acetate measured than that determined by earlier assay methods
-999
-
more
Michaelis-Menten kinetics
-999
-
more
Michaelis-Menten kinetics, kinetic analysis and mechanism, detailed overview
-999
-
more
Michaelis-Menten kinetics, thermodynamics
-999
-
more
the dependence of the activity on acetate and acetyl phosphate concentrations obeys the Michaelis-Menten kinetics, whereas the dependence on ATP and ADP concentrations is sigmoidal
-999
-
more
the turnover number of AckA1 is about an order of magnitude higher than that of AckA2 for the reaction in either direction. The Km values for acetyl phosphate, ATP, and ADP are similar for both isozymes. AckA2 has a higher affinity for acetate than does AckA1. Michaelis-Menten kinetics; the turnover number of AckA1 is about an order of magnitude higher than that of AckA2 for the reaction in either direction. The Km values for acetyl phosphate, ATP, and ADP are similar for both isozymes. AckA2 has a higher affinity for acetate than does AckA1. Michaelis-Menten kinetics
0.0026
-
acetyl phosphate
carried out at various temperatures
0.016
-
ATP
mutant R91A, pH 7.0
0.0499
-
ATP
mutant V93A, pH 7.0
Results 1 - 10 of 357 > >>