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Results 1 - 10 of 186 > >>
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Reference
-999
-
more
activity is dependent on the ionic strength of the buffer and diminishes considerably (approximately 80%) when assayed in buffers with less than 100 mM concentrations. At concentrations higher than 100 mM the activity levels are quite similar (tested up to 500 mM); Michaelis-Menten steady-state kinetic analysis, overview
-999
-
more
binding kinetics of Mg2+ and thiamine diphosphate with wild-type enzyme and mutant enzymes, overview
-999
-
more
cofactor affinities of wild-type and mutant enzymes, overview
-999
-
more
kinetics
-999
-
more
kinetics of isozymes
-999
-
more
kinetics of wild-type and mutant enzymes
-999
-
more
kinetics or recombinant wild-type and reconstituted isozymes AHAS I, exclusive binding model
-999
-
more
Michaelis-Menten kinetics and optimal reaction conditions, overview
-999
-
more
non-hyperbolic substrate-saturation curve, involving interaction between the active sites of the dimer
-999
-
more
steady-state kinetics at different reaction conditions
Results 1 - 10 of 186 > >>