Refine search

Search KM Value [mM]

show results
Don't show organism specific information (fast!)
Search organism in taxonomic tree (slow, choose "exact" as search mode, e.g. "mammalia" for rat,human,monkey,...)
(Not possible to combine with the first option)
Refine your search
Image of 2D Structure

Search term:

Results 1 - 10 of 57 > >>
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Reference
-999
-
more
Michaelis-Menten kinetics, the enzyme shows a steady-state random kinetic mechanism with a preferred order of addition of Mg2+ prior to NAD+. The same step(s) limit the reaction at limiting and saturating Mg2+ concentrations. Solvent kinetic deuterium isotope effects and viscosity effects are consistent with a rate-limiting pre-catalytic conformational change at saturating reactant concentrations
-999
-
more
mutant enzymes kinetic analysis and pH-dependencies, overview
-999
-
more
substitution of potassium acetate for KCl changes the kinetic mechanism of HIcDH from a steady state random to a fully ordered mechanism with the binding of Mg-HIc followed by K+ and NAD+, increase in the affinity of enzyme for Mg-HIc as a result of elimination of the inhibitory effect of Cl-, kinetic analysis, overview
0.0042
-
Mg-homoisocitrate
oxidate decarboxylation of homoisocitrate
0.01
-
homoisocitrate
value below
0.0164
-
isocitrate
pH 7.8, 70°C, recombinant enzyme
0.018
-
homoisocitrate
-
0.018
-
homoisocitrate
pH 7.8, 36°C, recombinant enzyme
0.0183
-
homoisocitrate
pH 7.8, 70°C, recombinant enzyme
0.02
-
trisodium (2S,3R)-2-(carboxylatomethoxy)-3-hydroxybutanedioate
-
Results 1 - 10 of 57 > >>