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EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Reference
1.1.1.87
0.018
-
homoisocitrate
-
685539
1.1.1.87
0.02
-
trisodium (2S,3R)-2-(carboxylatomethoxy)-3-hydroxybutanedioate
-
685539
1.1.1.87
0.065
-
NADH
-
644539
1.1.1.87
0.15
-
trisodium (2S,3R)-2-[(carboxylatomethyl)amino]-3-hydroxybutanedioate
-
685539
1.1.1.87
0.33
-
NAD+
-
644539
1.1.1.87
1.4
-
3-carboxy-2-hydroxyadipate
-
644543
1.1.1.87
1.4
-
homoisocitric acid
-
644541
1.1.1.87
1.5
-
alpha-ketoadipate
-
644539
1.1.1.87
-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
739958
1.1.1.87
0.64
-
NAD+
mutant enzyme I82N, with homoisocitrate as cosubstrate, at pH 8.0 and 60°C
760522
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