1.1.1.87	additional information	-	additional information	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	additional information	-	additional information	mutant enzymes kinetic analysis and pH-dependencies, overview	696350	
1.1.1.87	additional information	-	additional information	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	696220	
1.1.1.87	0.0042	-	homoisocitrate	oxidate decarboxylation of homoisocitrate	685232	
1.1.1.87	0.0073	-	homoisocitrate	wild type enzyme, with NAD+ as cosubstrate, at pH 8.0 and 60°C	760522	
1.1.1.87	0.01	-	homoisocitrate	value below	644539	
1.1.1.87	0.014	-	isocitrate	wild type enzyme, with NAD+ as cosubstrate, at pH 8.0 and 60°C	760522	
1.1.1.87	0.0164	-	isocitrate	pH 7.8, 70°C, recombinant enzyme	660907	
1.1.1.87	0.018	-	homoisocitrate	-	685539	
1.1.1.87	0.018	-	homoisocitrate	pH 7.8, 36°C, recombinant enzyme	667934