4.1.3.1	additional information	-	additional information	Michaelis-Menten kinetics of wild-type and mutant enzyme's overview	728845	
4.1.3.1	additional information	-	additional information	stopped-flow spectroscopy and steady-state kinetics, solvent kinetic isotope effects, overview. Whereas the D2OV is consistent with partially rate-limiting proton transfer during formation of the hydroxyl group of isocitrate, the large inverse D2O(V/Ksuccinate) indicates that substantially different kinetic parameters exist when the enzyme is saturated with succinate	727045	
4.1.3.1	0.008	-	threo-Ds-isocitrate	-	33115	
4.1.3.1	0.014	-	glyoxylate	-	33137	
4.1.3.1	0.015	-	DL-isocitrate	-	33115	
4.1.3.1	0.0157	-	isocitrate	pH 6.5	653476	
4.1.3.1	0.016	-	isocitrate	pH 7.5, 25°C	713812	
4.1.3.1	0.018	-	Ds-isocitrate	pH 6.8	33116	
4.1.3.1	0.018	-	threo-Ds-isocitrate	-	33124	
4.1.3.1	0.02	-	threo-Ds-isocitrate	25 mM imidazole buffer, pH 6.8	33135