2.2.1.6	additional information	-	additional information	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)	733241	
2.2.1.6	additional information	-	additional information	binding kinetics of Mg2+ and thiamine diphosphate with wild-type enzyme and mutant enzymes, overview	733987	
2.2.1.6	additional information	-	additional information	cofactor affinities of wild-type and mutant enzymes, overview	672866	
2.2.1.6	additional information	-	additional information	kinetics	671290, 671854, 673626	
2.2.1.6	additional information	-	additional information	kinetics of isozymes	673213	
2.2.1.6	additional information	-	additional information	kinetics of wild-type and mutant enzymes	674354	
2.2.1.6	additional information	-	additional information	kinetics or recombinant wild-type and reconstituted isozymes AHAS I, exclusive binding model	672368	
2.2.1.6	additional information	-	additional information	Michaelis-Menten kinetics and optimal reaction conditions, overview	733744	
2.2.1.6	additional information	-	additional information	Michaelis-Menten steady-state kinetic analysis, overview	733241	
2.2.1.6	additional information	-	additional information	non-hyperbolic substrate-saturation curve, involving interaction between the active sites of the dimer	395902