1.1.1.49	additional information	-	additional information	-	286819, 286982, 286984, 286986, 286987, 286988, 286991, 286992, 286996, 286998, 287001, 655712	
1.1.1.49	additional information	-	additional information	hyperbolic kinetics versus D-glucose 6-phosphate	722212	
1.1.1.49	additional information	-	additional information	kinetics	657147	
1.1.1.49	additional information	-	additional information	kinetics and thermodynamics, rapid equilibrium random bi bi kinetic model	655736	
1.1.1.49	additional information	-	additional information	kinetics, kinetic mechanism analysis, ternary-complex mechanism, overview	674379	
1.1.1.49	additional information	-	additional information	Michaelis-Menten kinetics	723340	
1.1.1.49	additional information	-	additional information	ping pong bi bi kinetic mechanism	673156	
1.1.1.49	additional information	-	additional information	steady-state kinetics of wild-type and mutant enzymes	672382, 673944	
1.1.1.49	additional information	-	additional information	the initial velocity plots of the enzyme follow the Michaelis-Menten equation in the absence of NADH. In its presence, however, the velocity versus substrate plots for NADP+ become sigmoidal but remain hyperbolic for glucose 6-phosphate as the variable substrate. Inhibition against both of the substrates of the enzyme by NADH is noncompetitive. The inhibition curves for NADH are also sigmoidal, suggesting a multisite binding of the inhibitor on the enzyme surface	722577	
1.1.1.49	additional information	-	additional information	thermodynamics, steady-state kinetics	657284