3.6.1.23	additional information	-	additional information	detailed pre-steady-state and steady-state kinetic analysis, quantitative kinetic model of the human dUTPase catalytic cycle, overview	687636	
3.6.1.23	additional information	-	additional information	kinetics of dUTP binding	670432	
3.6.1.23	additional information	-	additional information	ligand binding constants	689949	
3.6.1.23	additional information	-	additional information	lower affinity for dUTP than strict dUTPases	648212	
3.6.1.23	additional information	-	additional information	Michaelis-Menten and ligand binding kinetics, overview. Thermodynamic parameters for the interaction between Plasmodium falciparum dUTPase and deoxyuridine derivatives at 25.2 °C and pH 7.0	696412	
3.6.1.23	additional information	-	additional information	Michaelis-Menten kinetics, kinetics analysis	699236	
3.6.1.23	additional information	-	additional information	non-cooperative binding to 2'-dUMP, 1 molecule per enzyme subunit, kinetics and thermodynamics from isothermal titration microcalorimetry under different conditions, overview	667783	
3.6.1.23	additional information	-	additional information	steady-state kinetic analysis of the dual activities of the bifunctional enzyme, overview	688399	
3.6.1.23	additional information	-	additional information	transient state kinetics of substrate binding to the S72A mutant dUTPase, stopped-flow measurements, overview. Comparative kinetics of formation of the enzyme-substrate complexes of the wild-type and S72A	696282	
3.6.1.23	0.0001	-	dUTP	-	209966