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Results 1 - 10 of 133 > >>
EC Number KM Value [mM] KM Value Maximum [mM] Substrate Commentary Reference
Show all pathways known for 3.6.1.23Display the word mapDisplay the reaction diagram Show all sequences 3.6.1.23-999 - more detailed pre-steady-state and steady-state kinetic analysis, quantitative kinetic model of the human dUTPase catalytic cycle, overview 687636
Show all pathways known for 3.6.1.23Display the word mapDisplay the reaction diagram Show all sequences 3.6.1.23-999 - more kinetics of dUTP binding 670432
Show all pathways known for 3.6.1.23Display the word mapDisplay the reaction diagram Show all sequences 3.6.1.23-999 - more ligand binding constants 689949
Show all pathways known for 3.6.1.23Display the word mapDisplay the reaction diagram Show all sequences 3.6.1.23-999 - more lower affinity for dUTP than strict dUTPases 648212
Show all pathways known for 3.6.1.23Display the word mapDisplay the reaction diagram Show all sequences 3.6.1.23-999 - more 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
Show all pathways known for 3.6.1.23Display the word mapDisplay the reaction diagram Show all sequences 3.6.1.23-999 - more Michaelis-Menten kinetics, kinetics analysis 699236
Show all pathways known for 3.6.1.23Display the word mapDisplay the reaction diagram Show all sequences 3.6.1.23-999 - more non-cooperative binding to 2'-dUMP, 1 molecule per enzyme subunit, kinetics and thermodynamics from isothermal titration microcalorimetry under different conditions, overview 667783
Show all pathways known for 3.6.1.23Display the word mapDisplay the reaction diagram Show all sequences 3.6.1.23-999 - more steady-state kinetic analysis of the dual activities of the bifunctional enzyme, overview 688399
Show all pathways known for 3.6.1.23Display the word mapDisplay the reaction diagram Show all sequences 3.6.1.23-999 - more 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
Show all pathways known for 3.6.1.23Display the word mapDisplay the reaction diagram Show all sequences 3.6.1.230.0001 - dUTP - 209966
Results 1 - 10 of 133 > >>