EC Number |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
---|
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 |
3.6.1.23 | -999 |
- |
more |
kinetics of dUTP binding |
670432 |
3.6.1.23 | -999 |
- |
more |
ligand binding constants |
689949 |
3.6.1.23 | -999 |
- |
more |
lower affinity for dUTP than strict dUTPases |
648212 |
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 |
3.6.1.23 | -999 |
- |
more |
Michaelis-Menten kinetics, kinetics analysis |
699236 |
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 |
3.6.1.23 | -999 |
- |
more |
steady-state kinetic analysis of the dual activities of the bifunctional enzyme, overview |
688399 |
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 |
3.6.1.23 | 0.0001 |
- |
dUTP |
- |
209966 |