Protein Variants | Comment | Organism |
---|---|---|
D90N | site-directed mutagenesis | Escherichia coli |
S72A | site-directed mutagenesis, steady-state kinetic characterization, S72A mutation causes a 725fold reduction in kcat and a 35fold reduction in KM. | Escherichia coli |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
alpha,beta-imido-dUTP | substrate analogue, inhibits the wild-type enzyme, not mutant S72A | Escherichia coli | |
guanidine hydrochloride | kinetics of GuHCl-induced denaturation of the two dUTPase isozymes at pH 7.5, 4 °C and 1.5-4 M | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
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 | Escherichia coli |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | activates | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P06968 | - |
- |
Subunits | Comment | Organism |
---|---|---|
dimer | - |
Escherichia coli |
trimer | - |
Escherichia coli |
Synonyms | Comment | Organism |
---|---|---|
dUTPase | - |
Escherichia coli |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Escherichia coli |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
5.8 | 6.2 | dUTP | - |
Escherichia coli |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Escherichia coli |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
6.5 | 8.5 | - |
Escherichia coli |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0039 | - |
alpha,beta-imido-dUTP | pH 7.5, 25°C, wild-type enzyme | Escherichia coli |