Literature summary extracted from
Palmen, L.G.; Becker, K.; Buelow, L.; Kvassman, J.O.
A double role for a strictly conserved serine: further insights into the dUTPase catalytic mechanism (2008), Biochemistry, 47, 7863-7874.
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
3.6.1.23 |
D90N |
site-directed mutagenesis |
Escherichia coli |
3.6.1.23 |
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
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
3.6.1.23 |
alpha,beta-imido-dUTP |
substrate analogue, inhibits the wild-type enzyme, not mutant S72A |
Escherichia coli |
|
3.6.1.23 |
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]
EC Number |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Comment |
Organism |
Structure |
---|
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 |
Escherichia coli |
|
Metals/Ions
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
3.6.1.23 |
Mg2+ |
activates |
Escherichia coli |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
3.6.1.23 |
Escherichia coli |
P06968 |
- |
- |
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
3.6.1.23 |
dimer |
- |
Escherichia coli |
3.6.1.23 |
trimer |
- |
Escherichia coli |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
3.6.1.23 |
dUTPase |
- |
Escherichia coli |
Temperature Optimum [°C]
EC Number |
Temperature Optimum [°C] |
Temperature Optimum Maximum [°C] |
Comment |
Organism |
---|
3.6.1.23 |
25 |
- |
assay at |
Escherichia coli |
Turnover Number [1/s]
EC Number |
Turnover Number Minimum [1/s] |
Turnover Number Maximum [1/s] |
Substrate |
Comment |
Organism |
Structure |
---|
3.6.1.23 |
5.8 |
6.2 |
dUTP |
- |
Escherichia coli |
|
pH Optimum
EC Number |
pH Optimum Minimum |
pH Optimum Maximum |
Comment |
Organism |
---|
3.6.1.23 |
7.5 |
- |
assay at |
Escherichia coli |
pH Range
EC Number |
pH Minimum |
pH Maximum |
Comment |
Organism |
---|
3.6.1.23 |
6.5 |
8.5 |
- |
Escherichia coli |
Ki Value [mM]
EC Number |
Ki Value [mM] |
Ki Value maximum [mM] |
Inhibitor |
Comment |
Organism |
Structure |
---|
3.6.1.23 |
0.0039 |
- |
alpha,beta-imido-dUTP |
pH 7.5, 25°C, wild-type enzyme |
Escherichia coli |
|