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Literature summary for 3.6.1.23 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.
    View publication on PubMed

Protein Variants

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

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 [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

Metals/Ions Comment Organism Structure
Mg2+ activates Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P06968
-
-

Subunits

Subunits Comment Organism
dimer
-
Escherichia coli
trimer
-
Escherichia coli

Synonyms

Synonyms Comment Organism
dUTPase
-
Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
5.8 6.2 dUTP
-
Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Escherichia coli

pH Range

pH Minimum pH Maximum Comment Organism
6.5 8.5
-
Escherichia coli

Ki Value [mM]

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