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Literature summary for 3.6.1.23 extracted from

  • Barabas, O.; Pongracz, V.; Kovari, J.; Wilmanns, M.; Vertessy, B.G.
    Structural insights into the catalytic mechanism of phosphate ester hydrolysis by dUTPase (2004), J. Biol. Chem., 279, 42907-42915.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
native and mutant enzyme Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging-drop vapor diffusion method Escherichia coli

Protein Variants

Protein Variants Comment Organism
D90N no effect on Km, strong decrease in catalytic activity, H-bonding significantly altered Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.45
-
dUTP D90N mutant enzyme, pH 7.8, room temperature Escherichia coli
0.5
-
dUTP wild-type enzyme, pH 7.8, room temperature Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
dUTP + H2O Escherichia coli removes dUTP from the nucleotide triphosphate pool and therefore prevents the incorporation of uracil into the DNA dUMP + diphosphate
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli P06968
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant proteins Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dUTP + H2O
-
Escherichia coli dUMP + diphosphate
-
?
dUTP + H2O removes dUTP from the nucleotide triphosphate pool and therefore prevents the incorporation of uracil into the DNA Escherichia coli dUMP + diphosphate
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.0003
-
dUTP D90N mutant enzyme, pH 7.8, room temperature Escherichia coli
11
-
dUTP wild-type enzyme, pH 7.8, room temperature Escherichia coli