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Literature summary for 3.6.1.23 extracted from

  • Larsson, G.; Nyman, P.O.; Kvassman, J.O.
    Kinetic characterization of dUTPase from Escherichia coli (1996), J. Biol. Chem., 271, 24010-24016.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00018
-
dUTP
-
Escherichia coli
0.016
-
dUTP
-
Escherichia coli
0.025
-
dUDP
-
Escherichia coli
0.13
-
dUDP
-
Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ Mg2+ enhances binding to dUTPase of dUTP by a factor of 100 and dUDP by a factor of 10 Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
dUTP + H2O Escherichia coli the enzyme prevents a deleterious incorporation of uracil into DNA ?
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Reaction

Reaction Comment Organism Reaction ID
dUTP + H2O = dUMP + diphosphate mechanism Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dUDP + H2O
-
Escherichia coli deoxyuridine + diphosphate
-
?
dUTP + H2O
-
Escherichia coli dUMP + diphosphate
-
?
dUTP + H2O the enzyme prevents a deleterious incorporation of uracil into DNA Escherichia coli ?
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
6 9 dUTP
-
Escherichia coli