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Literature summary 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.6.1.23 0.00018
-
 dUTP
-
 Escherichia coli
3.6.1.23 0.016
-
 dUTP
-
 Escherichia coli
3.6.1.23 0.025
-
 dUDP
-
 Escherichia coli
3.6.1.23 0.13
-
 dUDP
-
 Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.6.1.23 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)

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

Organism

EC Number Organism UniProt Comment Textmining
3.6.1.23 Escherichia coli
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
3.6.1.23 dUTP + H2O = dUMP + diphosphate mechanism Escherichia coli
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.6.1.23 dUDP + H2O
-
 Escherichia coli deoxyuridine + diphosphate
-
 ?
3.6.1.23 dUTP + H2O
-
 Escherichia coli dUMP + diphosphate
-
 ?
3.6.1.23 dUTP + H2O the enzyme prevents a deleterious incorporation of uracil into DNA 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 6 9 dUTP
-
 Escherichia coli