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Literature summary for 3.6.1.23 extracted from

  • Zhang, Y.; Moriyama, H.; Homma, K.; Van Etten, J.L.
    Chlorella virus-encoded deoxyuridine triphosphatases exhibit different temperature optima (2005), J. Virol., 79, 9945-9953.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) Paramecium bursaria Chlorella virus 1

Inhibitors

Inhibitors Comment Organism Structure
dUTP substrate inhibition at higher concentrations Paramecium bursaria Chlorella virus 1
additional information no inhibition by dTTp, dGTP, dATP, and dCTP Paramecium bursaria Chlorella virus 1

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0117
-
dUTP pH 8.5, 50°C, recombinant enzyme Paramecium bursaria Chlorella virus 1

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ best divalent cation, bound at the center of the trimeric enzyme structure Paramecium bursaria Chlorella virus 1

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
54000
-
recombinant His-tagged enzyme, native PAGE Paramecium bursaria Chlorella virus 1
176000
-
3 * 176000, recombinant His-tagged enzyme, SDS-PAGE Paramecium bursaria Chlorella virus 1

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
dUTP + H2O Paramecium bursaria Chlorella virus 1 dUMP is required for biosynthesis of dTTP, overview dUMP + diphosphate
-
?

Organism

Organism UniProt Comment Textmining
Paramecium bursaria Chlorella virus 1
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Paramecium bursaria Chlorella virus 1

Reaction

Reaction Comment Organism Reaction ID
dUTP + H2O = dUMP + diphosphate active site structure, R84 and S81 are involved in substrate binding, molecular modeling Paramecium bursaria Chlorella virus 1

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Paramecium bursaria Chlorella virus 1
23.9
-
purified recombinant enzyme Paramecium bursaria Chlorella virus 1

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dUTP + H2O dUMP is required for biosynthesis of dTTP, overview Paramecium bursaria Chlorella virus 1 dUMP + diphosphate
-
?
dUTP + H2O the enzyme is highly specific for dUTP Paramecium bursaria Chlorella virus 1 dUMP + diphosphate
-
?

Subunits

Subunits Comment Organism
More molecular structure modeling Paramecium bursaria Chlorella virus 1
trimer 3 * 176000, recombinant His-tagged enzyme, SDS-PAGE Paramecium bursaria Chlorella virus 1

Synonyms

Synonyms Comment Organism
deoxyuridine triphosphatase
-
Paramecium bursaria Chlorella virus 1
dUTPase
-
Paramecium bursaria Chlorella virus 1

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
50
-
-
Paramecium bursaria Chlorella virus 1

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
25 65 active range Paramecium bursaria Chlorella virus 1

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
6.8
-
dUTP pH 8.5, 50°C, recombinant enzyme Paramecium bursaria Chlorella virus 1

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
-
Paramecium bursaria Chlorella virus 1

pH Range

pH Minimum pH Maximum Comment Organism
2 11 active range Paramecium bursaria Chlorella virus 1