Literature summary for 3.6.1.23 extracted from
Tarbouriech, N.; Buisson, M.; Seigneurin, J.; Cusack, S.; Burmeister, W.P.
The monomeric dUTPase from Epstein-Barr virus mimics trimeric dUTPases (2006), Structure, 14, 623.
No PubMed abstract available
Application
Application |
Comment |
Organism |
pharmacology |
the enzyme is a potential target for antiviral drug design |
Human gammaherpesvirus 4 |
Cloned(Commentary)
Cloned (Comment) |
Organism |
gene BLLF3, overexpression of His-tagged enzyme in Escherichia coli |
Human gammaherpesvirus 4 |
Crystallization (Commentary)
Crystallization (Comment) |
Organism |
purified enzyme in complex with either product dUMPand Mg2+, or with substrate analogue alpha,beta-imino-dUTP, hanging drop vapour diffusion method, the reservoir solution contains 0.1 M Tris-HCl, pH 8.5, 20% PEG 3350, and 0.2 M LiSO4, a few weeks, soaking in europium nitrate solution, X-ray diffraction structure determination and analysis at 1.5A and 2.7 A resolution, respectively, single-wavelength anomalous diffraction |
Human gammaherpesvirus 4 |
KM Value [mM]
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Comment |
Organism |
Structure |
0.0007 |
- |
dUTP |
pH 7.6, 25°C, recombinant enzyme, in presence of 1 mM MgCl2 |
Human gammaherpesvirus 4 |
|
Metals/Ions
Metals/Ions |
Comment |
Organism |
Structure |
Mg2+ |
binding structure, Mg2+ does not bind in the active site |
Human gammaherpesvirus 4 |
|
Natural Substrates/ Products (Substrates)
Natural Substrates |
Organism |
Comment (Nat. Sub.) |
Natural Products |
Comment (Nat. Pro.) |
Rev. |
Reac. |
dUTP + H2O |
Human gammaherpesvirus 4 |
the enzyme is essential in the lytic cycle of the virus |
dUMP + diphosphate |
- |
? |
|
Organism
Organism |
UniProt |
Comment |
Textmining |
Human gammaherpesvirus 4 |
- |
EBV, strain B95-8, gene BLLF3 |
- |
Purification (Commentary)
Purification (Comment) |
Organism |
recombinant His-tagged enzyme from Escherichia coli by metal affinity chromatography, cleavage of the tag |
Human gammaherpesvirus 4 |
Reaction
Reaction |
Comment |
Organism |
Reaction ID |
dUTP + H2O = dUMP + diphosphate |
product and substrate active site binding structure, catalytic mechanism of the monomeric enzyme in comparison to trimeric dUTPases, overview |
Human gammaherpesvirus 4 |
|
Substrates and Products (Substrate)
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
dUTP + H2O |
the enzyme is essential in the lytic cycle of the virus |
Human gammaherpesvirus 4 |
dUMP + diphosphate |
- |
? |
|
dUTP + H2O |
the enzyme is highly specific for dUTP |
Human gammaherpesvirus 4 |
dUMP + diphosphate |
- |
? |
|
Subunits
Subunits |
Comment |
Organism |
monomer |
overall enzyme fold, the enzyme contains five characteristic sequence motifs and one active site, three-domain structural organization and secondary structure, overview |
Human gammaherpesvirus 4 |
Synonyms
Synonyms |
Comment |
Organism |
deoxyuridine 5'-triphosphate pyrophosphatase |
- |
Human gammaherpesvirus 4 |
dUTPase |
- |
Human gammaherpesvirus 4 |
Temperature Optimum [°C]
Temperature Optimum [°C] |
Temperature Optimum Maximum [°C] |
Comment |
Organism |
25 |
- |
assay at |
Human gammaherpesvirus 4 |
Turnover Number [1/s]
Turnover Number Minimum [1/s] |
Turnover Number Maximum [1/s] |
Substrate |
Comment |
Organism |
Structure |
3.3 |
- |
dUTP |
pH 7.6, 25°C, recombinant enzyme, in presence of 1 mM MgCl2 |
Human gammaherpesvirus 4 |
|
pH Optimum
pH Optimum Minimum |
pH Optimum Maximum |
Comment |
Organism |
7.6 |
- |
assay at |
Human gammaherpesvirus 4 |