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

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	a

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