Literature summary for 3.6.1.23 extracted from

Dominguez-Perez, I.; Tellez-Sanz, R.; Leal, I.; Ruiz-Perez, L.M.; Gonzalez-Pacanowska, D.; Garcia-Fuentes, L.
Calorimetric determination of thermodynamic parameters of 2-dUMP binding to Leishmania major dUTPase (2004), Biochim. Biophys. Acta, 1702, 33-40.

Search for more literature for 3.6.1.23

Cloned(Commentary)

Cloned (Comment)	Organism
overexpression in Escherichia coli strain BL21	Leishmania major

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	non-cooperative binding to 2'-dUMP, 1 molecule per enzyme subunit, kinetics and thermodynamics from isothermal titration microcalorimetry under different conditions, overview	Leishmania major

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	-	Leishmania major

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
30300	-	2 * 30300, recombinant enzyme, SDS-PAGE	Leishmania major

Organism

Organism	UniProt	Comment	Textmining
Leishmania major	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant enzyme from Escherichia coli strain BL21 by hydroxyapatite and anion exchange chromatography	Leishmania major

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	the enzyme binds non-cooperatively to 2'-dUMP	Leishmania major	?	-	?

Subunits

Subunits	Comment	Organism
dimer	2 * 30300, recombinant enzyme, SDS-PAGE	Leishmania major

Synonyms

Synonyms	Comment	Organism
deoxyuridine 5'-triphosphate nucleotide hydrolase	-	Leishmania major
dUTPase	-	Leishmania major

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
25	-	assay at	Leishmania major

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
8	-	assay at	Leishmania major

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Release 2023.1 (January 2023)