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Literature summary for 3.6.1.23 extracted from

  • Quesada-Soriano, I.; Leal, I.; Casas-Solvas, J.M.; Vargas-Berenguel, A.; Baron, C.; Ruiz-Perez, L.M.; Gonzalez-Pacanowska, D.; Garcia-Fuentes, L.
    Kinetic and thermodynamic characterization of dUTP hydrolysis by Plasmodium falciparum dUTPase (2008), Biochim. Biophys. Acta, 1784, 1347-1355.
    View publication on PubMed

Application

Application Comment Organism
drug development the enzyme is a potential drug target against malaria Plasmodium falciparum

Cloned(Commentary)

Cloned (Comment) Organism
expression of the recombinant enzyme Plasmodium falciparum

Inhibitors

Inhibitors Comment Organism Structure
2'-deoxyuridine competitive inhibition Plasmodium falciparum
alpha,beta-imido-dUTP competitive inhibition Plasmodium falciparum
dUDP competitive inhibition Plasmodium falciparum
dUMP product, competitive inhibition Plasmodium falciparum
dUTP
-
Plasmodium falciparum
EDTA causes a 105fold decrease and a 12fold increase of the kcat and Km values for dUTP hydrolysis, respectively, compared to the dUTP-Mg2+ complex Plasmodium falciparum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information Michaelis-Menten and ligand binding kinetics, overview. Thermodynamic parameters for the interaction between Plasmodium falciparum dUTPase and deoxyuridine derivatives at 25.2 °C and pH 7.0 Plasmodium falciparum
0.0019
-
dUTP pH 7.0, 25°C, recombinant enzyme Plasmodium falciparum
0.0019
-
dUTP-Mg2+ pH 7.0, 25°C, recombinant enzyme Plasmodium falciparum
0.0027
-
dUTP-Co2+ pH 7.0, 25°C, recombinant enzyme Plasmodium falciparum
0.0137
-
dUTP-Mn2+ pH 7.0, 25°C, recombinant enzyme Plasmodium falciparum

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ can substitute the physiological cofactor Mg2+, however the kcat is significantly reduced compared to dUTP-Mg2+ Plasmodium falciparum
Mg2+ dependent on, the energetic barrier of the reaction is 4fold higher when Mg2+ is depleted Plasmodium falciparum
Mn2+ can substitute the physiological cofactor Mg2+, however the kcat is significantly reduced compared to dUTP-Mg2+ Plasmodium falciparum
NaCl maximal activity at 0.1 M Plasmodium falciparum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
dUTP + H2O Plasmodium falciparum
-
dUMP + diphosphate
-
?

Organism

Organism UniProt Comment Textmining
Plasmodium falciparum
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme by gel filtration Plasmodium falciparum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dUTP + H2O
-
Plasmodium falciparum dUMP + diphosphate
-
?
dUTP + H2O dUTPase catalyzes the hydrolysis of the alpha,beta-diphosphate bond of dUTP Plasmodium falciparum dUMP + diphosphate
-
?
dUTP-Co2+ + H2O
-
Plasmodium falciparum dUMP-Co2+ + diphosphate
-
?
dUTP-Mg2+ + H2O
-
Plasmodium falciparum dUMP-Mg2+ + diphosphate
-
?
dUTP-Mn2+ + H2O
-
Plasmodium falciparum dUMP-Mn2+ + diphosphate
-
?

Subunits

Subunits Comment Organism
trimer
-
Plasmodium falciparum

Synonyms

Synonyms Comment Organism
deoxyuridine 5'-triphosphate nucleotidohydrolase
-
Plasmodium falciparum
dUTPase
-
Plasmodium falciparum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Plasmodium falciparum

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.4
-
dUTP pH 7.0, 25°C, recombinant enzyme Plasmodium falciparum
4.1
-
dUTP-Co2+ pH 7.0, 25°C, recombinant enzyme Plasmodium falciparum
5.3
-
dUTP-Mn2+ pH 7.0, 25°C, recombinant enzyme Plasmodium falciparum
13.3
-
dUTP-Mg2+ pH 7.0, 25°C, recombinant enzyme Plasmodium falciparum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
assay at Plasmodium falciparum

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.0718
-
dUTP-Mn2+ pH 7.0, 25°C, recombinant enzyme Plasmodium falciparum
0.092
-
dUTP-Co2+ pH 7.0, 25°C, recombinant enzyme Plasmodium falciparum
0.0955
-
dUTP-Mg2+ pH 7.0, 25°C, recombinant enzyme Plasmodium falciparum
0.099
-
dUMP pH 7.0, 25°C Plasmodium falciparum
0.115
-
dUTP pH 7.0, 25°C, recombinant enzyme Plasmodium falciparum
0.121
-
dUTP pH 7.0, 25°C, recombinant enzyme, without NaCl, presence of EDTA Plasmodium falciparum