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Literature summary for 3.6.1.23 extracted from

  • Kovari, J.; Imre, T.; Szabo, P.; Vertessy, B.G.
    Mechanistic studies of dUTPases (2004), Nucleosides Nucleotides Nucleic Acids, 23, 1475-1479.
    View publication on PubMed

Application

Application Comment Organism
drug development inhibitor development against the enzyme can be useful in antiviral and anticancer therapy Drosophila melanogaster
drug development inhibitor development against the enzyme can be useful in antiviral and anticancer therapy Escherichia coli
pharmacology the enzyme is a chemotherapeutic target Drosophila melanogaster
pharmacology the enzyme is a chemotherapeutic target Escherichia coli

Cloned(Commentary)

Cloned (Comment) Organism
-
Drosophila melanogaster

Inhibitors

Inhibitors Comment Organism Structure
additional information the enzyme possesses a specific tryptic cleavage site Arg132-Ile133 20 A far from the active site of the enzyme, the enzyme is protected against tryptic digestion by binding alpha,beta-imino-dUTP which induces an allosteric conformational change within the central threefold channel of the homotrimer Drosophila melanogaster
additional information binding of alpha,beta-imino-dUTP does not induce allosteric conformational changes and does not protect the enzyme against tryptic digestion Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetics of dUTP binding Drosophila melanogaster
additional information
-
additional information kinetics of dUTP binding Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ binding as dUTP-Mg2+ at the C-terminus induces the closure of the C-terminal arm Drosophila melanogaster
Mg2+ binding as dUTP-Mg2+ at the C-terminus induces the closure of the C-terminal arm which opens up again after hydrolysis to expel the product Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
dUTP + H2O Drosophila melanogaster the essential enzyme is responsible for preventive DNA repair via exclusion of uracil, overview, lack of negative enzyme regulation leads to thymine-less cell death in cells performing active DNA synthesis dUMP + diphosphate
-
?
dUTP + H2O Escherichia coli the essential enzyme is responsible for preventive DNA repair via exclusion of uracil, overview, lack of negative enzyme regulation leads to thymine-less cell death in cells performing active DNA synthesis dUMP + diphosphate
-
?

Organism

Organism UniProt Comment Textmining
Drosophila melanogaster
-
-
-
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme Drosophila melanogaster

Reaction

Reaction Comment Organism Reaction ID
dUTP + H2O = dUMP + diphosphate structural and catalytic mechanism involving Mg2+ Drosophila melanogaster
dUTP + H2O = dUMP + diphosphate structural and catalytic mechanism involving Mg2+ Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dUTP + H2O the essential enzyme is responsible for preventive DNA repair via exclusion of uracil, overview, lack of negative enzyme regulation leads to thymine-less cell death in cells performing active DNA synthesis Drosophila melanogaster dUMP + diphosphate
-
?
dUTP + H2O the essential enzyme is responsible for preventive DNA repair via exclusion of uracil, overview, lack of negative enzyme regulation leads to thymine-less cell death in cells performing active DNA synthesis Escherichia coli dUMP + diphosphate
-
?
dUTP + H2O the enzyme is highly specific for dUTP Drosophila melanogaster dUMP + diphosphate
-
?
dUTP + H2O the enzyme is highly specific for dUTP Escherichia coli dUMP + diphosphate
-
?
additional information comparison of the Drosophila melanogaster and the Escherichia coli enzymes Drosophila melanogaster ?
-
?
additional information comparison of the Drosophila melanogaster and the Escherichia coli enzymes Escherichia coli ?
-
?

Subunits

Subunits Comment Organism
trimer each subunit contains an active site Escherichia coli
trimer each subunit contains an active site, alpha,beta-imino-dUTP which induces an allosteric conformational change within the central threefold channel of the homotrimer Drosophila melanogaster

Synonyms

Synonyms Comment Organism
dUTPase
-
Drosophila melanogaster
dUTPase
-
Escherichia coli