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Literature summary extracted from

  • Kovari, J.; Barabas, O.; Varga, B.; Bekesi, A.; Toelgyesi, F.; Fidy, J.; Nagy, J.; Vertessy, B.G.
    Methylene substitution at the alpha-beta bridging position within the phosphate chain of dUDP profoundly perturbs ligand accommodation into the dUTPase active site (2008), Proteins, 71, 308-319.
    View publication on PubMed

Application

EC Number Application Comment Organism
3.6.1.23 drug development the enzyme is a target for development of antimicrobial agents Escherichia coli

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.6.1.23 purified recombinant enzyme in complex with inhibitors, i.e. dUTPase-alpha,beta-methylene-dUDP and dUTPase-dUDP-Mn complexes, 20°C, hanging-drop vapor diffusion, 3 mg/ml of enzyme in 10 mM Tris/HCl buffer, pH 7.0, and 50 mM NaCl, as well as 1.25 mM alpha,beta-methylene-dUDP or dUDP and 10 mM MgCl2 or MnCl2, respectively, mixing with an equal volume of reservoir solution 0.1 M Tris/HCl buffer, pH 7.8, containing 18-20% PEG 3350, and 400 mM Na-acetate, X-ray diffraction structure determination and analysis at 1.7-1.84 resolution, analysis of the different alpha-phosphate sites, overview Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.6.1.23 3'-deoxy-5'-O-(hydroxy{[hydroxy(phosphonooxy)phosphoryl]amino}phosphoryl)uridine competitive inhibition Escherichia coli
3.6.1.23 3'-deoxy-5'-O-[hydroxy(phosphonoamino)phosphoryl]uridine competitive inhibition Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.6.1.23 additional information
-
additional information ligand binding constants Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.6.1.23 Mg2+
-
Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.6.1.23 dUTP + H2O Escherichia coli a preventive DNA repair enzyme, contributes to maintain the appropriate cellular dUTP/dTTP ratio by catalyzing dUTP hydrolysis, dUTPase is essential for viability dUMP + diphosphate
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.6.1.23 Escherichia coli P06968
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.6.1.23 dUTP + H2O a preventive DNA repair enzyme, contributes to maintain the appropriate cellular dUTP/dTTP ratio by catalyzing dUTP hydrolysis, dUTPase is essential for viability Escherichia coli dUMP + diphosphate
-
?
3.6.1.23 dUTP + H2O substrate binding structure, the strictly conserved residue Ser72 is involved in phosphate chain binding, overview Escherichia coli dUMP + diphosphate
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?

Synonyms

EC Number Synonyms Comment Organism
3.6.1.23 dUTP pyrophosphatase
-
Escherichia coli
3.6.1.23 dUTPase
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Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.6.1.23 25
-
assay at Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.6.1.23 7.5
-
assay at Escherichia coli