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Literature summary extracted from

  • Varga, B.; Barabas, O.; Takacs, E.; Nagy, N.; Nagy, P.; Vertessy, B.G.
    Active site of mycobacterial dUTPase: structural characteristics and a built-in sensor (2008), Biochem. Biophys. Res. Commun., 373, 8-13.
    View publication on PubMed

Application

EC Number Application Comment Organism
3.6.1.23 drug development dUTPase is a promising antituberculotic drug target Mycobacterium tuberculosis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.6.1.23 expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3) Mycobacterium tuberculosis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.6.1.23 dUTPase in complex with the isosteric substrate analogue, alpha,beta-imido-dUTP, and Mg2+, about 0.223 mM dUTPase, 1.25 mM alpha,beta-imido-dUTP and 10 mM MgCl2 in 10 mM Tris-HCl, pH7.0, 50 mM NaCl, and 0.1 mM TCEP buffer is mixed with different reservoir solutions, X-ray diffraction structure determination and analysis at 1.5 A resolution, molecular replacement Mycobacterium tuberculosis

Protein Variants

EC Number Protein Variants Comment Organism
3.6.1.23 H145W site-directed mutagenesis, the replacement introduces a 244 sensitive fluorescent label into the binding site. The steady-state kinetics show no difference in the case of the mutant and wild-type enzyme Mycobacterium tuberculosis

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.6.1.23 additional information fast screening for binding of potential inhibitors to the active site Mycobacterium tuberculosis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.6.1.23 Mg2+ required, binding structure, overview Mycobacterium tuberculosis

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 Mycobacterium tuberculosis dUTPase is essential to eliminate dUTP for DNA integrity and provide dUMP for thymidylate biosynthesis dUMP + diphosphate
-
 ?
3.6.1.23 dUTP + H2O Mycobacterium tuberculosis H37Rv dUTPase is essential to eliminate dUTP for DNA integrity and provide dUMP for thymidylate biosynthesis dUMP + diphosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.6.1.23 Mycobacterium tuberculosis P9WNS5
-
-
3.6.1.23 Mycobacterium tuberculosis H37Rv P9WNS5
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.6.1.23 recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Mycobacterium tuberculosis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.6.1.23 dUTP + H2O dUTPase is essential to eliminate dUTP for DNA integrity and provide dUMP for thymidylate biosynthesis Mycobacterium tuberculosis dUMP + diphosphate
-
 ?
3.6.1.23 dUTP + H2O development of a robust and continuous dUTPase enzyme activity assay method using phenolred indicator, overview Mycobacterium tuberculosis dUMP + diphosphate
-
 ?
3.6.1.23 dUTP + H2O dUTPase is essential to eliminate dUTP for DNA integrity and provide dUMP for thymidylate biosynthesis Mycobacterium tuberculosis H37Rv dUMP + diphosphate
-
 ?
3.6.1.23 dUTP + H2O development of a robust and continuous dUTPase enzyme activity assay method using phenolred indicator, overview Mycobacterium tuberculosis H37Rv dUMP + diphosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.6.1.23 dUTPase
-
 Mycobacterium tuberculosis

Temperature Optimum [°C]

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

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.6.1.23 3.7 5.8 dUTP pH 7.5, 25°C, recombinant wild-type and mutant enzymes Mycobacterium tuberculosis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.6.1.23 7.5
-
 assay at Mycobacterium tuberculosis