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Literature summary extracted from

  • Takacs, E.; Nagy, G.; Leveles, I.; Harmat, V.; Lopata, A.; Toth, J.; Vertessy, B.G.
    Direct contacts between conserved motifs of different subunits provide major contribution to active site organization in human and mycobacterial dUTPases (2010), FEBS Lett., 584, 3047-3054.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.6.1.23
-
 Homo sapiens
3.6.1.23
-
 Mycobacterium tuberculosis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.6.1.23 mutant enzymes D28N and T138STOP Mycobacterium tuberculosis

Protein Variants

EC Number Protein Variants Comment Organism
3.6.1.23 D28N/H145W the Asp/Asn mutation within Motif I results in approximately 50fold decrease of steady-state rate and significantly weakens the interaction of the protein with alpha,beta-imido-dUTP (15fold) whereas dUMP binding is only slightly affected Mycobacterium tuberculosis
3.6.1.23 D49N/F158W the Asp/Asn mutation within motif I results in approximately 1000fold decrease of steady-state rate and significantly weakens the interaction of the protein with alpha,beta-imido-dUTP (4fold) whereas dUMP binding is only slightly affected Homo sapiens
3.6.1.23 F158W the mutation has no significant effect on the catalytic properties of dUTPase Homo sapiens
3.6.1.23 H145W the mutation has no significant effect on the catalytic properties of dUTPase Mycobacterium tuberculosis

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.6.1.23 alpha,beta-imido-dUTP
-
 Mycobacterium tuberculosis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.6.1.23 Mg2+ required for full activity, In the absence of divalent cations, dUTPase retains about 50% of the catalytic rate observed in the presence of Mg2+ Homo sapiens
3.6.1.23 Mg2+ required for full activity, In the absence of divalent cations, dUTPase retains about 50% of the catalytic rate observed in the presence of Mg2+ Mycobacterium tuberculosis

Organism

EC Number Organism UniProt Comment Textmining
3.6.1.23 Homo sapiens
-
-
-
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
-
 Homo sapiens
3.6.1.23
-
 Mycobacterium tuberculosis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.6.1.23 dUTP + H2O
-
 Homo sapiens dUMP + diphosphate
-
 ?
3.6.1.23 dUTP + H2O
-
 Mycobacterium tuberculosis dUMP + diphosphate
-
 ?
3.6.1.23 dUTP + H2O
-
 Mycobacterium tuberculosis H37Rv dUMP + diphosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
3.6.1.23 homotrimer
-
 Homo sapiens
3.6.1.23 homotrimer
-
 Mycobacterium tuberculosis

Synonyms

EC Number Synonyms Comment Organism
3.6.1.23 dUTPase
-
 Homo sapiens
3.6.1.23 dUTPase
-
 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 0.007
-
 dUTP mutant enzyme D49N/F158W, in 1 mM HEPES pH 7.5 containing 100 mM KCl and 5 mM MgCl2, at 20°C Homo sapiens
3.6.1.23 0.024
-
 dUTP mutant enzyme D28N/H145W, in 1 mM HEPES pH 7.5 containing 100 mM KCl and 5 mM MgCl2, at 20°C Mycobacterium tuberculosis
3.6.1.23 1.2
-
 dUTP mutant enzyme H145W, in 1 mM HEPES pH 7.5 containing 100 mM KCl and 5 mM MgCl2, at 20°C Mycobacterium tuberculosis
3.6.1.23 6.3
-
 dUTP mutant enzyme F158W, in 1 mM HEPES pH 7.5 containing 100 mM KCl and 5 mM MgCl2, at 20°C Homo sapiens