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Literature summary extracted from

  • Harris, J.M.; McIntosh, E.M.; Muscat, G.E.O.
    Structure/function analysis of a dUTPase: catalytic mechanism of a potential chemotherapeutic target (1999), J. Mol. Biol., 288, 275-287.
    View publication on PubMed

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 human endogenous retrovirus elimination of dUTP, by dUTPase, is vital since its misincorporation into DNA by DNA polymerases can initiate a damaging iterative repair and misincorporation cycle, resulting in DNA fragmentation and cell death, the anti-tumour activity of folate agonists and thymidylate synthase inhibitors is thought to rely on UTP misincorporation. dUTPase activity is an ideal point of intervention in both chemotherapy and anti-retroviral therapy ?
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 ?

Organism

EC Number Organism UniProt Comment Textmining
3.6.1.23 human endogenous retrovirus
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-
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Reaction

EC Number Reaction Comment Organism Reaction ID
3.6.1.23 dUTP + H2O = dUMP + diphosphate mechanism human endogenous retrovirus
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.6.1.23 dUTP + H2O
-
 human endogenous retrovirus dUMP + diphosphate
-
 ?
3.6.1.23 dUTP + H2O elimination of dUTP, by dUTPase, is vital since its misincorporation into DNA by DNA polymerases can initiate a damaging iterative repair and misincorporation cycle, resulting in DNA fragmentation and cell death, the anti-tumour activity of folate agonists and thymidylate synthase inhibitors is thought to rely on UTP misincorporation. dUTPase activity is an ideal point of intervention in both chemotherapy and anti-retroviral therapy human endogenous retrovirus ?
-
 ?