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Literature summary extracted from

  • Saporito, S.M.; Gedenk, M.; Cunningham, R.P.
    Role of exonuclease III and endonuclease IV in repair of pyrimidine dimers initiated by bacteriophage T4 pyrimidine dimer-DNA glycosylase (1989), J. Bacteriol., 171, 2542-2546.
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.21.9 additional information Tequatrovirus T4 enzyme is capable of cleaving at the atypical apurinic-apyrimidinic site created by the action of T4 PD-DNA glycosylase. Exonuclease III and endonuclease IV are equally efficient in repair ?
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Organism

EC Number Organism UniProt Comment Textmining
3.1.21.9 Tequatrovirus T4
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.21.9 additional information enzyme is capable of cleaving at the atypical apurinic-apyrimidinic site created by the action of T4 PD-DNA glycosylase. Exonuclease III and endonuclease IV are equally efficient in repair Tequatrovirus T4 ?
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 ?

General Information

EC Number General Information Comment Organism
3.1.21.9 physiological function the absence of either exonuclease III or endonuclease IV has no effect on survival. Exonuclease III and endonuclease IV are equally able to repair the apurinic-apyrimidinic site created by PD-DNA glycosylase. This apurinic-apyrimidinic site is atypical, since only the 5' glycosyl bond in the dimer is cleaved and the product is a cyclobutane dimer bound to DNA by a single glycosyl bond. Neither T4 endonuclease V nor endonuclease III is required for the repair of these apurinic-apyrimidinic sites Tequatrovirus T4