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Literature summary for 3.2.2.29 extracted from

  • Li, Y.Q.; Zhou, P.Z.; Zheng, X.D.
    Walsh, C.P.; Xu, G.L.: Association of Dnmt3a and thymine DNA glycosylase links DNA methylation with base-excision repair (2007), Nucleic Acids Res., 35, 390-400.
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Mus musculus DNA methyltransferase Dnmt3a interacts with TDG. Both the PWWP domain and the catalytic domain of Dnmt3a are able to mediate the interaction with TDG at its N-terminus. The interaction affects the enzymatic activity of both proteins: Dnmt3a positively regulates the glycosylase activity of TDG, while TDG inhibits the methylation activity of Dnmt3a in vitro. Mechanistic link between DNA repair and remethylation at sites affected by methylcytosine deamination ?
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Organism

Organism UniProt Comment Textmining
Mus musculus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information DNA methyltransferase Dnmt3a interacts with TDG. Both the PWWP domain and the catalytic domain of Dnmt3a are able to mediate the interaction with TDG at its N-terminus. The interaction affects the enzymatic activity of both proteins: Dnmt3a positively regulates the glycosylase activity of TDG, while TDG inhibits the methylation activity of Dnmt3a in vitro. Mechanistic link between DNA repair and remethylation at sites affected by methylcytosine deamination Mus musculus ?
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thymine-mismatched double-stranded DNA + H2O DNA containing a single G/T mismatch Mus musculus thymine + double-stranded DNA with abasic site
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Synonyms

Synonyms Comment Organism
TDG
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Mus musculus