EC Number   |
Natural Substrates |
|---|
   3.2.2.29 | 3,N4-ethenocytosine-mismatched double-stranded DNA + H2O |
3,N4-ethenocytosine is recognized and efficiently excised by hTDG. The enzyme may be responsible for the repair of this mutagenic lesion in vivo and be important contributors to genetic stability |
| 3.2.2.29 | 5-bromouracil-mismatched double-stranded DNA + H2O |
potential role played by human TDG in the cytotoxic effects of 5-chlorouracil and 5-bromouracil incorporation into DNA, which can occur under inflammatory conditions |
| 3.2.2.29 | 5-carboxylcytosine mismatched double-stranded DNA + H2O |
- |
| 3.2.2.29 | 5-carboxylcytosine-mismatched double-stranded DNA + H2O |
- |
| 3.2.2.29 | 5-chlorouracil-mismatched double-stranded DNA + H2O |
potential role played by human TDG in the cytotoxic effects of 5-chlorouracil and 5-bromouracil incorporation into DNA, which can occur under inflammatory conditions |
| 3.2.2.29 | 5-formylcytosine-mismatched double-stranded DNA + H2O |
- |
| 3.2.2.29 | 5-hydroxymethyluracil-mismatched double-stranded DNA + H2O |
- |
| 3.2.2.29 | 5-hydroxymethyluridine-mismatched double-stranded DNA + H2O |
- |
| 3.2.2.29 | double-stranded DNA + H2O |
thymine-DNA glycosylase has a strong sequence preference for CpG sites in the excision of both thymine and ethenocytosine. This suggests a main role of thymine-DNA glycosylase in vivo is the removal of thymine produced by deamination of 5-methylcytosine at CpG sites |
| 3.2.2.29 | more |
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 |
