Activating Compound | Comment | Organism | Structure |
---|---|---|---|
AP1 | TDG activity is stimulated by APE1 | Mus musculus | |
AP1 | TDG activity is stimulated by APE1 | Homo sapiens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Mus musculus | TDG has a strong preference for uracil over thymine. TDG is an intriguing protein that, similar to SMUG1, has a low turnover number and strong binding to AP sites. The binding of the glycosylase to the AP site inhibits cleavage by the downstream AP endonuclease | ? | - |
? | |
additional information | Homo sapiens | TDG has a strong preference for uracil over thymine. TDG is an intriguing protein that, similar to SMUG1, has a low turnover number and strong binding to AP sites. The binding of the glycosylase to the AP site inhibits cleavage by the downstream AP endonuclease | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Mus musculus | - |
- |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
additional information | TDG catalytic efficiency of the protein is increased by SUMOylation | Mus musculus |
additional information | TDG catalytic efficiency of the protein is increased by SUMOylation | Homo sapiens |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
additional information | TDG is strictly cell-cycle regulated. TDG is regulated, opposite to UNG2, EC 3.2.2.27, by displaying the highest expression in the G1-phase and the lowest in the S-phase | Mus musculus | - |
additional information | TDG is strictly cell-cycle regulated. TDG is regulated, opposite to UNG2, EC 3.2.2.27, by displaying the highest expression in the G1-phase and the lowest in the S-phase | Homo sapiens | - |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
low catalytic turnover of TDG | Mus musculus |
additional information | - |
low catalytic turnover of TDG | Homo sapiens |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | TDG has a strong preference for uracil over thymine. TDG is an intriguing protein that, similar to SMUG1, has a low turnover number and strong binding to AP sites. The binding of the glycosylase to the AP site inhibits cleavage by the downstream AP endonuclease | Mus musculus | ? | - |
? | |
additional information | TDG has a strong preference for uracil over thymine. TDG is an intriguing protein that, similar to SMUG1, has a low turnover number and strong binding to AP sites. The binding of the glycosylase to the AP site inhibits cleavage by the downstream AP endonuclease | Homo sapiens | ? | - |
? | |
additional information | TDG has a strong preference for uracil over thymine, it also has a strong preference for U:G mismatches | Mus musculus | ? | - |
? | |
additional information | TDG has a strong preference for uracil over thymine, it also has a strong preference for U:G mismatches | Homo sapiens | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
T/U mismatch DNA glycosylase | - |
Mus musculus |
T/U mismatch DNA glycosylase | - |
Homo sapiens |
TDG | - |
Mus musculus |
TDG | - |
Homo sapiens |
General Information | Comment | Organism |
---|---|---|
physiological function | TDG seems not to have an important function in uracil repair compared with the leading enzymes UNG2 and SMUG1, EC 3.2.2.27 | Mus musculus |
physiological function | TDG seems not to have an important function in uracil repair compared with the leading enzymes UNG2 and SMUG1, EC 3.2.2.27 | Homo sapiens |