EC Number   |
Activating Compound |
Reference |
|---|
   3.2.2.29 | AP1 |
TDG activity is stimulated by APE1 |
710229 |
| 3.2.2.29 | more |
AP andonuclease 1 is able to stimulate the turnover of TDG on a G/T substrate |
692013 |
| 3.2.2.29 | more |
the enzyme can be stimulated by human AP endonuclease 1 |
691737 |
| 3.2.2.29 | SUMO-1 |
TDG interacts with, but also is modified by SUMO-1 and SUMO-3, SUMOs are small ubiquitin like modifiers, small polypeptides structurally related to ubiquitin that interact with and/or are attached to other proteins. SUMO conjugation involves Lys330 located in a C-terminal SUMOylation consensus motif, VKEE, it is ATP-dependent and, when performed in cell extracts, stimulated by the presence of DNA. SUMO attachment to K330 affects structural and enzymatic properties of TDG. The modified glycosylase is not longer able to interact with free SUMO or SUMO-conjugated proteins, or to bind stably to AP-sites or any other DNA. Yet, it processes a G-U substrate with enhanced efficiency due to an induced enzymatic turnover but, at the same time, loses its ability to hydrolyze T from a G-T substrate |
692013 |
| 3.2.2.29 | SUMO-3 |
TDG interacts with, but also is modified by SUMO-1 and SUMO-3, SUMOs are small ubiquitin like modifiers, small polypeptides structurally related to ubiquitin that interact with and/or are attached to other proteins. SUMO conjugation involves Lys330 located in a C-terminal SUMOylation consensus motif, VKEE, it is ATP-dependent and, when performed in cell extracts, stimulated by the presence of DNA. SUMO attachment to K330 affects structural and enzymatic properties of TDG. The modified glycosylase is not longer able to interact with free SUMO or SUMO-conjugated proteins, or to bind stably to AP-sites or any other DNA. Yet, it processes a G-U substrate with enhanced efficiency due to an induced enzymatic turnover but, at the same time, loses its ability to hydrolyze T from a G-T substrate |
692013 |
