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Literature summary for 3.2.2.29 extracted from
- The enigmatic thymine DNA glycosylase (2007), DNA Repair, 6, 489-504.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| additional information | AP andonuclease 1 is able to stimulate the turnover of TDG on a G/T substrate | Homo sapiens | |
| 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 | Homo sapiens | |
| 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 | Homo sapiens |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| DNA and amino acid sequence determination and analysis, phylogenetic tree of MUG proteins, expression in African green monkey kidney cells, the enzyme efficiently replaces the T with a C in G-T mismatched SV40 DNA exhibiting a G-T directed repair activity | Homo sapiens |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Homo sapiens | uncertainty about the biological function of TDG. TDG is a DNA glycosylase involved in the repair of damaged DNA bases. Judged from its interactions with other proteins, it is a co-regulator of gene expression | ? | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | Q13569 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 3,N4-ethenocytosine-mismatched double-stranded DNA + H2O | removes 3,N4-ethenocytosine from G/3,N4-ethenocytosine and A/3,N4-ethenocytosine mismatches | Homo sapiens | 3,N4-ethenocytosine + double-stranded DNA with abasic site | - |
? | |
| 5-bromouracil-mismatched double-stranded DNA + H2O | removes 5-bromouracil from G/5-bromouracil mismatches | Homo sapiens | 5-bromouracil + double-stranded DNA with abasic site | - |
? | |
| 5-fluorouracil-mismatched double-stranded DNA + H2O | removes 5-fluorouracil from G/5-fluorouracil and A/5-fluorouracil mismatches | Homo sapiens | 5-fluorouracil + double-stranded DNA with abasic site | - |
? | |
| 5-hydroxymethyluracil-mismatched double-stranded DNA + H2O | removes 5-hydroxymethyluracil from G/5-hydroxymethyluracil mismatches | Homo sapiens | 5-hydroxymethyluracil + double-stranded DNA with abasic site | - |
? | |
| 5-hydroxyuracil-mismatched double-stranded DNA + H2O | removes 5-hydroxyuracil from G/5-hydroxyuracil mismatches | Homo sapiens | 5-hydroxyuracil + double-stranded DNA with abasic site | - |
? | |
| additional information | uncertainty about the biological function of TDG. TDG is a DNA glycosylase involved in the repair of damaged DNA bases. Judged from its interactions with other proteins, it is a co-regulator of gene expression | Homo sapiens | ? | - |
? | |
| additional information | TDG interacts with, but also is modified by SUMO-1 and SUMO-3, SUMOylation enhances G-U processing while abolishing G-T processing, mechanism, overview. SUMO modification in the C-terminus converts TDG to an enzyme with Mug-like properties, as does the deletion of the N-terminus, overview | Homo sapiens | ? | - |
? | |
| thymine glycol -mismatched double-stranded DNA + H2O | thymine glycol from G/thymine glycol mismatches | Homo sapiens | thymine glycol + double-stranded DNA with abasic site | - |
? | |
| thymine-mismatched double-stranded DNA + H2O | removes thymine from G/T mismatches | Homo sapiens | thymine + double-stranded DNA with abasic site | - |
? | |
| uracil-mismatched double-stranded DNA + H2O | removes uracil from G/U mismatches | Homo sapiens | uracil + double-stranded DNA with abasic site | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | primary and domain structure, tertiary structure and structure-function analysis, overview | Homo sapiens |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| hsTDG | - |
Homo sapiens |
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