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Literature summary for 3.2.2.29 extracted from
- Thymine-DNA glycosylase and G to A transition mutations at CpG sites (2000), Mutat. Res., 462, 137-147.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
- |
Homo sapiens |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| structural basis of substrate specificity | Homo sapiens |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| thymine-mismatched double-stranded DNA + H2O | Homo sapiens | about 23% of mutations in hereditary human diseases and 24% of mutations in p53 in human cancers are G to A transitions at sites of cytosine methylation suggesting that these sites are either foci for DNA damage, or foci for damage that is poorly repaired. Thymine produced at these sites by the hydrolytic deamination of 5-methylcytosine is removed by thymine-DNA glycosylase. Thymine-DNA glycosylase also removes 3,N4-ethenocytosine and uracil from DNA. The action of this enzyme is limited by its very low kcat and by tight binding to the apurinic site produced when the thymine is removed. These properties of the enzyme suggest that the inefficiency of the base excision repair pathway that it initiates may be the underlying cause of the prevalence of these mutations | thymine + double-stranded DNA with abasic site | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | Q13569 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Homo sapiens |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| HeLa cell | - |
Homo sapiens | - |
| thymus | highest expression | Homo sapiens | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| thymine-mismatched double-stranded DNA + H2O | about 23% of mutations in hereditary human diseases and 24% of mutations in p53 in human cancers are G to A transitions at sites of cytosine methylation suggesting that these sites are either foci for DNA damage, or foci for damage that is poorly repaired. Thymine produced at these sites by the hydrolytic deamination of 5-methylcytosine is removed by thymine-DNA glycosylase. Thymine-DNA glycosylase also removes 3,N4-ethenocytosine and uracil from DNA. The action of this enzyme is limited by its very low kcat and by tight binding to the apurinic site produced when the thymine is removed. These properties of the enzyme suggest that the inefficiency of the base excision repair pathway that it initiates may be the underlying cause of the prevalence of these mutations | Homo sapiens | thymine + double-stranded DNA with abasic site | - |
? | |
| thymine-mismatched double-stranded DNA + H2O | thymine-DNA glycosylase is more active on mismatches containing uracil than on mismatches containing thymine | Homo sapiens | thymine + double-stranded DNA with abasic site | - |
? | |
| uracil-mismatched double-stranded DNA + H2O | thymine-DNA glycosylase is more active on mismatches containing uracil than on mismatches containing thymine | Homo sapiens | uracil + double-stranded DNA with abasic site | - |
? | |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | effect of the 5'-flanking base pair on kcat | Homo sapiens |
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Release 2023.1 (January 2023)
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