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Literature summary for 3.2.2.15 extracted from
- Specificity and catalytic mechanism in family 5 uracil DNA glycosylase (2014), J. Biol. Chem., 289, 18413-18426.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed in Escherichia coli BH214 cells | Thermus thermophilus |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| hypoxanthine-containing double-stranded DNA + H2O | Thermus thermophilus | strongest activity on the G/I base pair but no activity detected on the C/I base pair | hypoxanthine + double-stranded DNA | - |
? |  |
| hypoxanthine-containing double-stranded DNA + H2O | Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | strongest activity on the G/I base pair but no activity detected on the C/I base pair | hypoxanthine + double-stranded DNA | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Thermus thermophilus | Q5SJ65 | - |
- |
| Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | Q5SJ65 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| hypoxanthine-containing double-stranded DNA + H2O | strongest activity on the G/I base pair but no activity detected on the C/I base pair | Thermus thermophilus | hypoxanthine + double-stranded DNA | - |
? | |
| hypoxanthine-containing double-stranded DNA + H2O | strongest activity on the G/I base pair but no activity detected on the C/I base pair | Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | hypoxanthine + double-stranded DNA | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| family 5 UDGb | the enzyme is an uracil, hypoxanthine, and xanthine DNA glycosylase | Thermus thermophilus |
| hypoxanthine DNA glycosylase | - |
Thermus thermophilus |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | a repair enzyme involved in the removal of base damage | Thermus thermophilus |
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