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Literature summary for 3.2.2.27 extracted from
- Thermostable uracil-DNA glycosylase from Thermotoga maritima, a member of a novel class of DNA repair enzymes (1999), Curr. Biol., 9, 531-534 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli | Thermotoga maritima |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Thermotoga maritima | Q9WYY1 | - |
- |
| Thermotoga maritima DSM 3109 | Q9WYY1 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Thermotoga maritima |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | the enzyme is capable of removing uracil from DNA containing either a U-A or a U-G base pair. The enzyme is also active on single-stranded DNA containing uracil | Thermotoga maritima | ? | - |
? |  |
| additional information | the enzyme is capable of removing uracil from DNA containing either a U-A or a U-G base pair. The enzyme is also active on single-stranded DNA containing uracil | Thermotoga maritima DSM 3109 | ? | - |
? | |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 75 | - |
stable up to | Thermotoga maritima |
General Information
| General Information | Comment | Organism |
|---|---|---|
| metabolism | the enzyme removes uracil bases that are present in DNA as a result of either deamination of cytosine or misincorporation of dUMP instead of dTMP, and it is the primary activity in the DNA base excision repair pathway | Thermotoga maritima |
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Release 2023.1 (January 2023)
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