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Literature summary extracted from
- Characterization of an 8-oxoguanine DNA glycosylase from Methanococcus jannaschii (1999), J. Biol. Chem., 274, 30447-30450.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.2.2.B5 | expressed in Escherichia coli | Methanocaldococcus jannaschii |
| 4.2.99.18 | expressed in Escherichia coli | Methanocaldococcus jannaschii |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.2.2.B5 | K129S | inactive mutant enzyme | Methanocaldococcus jannaschii |
| 4.2.99.18 | K129S | inactive mutant enzyme | Methanocaldococcus jannaschii |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.2.2.B5 | Methanocaldococcus jannaschii | Q58134 | - |
- |
| 3.2.2.B5 | Methanocaldococcus jannaschii DSM 2661 | Q58134 | - |
- |
| 4.2.99.18 | Methanocaldococcus jannaschii | Q58134 | - |
- |
| 4.2.99.18 | Methanocaldococcus jannaschii DSM 2661 | Q58134 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.2.2.B5 | - |
Methanocaldococcus jannaschii |
| 4.2.99.18 | - |
Methanocaldococcus jannaschii |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.2.2.B5 | DNA containing 8-oxoguanine + H2O | the enzyme has little specificity for the base opposite 8-oxoguanine. The enzyme has both DNA glycosylase and DNA lyase (beta-elimination) activity, and the combined glycosylase/lyase activity occurs at a rate comparable with the glycosylase activity alone | Methanocaldococcus jannaschii | DNA with an abasic site + 8-oxoguanine | - |
? |  |
| 3.2.2.B5 | DNA containing 8-oxoguanine + H2O | the enzyme has little specificity for the base opposite 8-oxoguanine. The enzyme has both DNA glycosylase and DNA lyase (beta-elimination) activity, and the combined glycosylase/lyase activity occurs at a rate comparable with the glycosylase activity alone | Methanocaldococcus jannaschii DSM 2661 | DNA with an abasic site + 8-oxoguanine | - |
? | |
| 4.2.99.18 | DNA with an abasic site | the enzyme has little specificity for the base opposite 8-oxoguanine. The enzyme has both DNA glycosylase and DNA lyase (beta-elimination) activity, and the combined glycosylase/lyase activity occurs at a rate comparable with the glycosylase activity alone | Methanocaldococcus jannaschii | ? | - |
? | |
| 4.2.99.18 | DNA with an abasic site | the enzyme has little specificity for the base opposite 8-oxoguanine. The enzyme has both DNA glycosylase and DNA lyase (beta-elimination) activity, and the combined glycosylase/lyase activity occurs at a rate comparable with the glycosylase activity alone | Methanocaldococcus jannaschii DSM 2661 | ? | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.2.2.B5 | mjOgg | - |
Methanocaldococcus jannaschii |
| 3.2.2.B5 | oxoG DNA glycosylase | - |
Methanocaldococcus jannaschii |
| 4.2.99.18 | mjOgg | - |
Methanocaldococcus jannaschii |
| 4.2.99.18 | oxoG DNA glycosylase | - |
Methanocaldococcus jannaschii |
Temperature Range [°C]
| EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.2.2.B5 | 37 | 50 | the enzyme is 6fold more active at 50°C than at 37°C, glycosylase/lyase activity is very similarto that of the glycosylase activity alone | Methanocaldococcus jannaschii |
| 4.2.99.18 | 37 | 50 | the enzyme is 6fold more active at 50°C than at 37°C, glycosylase/lyase activity is very similarto that of the glycosylase activity alone | Methanocaldococcus jannaschii |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.2.2.B5 | 50 | - |
3 h, activity is decreased by one-third | Methanocaldococcus jannaschii |
| 3.2.2.B5 | 93 | - |
the enzyme is thermally stable, denaturing at 93 °C | Methanocaldococcus jannaschii |
| 4.2.99.18 | 50 | - |
3 h, activity is decreased by one-third | Methanocaldococcus jannaschii |
| 4.2.99.18 | 93 | - |
the enzyme is thermally stable, denaturing at 93 °C | Methanocaldococcus jannaschii |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.2.2.B5 | 8.5 | - |
assay at | Methanocaldococcus jannaschii |
| 4.2.99.18 | 8.5 | - |
assay at | Methanocaldococcus jannaschii |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.2.2.B5 | 7.3 | 9.5 | pH 7.3: about 50% of maximal activity, pH 9.5: about 45% of maximal ativity, glycosylase/lyase activity is very similar to that of the glycosylase activity alone | Methanocaldococcus jannaschii |
| 4.2.99.18 | 7.3 | 9.5 | pH 7.3: about 50% of maximal activity, pH 9.5: about 45% of maximal ativity, glycosylase/lyase activity is very similar to that of the glycosylase activity alone | Methanocaldococcus jannaschii |
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Release 2023.1 (January 2023)
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