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Literature summary for 4.2.99.18 extracted from
- Repair activities of 8-oxoguanine DNA glycosylase from Archaeoglobus fulgidus, a hyperthermophilic archaeon (2001), Mutat. Res., 486, 99-111.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| overproduced in Escherichia coli as a maltose binding protein(MBP)-Afogg fusion protein | Archaeoglobus fulgidus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| NaCl | catalytic activity is inhibited in buffer more than 100 mM NaCl | Archaeoglobus fulgidus |  |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 22000 | - |
1 * 22000, SDS-PAGE | Archaeoglobus fulgidus |
| 22639 | - |
1 * 22639, calculated from sequenec | Archaeoglobus fulgidus |
| 23000 | - |
gel filtration | Archaeoglobus fulgidus |
| 23124 | - |
1 * 23124, mass spectrophotometry | Archaeoglobus fulgidus |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| DNA with an abasic site | Archaeoglobus fulgidus | the enzyme excises an oxidatively-damaged form of guanine. Bifunctional enzyme with both DNA glycosylase and apurinic/apyrimidinic lyase activities | DNA with 5'-phosphate terminus + DNA with 3'-alpha,beta-unsaturated aldehyde | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Archaeoglobus fulgidus | O29876 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| overproduced in Escherichia coli | Archaeoglobus fulgidus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| DNA with an abasic site | the enzyme excises an oxidatively-damaged form of guanine. Bifunctional enzyme with both DNA glycosylase and apurinic/apyrimidinic lyase activities | Archaeoglobus fulgidus | DNA with 5'-phosphate terminus + DNA with 3'-alpha,beta-unsaturated aldehyde | - |
? | |
| DNA with an abasic site | bifunctional enzyme with both DNA glycosylase and apurinic/apyrimidinic lyase activities. The specificity of DNA glycosylase activity of is compared using 39-mer DNA duplexes containing an 8-oxoG residue opposite each of the four natural DNA bases (A, T, G and C). The enzyme efficiently cleaves oligomers containing 8-oxoG:C and 8-oxoG:G base pairs, less effective on oligomers containing 8-oxoG:T and 8-oxoG:A mispairs. The enzyme catalyzes a beta-elimination reaction at the apurinic site produced by excision of the 8-oxoguanine and thus generates a 5'-phosphate terminus and a 3'-alpha,beta-unsaturated aldehyde sugar terminus at the incision site. Bifunctional enzyme with both DNA glycosylase and apurinic/apyrimidinic lyase activities | Archaeoglobus fulgidus | DNA with 5'-phosphate terminus + DNA with 3'-alpha,beta-unsaturated aldehyde | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| monomer | 1 * 22000, SDS-PAGE | Archaeoglobus fulgidus |
| monomer | 1 * 22639, calculated from sequenec | Archaeoglobus fulgidus |
| monomer | 1 * 23124, mass spectrophotometry | Archaeoglobus fulgidus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| 8-oxoG DNA glycosylase | - |
Archaeoglobus fulgidus |
| Af0371 | - |
Archaeoglobus fulgidus |
| Afogg enzyme | bifunctional enzyme with both DNA glycosylase and apurinic/apyrimidinic lyase activities | Archaeoglobus fulgidus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 50 | - |
assay at | Archaeoglobus fulgidus |
| 60 | - |
since the Tm-value of the DNA substrates (39-mer) is 74°C, the activity above 60°C is not convincible. The actual optimum temperature of the enzyme might be higher than 60°C | Archaeoglobus fulgidus |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 40 | 80 | 40°C: about 60% of maximal activity, 80°C: about 70% of maximal activity | Archaeoglobus fulgidus |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
thermostability of the enzyme is the highest near 0.5 M NaCl | Archaeoglobus fulgidus |
| 80 | - |
pH 7.5 (20 mM TrisCl buffer), denatured irreversibly above 80°C | Archaeoglobus fulgidus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8.5 | - |
- |
Archaeoglobus fulgidus |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | 10 | pH 7.5: about 50% of maximal activity, pH 10.0: about 50% of maximal activity | Archaeoglobus fulgidus |
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