EC Number | Cloned (Comment) | Organism |
---|---|---|
3.2.2.B5 | overproduced in Escherichia coli as a maltose binding protein(MBP)-Afogg fusion protein | Archaeoglobus fulgidus |
4.2.99.18 | overproduced in Escherichia coli as a maltose binding protein(MBP)-Afogg fusion protein | Archaeoglobus fulgidus |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
3.2.2.B5 | NaCl | catalytic activity is inhibited in buffer more than 100 mM NaCl | Archaeoglobus fulgidus | |
4.2.99.18 | NaCl | catalytic activity is inhibited in buffer more than 100 mM NaCl | Archaeoglobus fulgidus |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
3.2.2.B5 | 22000 | - |
1 * 22000, SDS-PAGE | Archaeoglobus fulgidus |
3.2.2.B5 | 22639 | - |
1 * 22639, calculated from sequenec | Archaeoglobus fulgidus |
3.2.2.B5 | 23000 | - |
gel filtration | Archaeoglobus fulgidus |
3.2.2.B5 | 23124 | - |
1 * 23124, mass spectrophotometry | Archaeoglobus fulgidus |
4.2.99.18 | 22000 | - |
1 * 22000, SDS-PAGE | Archaeoglobus fulgidus |
4.2.99.18 | 22639 | - |
1 * 22639, calculated from sequenec | Archaeoglobus fulgidus |
4.2.99.18 | 23000 | - |
gel filtration | Archaeoglobus fulgidus |
4.2.99.18 | 23124 | - |
1 * 23124, mass spectrophotometry | Archaeoglobus fulgidus |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.2.2.B5 | DNA containing 8-oxoguanine + H2O | Archaeoglobus fulgidus | the enzyme excises an oxidatively-damaged form of guanine. Bifunctional enzyme with both DNA glycosylase and apurinic/apyrimidinic lyase activities | DNA with an abasic site + 8-oxoguanine | - |
? | |
4.2.99.18 | 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 | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.2.2.B5 | Archaeoglobus fulgidus | O29876 | - |
- |
4.2.99.18 | Archaeoglobus fulgidus | O29876 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
3.2.2.B5 | overproduced in Escherichia coli | Archaeoglobus fulgidus |
4.2.99.18 | overproduced in Escherichia coli | Archaeoglobus fulgidus |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.2.2.B5 | DNA containing 8-oxoguanine + H2O | the enzyme excises an oxidatively-damaged form of guanine. Bifunctional enzyme with both DNA glycosylase and apurinic/apyrimidinic lyase activities | Archaeoglobus fulgidus | DNA with an abasic site + 8-oxoguanine | - |
? | |
3.2.2.B5 | DNA containing 8-oxoguanine + H2O | 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 | Archaeoglobus fulgidus | DNA with an abasic site + 8-oxoguanine | - |
? | |
4.2.99.18 | 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 | - |
? | |
4.2.99.18 | 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 | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
3.2.2.B5 | monomer | 1 * 22000, SDS-PAGE | Archaeoglobus fulgidus |
3.2.2.B5 | monomer | 1 * 22639, calculated from sequenec | Archaeoglobus fulgidus |
3.2.2.B5 | monomer | 1 * 23124, mass spectrophotometry | Archaeoglobus fulgidus |
4.2.99.18 | monomer | 1 * 22000, SDS-PAGE | Archaeoglobus fulgidus |
4.2.99.18 | monomer | 1 * 22639, calculated from sequenec | Archaeoglobus fulgidus |
4.2.99.18 | monomer | 1 * 23124, mass spectrophotometry | Archaeoglobus fulgidus |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.2.2.B5 | 8-oxoG DNA glycosylase | - |
Archaeoglobus fulgidus |
3.2.2.B5 | Af0371 | - |
Archaeoglobus fulgidus |
3.2.2.B5 | Afogg enzyme | bifunctional enzyme with both DNA glycosylase and apurinic/apyrimidinic lyase activities | Archaeoglobus fulgidus |
4.2.99.18 | 8-oxoG DNA glycosylase | - |
Archaeoglobus fulgidus |
4.2.99.18 | Af0371 | - |
Archaeoglobus fulgidus |
4.2.99.18 | Afogg enzyme | bifunctional enzyme with both DNA glycosylase and apurinic/apyrimidinic lyase activities | Archaeoglobus fulgidus |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.2.2.B5 | 50 | - |
assay at | Archaeoglobus fulgidus |
3.2.2.B5 | 60 | - |
since the Tm-value of the DNA substrates (39-mer) of 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 |
4.2.99.18 | 50 | - |
assay at | Archaeoglobus fulgidus |
4.2.99.18 | 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 |
EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.2.2.B5 | 40 | 80 | 40°C: about 60% of maximal activity, 80°C: about 70% of maximal activity | Archaeoglobus fulgidus |
4.2.99.18 | 40 | 80 | 40°C: about 60% of maximal activity, 80°C: about 70% of maximal activity | Archaeoglobus fulgidus |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.2.2.B5 | additional information | - |
thermostability of the enzyme is the highest near 0.5 M NaCl | Archaeoglobus fulgidus |
3.2.2.B5 | 80 | - |
pH 7.5 (20 mM TrisCl buffer), denatured irreversibly above 80°C | Archaeoglobus fulgidus |
4.2.99.18 | additional information | - |
thermostability of the enzyme is the highest near 0.5 M NaCl | Archaeoglobus fulgidus |
4.2.99.18 | 80 | - |
pH 7.5 (20 mM TrisCl buffer), denatured irreversibly above 80°C | Archaeoglobus fulgidus |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.2.2.B5 | 8.5 | - |
- |
Archaeoglobus fulgidus |
4.2.99.18 | 8.5 | - |
- |
Archaeoglobus fulgidus |
EC Number | pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|---|
3.2.2.B5 | 7.5 | 10 | pH 7.5: about 50% of maximal activity, pH 10.0: about 50% of maximal activity | Archaeoglobus fulgidus |
4.2.99.18 | 7.5 | 10 | pH 7.5: about 50% of maximal activity, pH 10.0: about 50% of maximal activity | Archaeoglobus fulgidus |