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Literature summary extracted from
- Mutational studies of Pa-AGOG DNA glycosylase from the hyperthermophilic crenarchaeon Pyrobaculum aerophilum (2009), DNA Repair, 8, 857-864.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.2.2.B5 | expression in Escherichia coli | Pyrobaculum aerophilum |
| 4.2.99.18 | expression in Escherichia coli | Pyrobaculum aerophilum |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.2.2.B5 | D172N | binds to 8-oxoguanine containing single-stranded DNA more tightly than double-stranded DNA containing a 8-oxoguanine/cytosine base pair | Pyrobaculum aerophilum |
| 3.2.2.B5 | D172Q | binds to 8-oxoguanine containing single-stranded DNA more tightly than double-stranded DNA containing a 8-oxoguanine/cytosine base pair | Pyrobaculum aerophilum |
| 3.2.2.B5 | D172Q | no detectable glycosylase activity | Pyrobaculum aerophilum |
| 3.2.2.B5 | K140Q | binds to 8-oxoguanine containing single-stranded DNA more tightly than double-stranded DNA containing a 8-oxoguanine/cytosine base pair | Pyrobaculum aerophilum |
| 3.2.2.B5 | Q31E/D218S | almost no glycosylase activity | Pyrobaculum aerophilum |
| 3.2.2.B5 | Q31S | significantly reduced glycosylase activity | Pyrobaculum aerophilum |
| 3.2.2.B5 | W222A | almost no glycosylase activity | Pyrobaculum aerophilum |
| 3.2.2.B5 | W222F | mutant is similarly active as wild type on 8-oxoguanine/C substrates | Pyrobaculum aerophilum |
| 3.2.2.B5 | W69F | mutant is similarly active as wild type on 8-oxoguanine/C substrates | Pyrobaculum aerophilum |
| 4.2.99.18 | D172N | binds to 8-oxoguanine containing single-stranded DNA more tightly than double-stranded DNA containing a 8-oxoguanine/cytosine base pair | Pyrobaculum aerophilum |
| 4.2.99.18 | D172Q | binds to 8-oxoguanine containing single-stranded DNA more tightly than double-stranded DNA containing a 8-oxoguanine/cytosine base pair | Pyrobaculum aerophilum |
| 4.2.99.18 | D172Q | no detectable glycosylase activity | Pyrobaculum aerophilum |
| 4.2.99.18 | K140Q | binds to 8-oxoguanine containing single-stranded DNA more tightly than double-stranded DNA containing a 8-oxoguanine/cytosine base pair | Pyrobaculum aerophilum |
| 4.2.99.18 | Q31E/D218S | almost no glycosylase activity | Pyrobaculum aerophilum |
| 4.2.99.18 | Q31S | significantly reduced glycosylase activity | Pyrobaculum aerophilum |
| 4.2.99.18 | W222A | almost no glycosylase activity | Pyrobaculum aerophilum |
| 4.2.99.18 | W222F | mutant is similarly active as wild type on 8-oxoguanine/C substrates | Pyrobaculum aerophilum |
| 4.2.99.18 | W69F | mutant is similarly active as wild type on 8-oxoguanine/C substrates | Pyrobaculum aerophilum |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.2.2.B5 | DNA containing 8-oxoguanine + H2O | Pyrobaculum aerophilum | bifunctional enzyme that catalyzes the excision of 8-oxoguanine by cleaving the N-glycosylic bond between the base and the deoxyribose moiety (glycosylase activity) and subsequently cleave the DNA backbone (lyase activity, EC 4.2.99.18) | DNA with an abasic site + 8-oxoguanine | - |
? |  |
| 3.2.2.B5 | DNA containing 8-oxoguanine + H2O | Pyrobaculum aerophilum DSM 7523 | bifunctional enzyme that catalyzes the excision of 8-oxoguanine by cleaving the N-glycosylic bond between the base and the deoxyribose moiety (glycosylase activity) and subsequently cleave the DNA backbone (lyase activity, EC 4.2.99.18) | DNA with an abasic site + 8-oxoguanine | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.2.2.B5 | Pyrobaculum aerophilum | Q8ZVK6 | - |
- |
| 3.2.2.B5 | Pyrobaculum aerophilum DSM 7523 | Q8ZVK6 | - |
- |
| 4.2.99.18 | Pyrobaculum aerophilum | Q8ZVK6 | - |
- |
| 4.2.99.18 | Pyrobaculum aerophilum DSM 7523 | Q8ZVK6 | - |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.2.2.B5 | DNA containing 8-oxoguanine + H2O | bifunctional enzyme that catalyzes the excision of 8-oxoguanine by cleaving the N-glycosylic bond between the base and the deoxyribose moiety (glycosylase activity) and subsequently cleave the DNA backbone (lyase activity, EC 4.2.99.18) | Pyrobaculum aerophilum | DNA with an abasic site + 8-oxoguanine | - |
? | |
| 3.2.2.B5 | DNA containing 8-oxoguanine + H2O | at 37°C and 47°C, the enzyme shows a slightly higher rate for the removal of 8-oxoguanine fom the double-stranded DNA substrate as compared to the single stranded substrate. At 5°C, the activity on 8-oxoguanine containing duplex DNA is much more strongly reduced than on the single-stranded substrate. For the double-stranded DNA substrates, the observed rate constants for both base excision and base excision/beta-lyase activity show a small but significant preference for 8-oxoguanine/G as against 8-oxoguanine/C and 8-oxoguanine/A | Pyrobaculum aerophilum | DNA with an abasic site + 8-oxoguanine | - |
? | |
| 3.2.2.B5 | DNA containing 8-oxoguanine + H2O | bifunctional enzyme that catalyzes the excision of 8-oxoguanine by cleaving the N-glycosylic bond between the base and the deoxyribose moiety (glycosylase activity) and subsequently cleave the DNA backbone (lyase activity, EC 4.2.99.18) | Pyrobaculum aerophilum DSM 7523 | DNA with an abasic site + 8-oxoguanine | - |
? | |
| 3.2.2.B5 | DNA containing 8-oxoguanine + H2O | at 37°C and 47°C, the enzyme shows a slightly higher rate for the removal of 8-oxoguanine fom the double-stranded DNA substrate as compared to the single stranded substrate. At 5°C, the activity on 8-oxoguanine containing duplex DNA is much more strongly reduced than on the single-stranded substrate. For the double-stranded DNA substrates, the observed rate constants for both base excision and base excision/beta-lyase activity show a small but significant preference for 8-oxoguanine/G as against 8-oxoguanine/C and 8-oxoguanine/A | Pyrobaculum aerophilum DSM 7523 | DNA with an abasic site + 8-oxoguanine | - |
? | |
| 4.2.99.18 | DNA with an abasic site | - |
Pyrobaculum aerophilum | ? | - |
? | |
| 4.2.99.18 | DNA with an abasic site | - |
Pyrobaculum aerophilum DSM 7523 | ? | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.2.2.B5 | Pa-AGOG DNA glycosylase | bifunctional enzyme that catalyzes the excision of 8-oxoguanine by cleaving the N-glycosylic bond between the base and the deoxyribose moiety (glycosylase activity) and subsequently cleave the DNA backbone (lyase activity, EC 4.2.99.18) | Pyrobaculum aerophilum |
| 4.2.99.18 | Pa-AGOG DNA glycosylase | bifunctional enzyme that catalyzes the excision of 8-oxoguanine by cleaving the N-glycosylic bond between the base and the deoxyribose moiety (glycosylase activity) and subsequently cleave the DNA backbone (lyase activity) | Pyrobaculum aerophilum |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.2.2.B5 | 78 | - |
Tm-value for mutant enzyme W69F | Pyrobaculum aerophilum |
| 3.2.2.B5 | 84 | - |
Tm-value for mutant enzyme D172Q | Pyrobaculum aerophilum |
| 3.2.2.B5 | 86 | - |
Tm-value for mutant enzyme Q31S | Pyrobaculum aerophilum |
| 3.2.2.B5 | 87 | - |
Tm-value for mutant enzyme Q31E/D218S | Pyrobaculum aerophilum |
| 3.2.2.B5 | 87 | - |
Tm-value for mutant enzyme W222A | Pyrobaculum aerophilum |
| 3.2.2.B5 | 88 | - |
Tm-value for mutant enzyme W222F | Pyrobaculum aerophilum |
| 3.2.2.B5 | 93 | - |
Tm-value for wild-type enzyme | Pyrobaculum aerophilum |
| 4.2.99.18 | 78 | - |
Tm-value for mutant enzyme W69F | Pyrobaculum aerophilum |
| 4.2.99.18 | 84 | - |
Tm-value for mutant enzyme D172Q | Pyrobaculum aerophilum |
| 4.2.99.18 | 86 | - |
Tm-value for mutant enzyme Q31S | Pyrobaculum aerophilum |
| 4.2.99.18 | 87 | - |
Tm-value for mutant enzyme Q31E/D218S | Pyrobaculum aerophilum |
| 4.2.99.18 | 87 | - |
Tm-value for mutant enzyme W222A | Pyrobaculum aerophilum |
| 4.2.99.18 | 88 | - |
Tm-value for mutant enzyme W222F | Pyrobaculum aerophilum |
| 4.2.99.18 | 93 | - |
Tm-value for wild-type enzyme | Pyrobaculum aerophilum |
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