Protein Variants | Comment | Organism |
---|---|---|
additional information | mutant Fpg protein with NH2-terminal modifications | Escherichia coli |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Zn2+ | contains a single zinc finger motif near the C-terminus | Escherichia coli |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
34400 | - |
x * 34400, SDS-PAGE | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
DNA + H2O | Escherichia coli | DNA base excision repair enzyme | ? | - |
? | |
DNA + H2O | Escherichia coli JM109 | DNA base excision repair enzyme | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Escherichia coli JM109 | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Escherichia coli |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
DNA containing ring-opened N7-methylguanine + H2O = deguanylated DNA + 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine | catalytic mechanism | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
DNA + H2O | enzyme has N-glycosylase and apurinic/apyrimidinic lyase activity | Escherichia coli | ? | - |
? | |
DNA + H2O | DNA base excision repair enzyme | Escherichia coli | ? | - |
? | |
DNA + H2O | enzyme has N-glycosylase and apurinic/apyrimidinic lyase activity | Escherichia coli JM109 | ? | - |
? | |
DNA + H2O | DNA base excision repair enzyme | Escherichia coli JM109 | ? | - |
? | |
DNA containing 7-hydro-8-oxoguanine residues + H2O | mechanism involving protonation at O-6 of 8-oxodeoxyguanine | Escherichia coli | DNA + 7-hydro-8-oxoguanine | - |
? | |
DNA containing 7-hydro-8-oxoguanine residues + H2O | dublex 20-oligomer, catalytic mechanism with enzyme-substrate Schiff base intermediate, amino terminal localization of the catalytic site, C-8 keto group of 8-oxodeoxyguanine plays a critical role in binding enzyme | Escherichia coli | DNA + 7-hydro-8-oxoguanine | - |
? | |
DNA containing 7-hydro-8-oxoguanine residues + H2O | mechanism involving protonation at O-6 of 8-oxodeoxyguanine | Escherichia coli JM109 | DNA + 7-hydro-8-oxoguanine | - |
? | |
DNA containing 7-hydro-8-oxoguanine residues + H2O | dublex 20-oligomer, catalytic mechanism with enzyme-substrate Schiff base intermediate, amino terminal localization of the catalytic site, C-8 keto group of 8-oxodeoxyguanine plays a critical role in binding enzyme | Escherichia coli JM109 | DNA + 7-hydro-8-oxoguanine | - |
? | |
DNA containing ring-opened N7-methylguanine residues + H2O | amino terminal localization of the catalytic site | Escherichia coli | 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine + DNA | - |
? | |
DNA containing ring-opened N7-methylguanine residues + H2O | amino terminal localization of the catalytic site | Escherichia coli JM109 | 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine + DNA | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 34400, SDS-PAGE | Escherichia coli |