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Literature summary for 3.1.99.B1 extracted from
- Newly discovered archaebacterial flap endonucleases show a structure-specific mechanism for DNA substrate binding and catalysis resembling human flap endonuclease-1 (1998), J. Biol. Chem., 273, 27154-27161.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli | Archaeoglobus fulgidus |
| expression in Escherichia coli | Methanocaldococcus jannaschii |
| expression in Escherichia coli | Pyrococcus furiosus |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | kinetic parameters for flap substrate cleavage | Archaeoglobus fulgidus | |
| additional information | - |
additional information | kinetic parameters for flap substrate cleavage | Methanocaldococcus jannaschii | |
| additional information | - |
additional information | kinetic parameters for flap substrate cleavage | Pyrococcus furiosus |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | endonucleolytic cleavage of flap substrate is only supported by Mg2+ and Mn2+, the cleavage site preferences for each enzyme is altered in the presence of Mn2+ | Archaeoglobus fulgidus |  |
| Mg2+ | endonucleolytic cleavage of flap substrate is only supported by Mg2+ and Mn2+, the cleavage site preferences for each enzyme is altered in the presence of Mn2+ | Methanocaldococcus jannaschii | |
| Mg2+ | endonucleolytic cleavage of flap substrate is only supported by Mg2+ and Mn2+, the cleavage site preferences for each enzyme is altered in the presence of Mn2+ | Pyrococcus furiosus | |
| Mn2+ | endonucleolytic cleavage of flap substrate is only supported by Mg2+ and Mn2+, the cleavage site preferences for each enzyme is altered in the presence of Mn2+ | Archaeoglobus fulgidus | |
| Mn2+ | endonucleolytic cleavage of flap substrate is only supported by Mg2+ and Mn2+, the cleavage site preferences for each enzyme is altered in the presence of Mn2+ | Methanocaldococcus jannaschii | |
| Mn2+ | endonucleolytic cleavage of flap substrate is only supported by Mg2+ and Mn2+, the cleavage site preferences for each enzyme is altered in the presence of Mn2+ | Pyrococcus furiosus | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Archaeoglobus fulgidus | O29975 | - |
- |
| Methanocaldococcus jannaschii | Q58839 | - |
- |
| Pyrococcus furiosus | O93634 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Archaeoglobus fulgidus |
- |
Methanocaldococcus jannaschii |
- |
Pyrococcus furiosus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | the archaebacterial FEN-1 binds to flap, pseudo Y, 3' overhang, and nicked DNA structures. It binds weakly to 5' overhangs and shows no apparent affinity toward either single-stranded or duplex DNA | Archaeoglobus fulgidus | ? | - |
? | |
| additional information | the archaebacterial FEN-1 binds to flap, pseudo Y, 3' overhang, and nicked DNA structures. It binds weakly to 5' overhangs and shows no apparent affinity toward either single-stranded or duplex DNA | Methanocaldococcus jannaschii | ? | - |
? | |
| additional information | the archaebacterial FEN-1s bind to flap, pseudo Y, 3' overhang, and nicked DNA structures. It binds weakly to 5' overhangs and shows no apparent affinity toward either single-stranded or duplex DNA | Pyrococcus furiosus | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| FEN-1 | - |
Archaeoglobus fulgidus |
| FEN-1 | - |
Methanocaldococcus jannaschii |
| FEN-1 | - |
Pyrococcus furiosus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 35 | - |
enzyme begins to show activity at temperatures above 35 °C | Archaeoglobus fulgidus |
| 35 | - |
enzyme begins to show activity at temperatures above 35 °C | Pyrococcus furiosus |
| 55 | - |
assay at | Archaeoglobus fulgidus |
| 55 | - |
assay at | Methanocaldococcus jannaschii |
| 55 | - |
assay at | Pyrococcus furiosus |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 35 | - |
enzyme begins to show activity at temperatures above 35 °C | Methanocaldococcus jannaschii |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | 8.8 | - |
Pyrococcus furiosus |
| 8.8 | - |
- |
Archaeoglobus fulgidus |
| 8.8 | - |
- |
Methanocaldococcus jannaschii |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 5 | 9.5 | pH 5.0: 38% of maximal activity, pH 9.5: 56% of maximal activity | Pyrococcus furiosus |
| 5 | 9.5 | pH 5.0: 65% of maximal activity, pH 9.5: 21% of maximal activity | Archaeoglobus fulgidus |
| 5.7 | 9.5 | pH 7.7: 77% of maximal activity, pH 9.5: 91% of maximal activity | Methanocaldococcus jannaschii |
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