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Literature summary for 3.1.16.1 extracted from
- Expression and biochemical characterization of the Plasmodium falciparum DNA repair enzyme, flap endonuclease-1 (PfFEN-1) (2008), Mol. Biochem. Parasitol., 157, 1-12.
Application
| Application | Comment | Organism |
|---|---|---|
| additional information | Plasmodium FEN-1s have enzymatic activities similar to other species but contain extended C-termini and a more internally located proliferating cell nuclear antigen-binding site. FEN-1 homologs exhibit both endonuclease and exonuclease activities in vitro | Plasmodium falciparum |
| additional information | Plasmodium FEN-1s have enzymatic activities similar to other species but contain extended C-termini and a more internally located proliferating cell nuclear antigen-binding site. FEN-1 homologs exhibit both endonuclease and exonuclease activities in vitro | Plasmodium yoelii |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| FEN-1 cloned into the pCAL-n-FLAG expression vector and expressed in Escherichia coli BLR(DE3)pLysS cells. C-terminal truncation mutant cloned into pET24d(+) and expressed in Escherichia coli BL21(DE3)CodonPlus-RIL | Plasmodium falciparum |
| HIS6 tagged gene subcloned into pET24d(+) and expressed in Escherichia coli BL21(DE3)CodonPlus-RIL | Plasmodium yoelii |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | C-terminal truncation mutant lacking the terminal 250 amino acids has endonuclease activity that is ca. 130fold greater than full-length FEN-1 | Plasmodium falciparum |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| KCl | FEN-1 retains up to approximately 70.0% of its endonuclease at 0-50.0 mM, between 75 and 100 mM FEN-1 displays a significant reduction in activity and at the highest salt concentrations between 125-200 mM almost a complete ablation of activity occurres | Plasmodium falciparum |  |
| Mg2+ | inhibits above 20 mM | Plasmodium falciparum | |
| NaCl | FEN-1 retains up to approximately 70.0% of its endonuclease at 0-50.0 mM, between 75 and 100 mM FEN-1 displays a significant reduction in activity and at the highest salt concentrations between 125-200 mM almost a complete ablation of activity occurres | Plasmodium falciparum | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.0000038 | - |
Flap34endo | - |
Plasmodium falciparum | |
| 0.0000045 | - |
Flap34endo | C-terminal truncation mutant | Plasmodium falciparum | |
| 0.0000066 | - |
Flap34endo | - |
Plasmodium yoelii |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| additional information | expression of endogenous FEN-1 occurres in the ring, trophozoite, and schizont stages | Plasmodium falciparum | - |
- |
| nucleus | - |
Plasmodium falciparum | 5634 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | yields the highest activity for FEN-1 | Plasmodium yoelii | |
| Mg2+ | yields the highest activity for FEN-1, activity is stimulated above 0.1 mM, reaching a maximum at ca. 10 mM | Plasmodium falciparum | |
| Mn2+ | yields the highest activity for FEN-1 | Plasmodium falciparum | |
| additional information | Ni2+ or Mn2+ does not have a pronounced stimulatory effect | Plasmodium yoelii | |
| Ni2+ | minimally stimulates activity | Plasmodium falciparum | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 46000 | - |
C-terminal truncation mutant, Western blot analysis | Plasmodium falciparum |
| 54500 | - |
sequence analysis | Plasmodium yoelii |
| 75000 | - |
sequence analysis, Western blot analysis | Plasmodium falciparum |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Plasmodium falciparum | Q9GZ01 | - |
- |
| Plasmodium falciparum FCR-3/C5 | Q9GZ01 | - |
- |
| Plasmodium yoelii | Q7RME3 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| by cation exchange column and on Ni-NTA column | Plasmodium yoelii |
| FEN-1 purified by cation exchange column followed by a calmodulin affinity resin, more than 95% pure, C-terminal truncation mutant purified on Ni-NTA column and by cation exchange column, more than 95% pure | Plasmodium falciparum |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| DNA + H2O | - |
Plasmodium falciparum | deoxyribonucleoside 3'-phosphate + ? | - |
? | |
| DNA + H2O | - |
Plasmodium falciparum FCR-3/C5 | deoxyribonucleoside 3'-phosphate + ? | - |
? | |
| Flap34endo + H2O | - |
Plasmodium falciparum | ? | - |
? | |
| Flap34endo + H2O | - |
Plasmodium yoelii | ? | - |
? | |
| Flap34endo + H2O | - |
Plasmodium falciparum FCR-3/C5 | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| FEN-1 | - |
Plasmodium falciparum |
| FEN-1 | - |
Plasmodium yoelii |
| flap endonuclease-1 | - |
Plasmodium falciparum |
| flap endonuclease-1 | - |
Plasmodium yoelii |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 1.2 | - |
Flap34endo | C-terminal truncation mutant | Plasmodium falciparum | |
| 4.9 | - |
Flap34endo | - |
Plasmodium yoelii | |
| 9.1 | - |
Flap34endo | - |
Plasmodium falciparum |
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