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Literature summary for 3.1.3.1 extracted from
- Activation of Pyrococcus furiosus alkaline phosphatase by divalent metal ions (2012), Biotechnol. Lett., 34, 2055-2060.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression of the wild-type enzyme in Escherichia coli BL21(DE3) | Pyrococcus furiosus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| EDTA | completely deactivates the enzyme | Pyrococcus furiosus |  |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | partly restores enzymatic activity after EDTA treatment. When Mg2+ is combined with Zn2+, it enhances the catalytic activity up to 3fold | Pyrococcus furiosus | |
| Co2+ | 50fold increase in activity compared with activity before EDTA treatment | Pyrococcus furiosus | |
| Mg2+ | partly restores enzymatic activity after EDTA treatment. When Mg2+ is combined with Zn2+, it enhances the catalytic activity up to 3fold | Pyrococcus furiosus | |
| Mn2+ | fully restores enzymatic activity after EDTA treatment | Pyrococcus furiosus | |
| Ni2+ | partly restores enzymatic activity after EDTA treatment | Pyrococcus furiosus | |
| Zn2+ | fully restores enzymatic activity after EDTA treatment | Pyrococcus furiosus | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Pyrococcus furiosus | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 4-nitrophenyl phosphate + H2O | - |
Pyrococcus furiosus | 4-nitrophenol + phosphate | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| PfuAP | - |
Pyrococcus furiosus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Pyrococcus furiosus |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 75 | - |
addition of Co2+ after treatment with EDTA results in an enzyme that has low tolerance toward heat treatment of more than 75°C, suggesting that Co2+ destabilizes the tertiary structure of the enzyme at high temperature | Pyrococcus furiosus |
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Release 2023.1 (January 2023)
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