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Literature summary extracted from

  • Minamihata, K.; Goto, M.; Kamiya, N.
    Activation of Pyrococcus furiosus alkaline phosphatase by divalent metal ions (2012), Biotechnol. Lett., 34, 2055-2060.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.3.1 expression of the wild-type enzyme in Escherichia coli BL21(DE3) Pyrococcus furiosus

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.3.1 EDTA completely deactivates the enzyme Pyrococcus furiosus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.3.1 Ca2+ partly restores enzymatic activity after EDTA treatment. When Mg2+ is combined with Zn2+, it enhances the catalytic activity up to 3fold Pyrococcus furiosus
3.1.3.1 Co2+ 50fold increase in activity compared with activity before EDTA treatment Pyrococcus furiosus
3.1.3.1 Mg2+ partly restores enzymatic activity after EDTA treatment. When Mg2+ is combined with Zn2+, it enhances the catalytic activity up to 3fold Pyrococcus furiosus
3.1.3.1 Mn2+ fully restores enzymatic activity after EDTA treatment Pyrococcus furiosus
3.1.3.1 Ni2+ partly restores enzymatic activity after EDTA treatment Pyrococcus furiosus
3.1.3.1 Zn2+ fully restores enzymatic activity after EDTA treatment Pyrococcus furiosus

Organism

EC Number Organism UniProt Comment Textmining
3.1.3.1 Pyrococcus furiosus
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.3.1 4-nitrophenyl phosphate + H2O
-
Pyrococcus furiosus 4-nitrophenol + phosphate
-
?

Synonyms

EC Number Synonyms Comment Organism
3.1.3.1 PfuAP
-
Pyrococcus furiosus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.3.1 37
-
assay at Pyrococcus furiosus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.1.3.1 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