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Literature summary for 3.1.3.41 extracted from

  • Bramkamp, M.; Gassel, M.; Altendorf, K.
    FITC binding site and p-nitrophenyl phosphatase activity of the Kdp-ATPase of Escherichia coli (2004), Biochemistry, 43, 4559-4567.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
ATP stimulates the 4-nitrophenyl phosphatase activity 3.5fold at concentrations of 0.001-0.030 mM, but inhibits it at concentrations above 0.5 mM, mechanism Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
ATP stimulates the 4-nitrophenyl phosphatase activity at concentrations of 0.001-0.030 mM, but inhibits it at concentrations above 0.5 mM, mechanism Escherichia coli
Fluorescein isothiocyanate i.e. FITC, inhibits both the ATPase and 4-nitrophenyl phosphatase activities of the enzyme, fluorescence labeling, inhibition depends on pH Escherichia coli
o-vanadate inhibits the 4-nitrophenyl phosphatase activity Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ the 4-nitrophenyl phosphatase activity is dependent on Mg2+ Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4-nitrophenyl phosphate + H2O Escherichia coli
-
4-nitrophenol + phosphate
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl phosphate + H2O
-
Escherichia coli 4-nitrophenol + phosphate
-
?
additional information the Kdp-ATPase, i.e. KdpA, the potassium channel part of the KdpFABC complex, of Escherichia coli shows 4-nitrophenyl phosphatase activity Escherichia coli ?
-
?

Synonyms

Synonyms Comment Organism
p-nitrophenyl phosphatase
-
Escherichia coli
pNPP
-
Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at, 4-nitrophenyl phosphatase activity Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.8
-
assay at, 4-nitrophenyl phosphatase activity Escherichia coli

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.0022
-
o-vanadate pH 7.8, 37°C, inhibition of 4-nitrophenyl phosphatase activity Escherichia coli
0.5
-
ATP about, pH 7.8, 37°C, inhibition of 4-nitrophenyl phosphatase activity Escherichia coli