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Literature summary for 3.1.3.1 extracted from

  • Angkawidjaja, C.; Kuwahara, K.; Omori, K.; Koga, Y.; Takano, K.; Kanaya, S.
    Extracellular secretion of Escherichia coli alkaline phosphatase with a C-terminal tag by type I secretion system: purification and biochemical characterization (2006), Protein Eng. Des. Sel., 19, 337-343.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
Escherichia coli alkaline phosphatase is fused to a C-terminal region of Pseudomonas sp. MIS38 lipase (PML) and examined for secretion using the Escherichia coli cells carrying the heterologous type I secretion system. PML is one of the passenger proteins of TISS and contains 12 repetitive sequences and a secretion signal at the C-terminal region. The fusion protein is efficiently secreted to the extracellular medium, while alkaline phosphatase is not secreted at all, indicating that the secretion of alkaline phosphatase is promoted by a secretion signal of Pseudomonas sp. MIS38 lipase. The fusion protein purified from the culture supernatant existed as a homodimer, like AP, and is indistinguishable from alkaline phosphatase in enzymatic properties and stability Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Subunits

Subunits Comment Organism
dimer
-
Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
60 70 wild-type enzyme and alkaline phosphatase fused to a C-terminal region of Pseudomonas sp. MIS38 lipase Escherichia coli

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
30 85 30°C: about 60% of maximal activity, 85°C: about 40% of maximal activity, wild-type enzyme and alkaline phosphatase fused to a C-terminal region of Pseudomonas sp. MIS38 lipase Escherichia coli

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
90
-
10 min, pH 8.5, containing 10 mM MgCl2 and 1 mM ZnSO4, about 50% loss of activity Escherichia coli
95
-
10 min, pH 8.5, containing 10 mM MgCl2 and 1 mM ZnSO4, aout 80% loss of activity Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
wild-type enzyme and alkaline phosphatase fused to a C-terminal region of Pseudomonas sp. MIS38 lipase Escherichia coli

pH Range

pH Minimum pH Maximum Comment Organism
7.5 9.5 pH 7.5: about 60% of maximal activity, pH 9.5: about 65% of maximal activity, wild-type enzyme and alkaline phosphatase fused to a C-terminal region of Pseudomonas sp. MIS38 lipase Escherichia coli