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Literature summary extracted from

  • Fujii, R.; Nakagawa, Y.; Hiratake, J.; Sogabe, A.; Sakata, K.
    Directed evolution of Pseudomonas aeruginosa lipase for improved amide-hydrolyzing activity (2005), Protein Eng. Des. Sel., 18, 93-101.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.1.3 subcloning in Escherichia coli strains DH5alpha and JM109, expression of wild-type and mutant enzymes in Pseudomonas aeruginosa strain PAO1162 Pseudomonas aeruginosa

Protein Variants

EC Number Protein Variants Comment Organism
3.1.1.3 A213D random mutagenesis, the mutation occurs at the sites near the surface and remote from the catalytic triad, but close to the calcium binding site, and leads to increased amidase activity of the enzyme Pseudomonas aeruginosa
3.1.1.3 A213D/F265L random mutagenesis, the mutation occurs at the sites near the surface and remote from the catalytic triad, but close to the calcium binding site, and leads to increased amidase activity of the enzyme Pseudomonas aeruginosa
3.1.1.3 F207S random mutagenesis, the mutation occurs at the sites near the surface and remote from the catalytic triad, but close to the calcium binding site, and leads to increased amidase activity of the enzyme Pseudomonas aeruginosa
3.1.1.3 F207S/A213D random mutagenesis, the mutation occurs at the sites near the surface and remote from the catalytic triad, but close to the calcium binding site, and leads to increased amidase activity of the enzyme Pseudomonas aeruginosa
3.1.1.3 F207S/A213D/F265L random mutagenesis, the mutation occurs at the sites near the surface and remote from the catalytic triad, but close to the calcium binding site, and leads to increased amidase activity of the enzyme Pseudomonas aeruginosa
3.1.1.3 F207S/F265L random mutagenesis, the mutation occurs at the sites near the surface and remote from the catalytic triad, but close to the calcium binding site, and leads to increased amidase activity of the enzyme Pseudomonas aeruginosa
3.1.1.3 F265L random mutagenesis, the mutation occurs at the sites near the surface and remote from the catalytic triad, but close to the calcium binding site, and leads to increased amidase activity of the enzyme Pseudomonas aeruginosa
3.1.1.3 P96H/F207S random mutagenesis, double mutation plus an additional silent mutation, the mutation occurs at the sites near the surface and remote from the catalytic triad, but close to the calcium binding site, and leads to increased amidase activity of the enzyme Pseudomonas aeruginosa

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.3 Pseudomonas aeruginosa
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
3.1.1.3 triacylglycerol + H2O = diacylglycerol + a carboxylate structure-function relationship Pseudomonas aeruginosa

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.1.1.3 additional information
-
activity of mutant enzymes, overview Pseudomonas aeruginosa

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.3 oleoyl 2-naphthyl ester + H2O
-
Pseudomonas aeruginosa oleic acid + 2-naphthol
-
?
3.1.1.3 oleoyl 2-naphthylamide + H2O
-
Pseudomonas aeruginosa oleic acid + 2-naphthylamine
-
?

Synonyms

EC Number Synonyms Comment Organism
3.1.1.3 lipase
-
Pseudomonas aeruginosa

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.1.3 30
-
assay at Pseudomonas aeruginosa

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.1.3 7
-
assay at Pseudomonas aeruginosa