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Literature summary for 3.1.1.3 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)

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

Protein Variants

Protein Variants Comment Organism
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
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
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
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
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
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
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
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

Organism UniProt Comment Textmining
Pseudomonas aeruginosa
-
-
-

Reaction

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

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
lipase
-
Pseudomonas aeruginosa

Temperature Optimum [°C]

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

pH Optimum

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