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 | 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 | UniProt | Comment | Textmining |
---|---|---|---|
Pseudomonas aeruginosa | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
triacylglycerol + H2O = diacylglycerol + a carboxylate | structure-function relationship | Pseudomonas aeruginosa |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
activity of mutant enzymes, overview | Pseudomonas aeruginosa |
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 | Comment | Organism |
---|---|---|
lipase | - |
Pseudomonas aeruginosa |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Pseudomonas aeruginosa |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
assay at | Pseudomonas aeruginosa |