EC Number   |
Protein Variants |
Reference |
|---|
    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 |
682631 |
| 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 |
682631 |
| 3.1.1.3 | A217S |
the mutant movement of the lids is very similar to that in the wild-type lipase |
682482 |
| 3.1.1.3 | A9T |
random mutagenesis, the mutation of residue A9 results in only marginally affected thermostability and optimum reaction temperature compared to the wild-type enzyme |
681485 |
| 3.1.1.3 | A9T/E190V/M225I |
random mutagenesis, the mutation of residues A9 and M225 result in only marginally affected thermostability and optimum reaction temperature compared to the wild-type enzyme, while the mutation of E190 is critical for thermostability and optimum reaction temperature |
681485 |
| 3.1.1.3 | biofuel |
the high organic solvent stability and thermal stability suggest that this enzyme may have useful biodiesel-related applications |
694965 |
| 3.1.1.3 | D134S |
the mutant shows increased activity compared to the wild type enzyme |
715694 |
| 3.1.1.3 | D157A |
mutant lacks the Ca2+ binding site Ca1, is as stable as the wild type enzyme but exhibits less than 0.4% lipase activity |
-, 694953 |
| 3.1.1.3 | D20N/S53P/S155M/L162G/T180I/T234S |
site-directed mutagenesis, the mutant shows reduced enantioselectivity compared to the wild-type enzyme with substrates 4-nitrophenyl 4-cyclohexyl-2-methylbuta-2,3-dienoate and 4-nitrophenyl 2-methyldecanoate |
679192 |
| 3.1.1.3 | D260A |
the mutant shows reduced activity compared to the wild type enzyme |
-, 713808 |
