EC Number   |
Protein Variants |
Reference |
|---|
   1.11.2.1 | A161L |
the mutant substantially diminishes the 4- and 3-octanol formation from octane while preserving the 2-octanol regioisomer formation as compared to the wild type enzyme |
764414 |
| 1.11.2.1 | F12Y/A14V/R15G/A21D/V57A/L67F/V75I/I248V/F311L |
the mutant enzyme exhibits enhanced activity, secretion and stability compared to the wild type enzyme |
743724 |
| 1.11.2.1 | F12Y/A14V/R15G/A21D/V57A/L67F/V75I/I248V/F311L |
the variant carries nine mutations that enhance its activity in the presence of 30% acetonitrile (v/v) up to 23fold over parental type. The mutant is also active and stable in aqueous acetone, methanol and dimethyl sulfoxide mixtures |
764347 |
| 1.11.2.1 | F12Y/A14V/R15GA21D/V57A/L67F/V75I/I248V/F311L |
this mutant retains strong activity and stability, particularly in terms of temperature and the presence of co-solvents, compared to the wild type enzyme |
742286 |
| 1.11.2.1 | F154V |
the mutant demonstrates 1.8fold improved turnover numbers for formation of the 4-octanol regioisomer relative to the wild type enzyme. Also, a 1.5 and 4fold decreased formation of 3- and 2-octanol, respectively, are observed |
764414 |
| 1.11.2.1 | F310A/A320Q |
site-directed mutagenesis, the mutant exhibits a 30 mV positive shift in redox potential for the FeIII/FeII couple compared with wild-type P450st due to weakening of the electron-donating effect (push effect) of the proximal thiolate in the mutant. This result indicates that the electron density around the heme is decreased, and thus the Lewis acidity of the heme is expected to be increased. Mutant F310A/A320Q maintains higher thermal stability than typical P450s |
-, 744870 |
| 1.11.2.1 | F310A/A320Q |
specific activity of peroxygenase is significantly increased over a broad pH-range. The pH dependence of the reaction is altered to bell shaped, with maximum activities near pH 5. At pH 5, the mutant is over 15 times more active than wild-type P450st |
-, 724982 |
| 1.11.2.1 | F59Q/L60F/S159G |
the mutant shows 2.6fold improved conversion efficiency with 5-nitro-1,3-benzodioxole as compared to the wild type enzyme |
763793 |
| 1.11.2.1 | F59Q/L60M/S159G/F154A |
the mutant shows 2.7fold improved conversion efficiency with 5-nitro-1,3-benzodioxole as compared to the wild type enzyme |
763793 |
| 1.11.2.1 | F88L |
the mutant shows reduced mono-epoxide production compared to the wild type enzyme |
763908 |
