EC Number   |
Protein Variants |
Reference |
|---|
   3.1.1.74 | A102D/Q105R/G106E |
pH-optima for activity and stability are identical to wild-type enzym. Improvement in Tm-value of 3.4°C. Increased half-life at 6°C relative to the wild-type enzyme of approximately 3fold |
-, 752140 |
| 3.1.1.74 | A102D/Q105R/G106E/N133A/S140P/E161T/A166P |
large improvement of stability at 60°C |
752140 |
| 3.1.1.74 | A102D/Q105R/G106E/N133A/S140P/E161T/A166P/K137E |
large improvement of stability at 60°C |
752140 |
| 3.1.1.74 | A102D/Q105R/G106E/Q98N/A99D/E109Q |
thermodynamically most stable variant, improving on wild-type enzyme by 6.7 kJ/mol |
752140 |
| 3.1.1.74 | A164E |
amino acid substitution, 74% of wild-type activity |
694949 |
| 3.1.1.74 | A164R |
41% of the activity of the wild-type enzyme |
208333 |
| 3.1.1.74 | A164R |
site-directed mutagenesis, the mutant shows 59% reduced activity in olive oil compared to the wild-type enzyme |
729450 |
| 3.1.1.74 | A178P/V179P |
loss of stability and activity |
752140 |
| 3.1.1.74 | A185L |
96% of the activity of the wild-type enzyme |
208333 |
| 3.1.1.74 | A185L |
site-directed mutagenesis, the mutant shows unaltered activity in olive oil compared to the wild-type enzyme |
729450 |
