EC Number   |
Protein Variants |
Reference |
|---|
   4.1.2.47 | E79A |
no difference can be observed in the electrophoretic mobilities between the wild-type and mutant protein on native polyacrylamide gels and by isoelectric focusing. Mutation greatly reduces, but does not abolish activity. The negative charge provided by Glu-79 may be required in the active site, but a direct participation of this residue in enzyme catalysis is not suggested |
706644 |
| 4.1.2.47 | F125T |
2.6fold increase in kcat for racemic mandelonitrile, 4.5fold increase in specificity constants (kcat/Km) for racemic mandelonitrile |
747531 |
| 4.1.2.47 | F125T |
the mutant has high enantioselectivity towards (R)-mandelonitrile with a kcat value 2.6times and a kcat/Km value 4.5times higher compared to the wild type enzyme |
747531 |
| 4.1.2.47 | F125T/L146M |
the mutant shows higher specific activity towards racemic mandelonitrile compared to the wild type enzyme |
747531 |
| 4.1.2.47 | F125T/Y133F |
the mutant shows higher specific activity towards racemic mandelonitrile compared to the wild type enzyme |
747531 |
| 4.1.2.47 | F210I |
mutant yields mostly insoluble protein, which suggests that the substitution hinders protein folding |
747531 |
| 4.1.2.47 | F210I |
the mutant shows lower specific activity towards racemic mandelonitrile compared to the wild type enzyme |
747531 |
| 4.1.2.47 | G113S |
enhanced thermal stability compared to wild-type enzyme, mutant enzyme retains slight higher activity than the wild-type enzyme in an acidic environment, so the mutant enzyme maybe more effective for synthesis of (S)-cyanohydrin than the wild-type enzyme |
650692 |
| 4.1.2.47 | H103C |
the mutant displays 9.3fold increase in total specific activity in the cell-free extract compared with the wild type |
716823 |
| 4.1.2.47 | H103C |
the mutated enzyme shows low enantioselectivity and specific activity for (S)-mandelonitrile synthesis. (S)-Mandelonitrile enantiomeric excess is 60% |
747534 |
