EC Number   |
Protein Variants |
Reference |
|---|
   3.5.5.5 | A165H |
the mutant enzyme shows a significantly increased relative activity for mandelonitrile (compared to (R,S)-2-phenylpropionitrile) |
710930 |
| 3.5.5.5 | A165R |
mutant with very low activities toward (R,S)-mandelonitrile and substrate (R,S)-2-phenylpropionitrile |
710930 |
| 3.5.5.5 | A165W |
the mutant enzyme converts racemic mandelonitrile and (R,S)-2-phenylpropionitrile to increased amounts of the R enantiomers of the corresponding acids |
710930 |
| 3.5.5.5 | A165Y |
the mutant enzyme converts racemic mandelonitrile and (R,S)-2-phenylpropionitrile to increased amounts of the R enantiomers of the corresponding acids |
710930 |
| 3.5.5.5 | C163A |
the mutation results in significantly decreased amounts of amides formed using (R,S)-mandelonitrile and (R,S)-2-phenylpropionitrile as substrates. The mutant demonstrates no significant difference in the enzyme activity compared to the wild type, but shows an extremely low degree of enantioselectivity for the formation of (R)-mandelic acid |
710940 |
| 3.5.5.5 | C163G |
site-directed mutagenesis |
-, 719629 |
| 3.5.5.5 | C163N |
the mutation results in significantly increased amounts of amides formed using (R,S)-mandelonitrile and (R,S)-2-phenylpropionitrile as substrates |
710940 |
| 3.5.5.5 | C163N/A165R |
the mutant demonstrates increased amide formation capacity in comparison to the mutants carrying only single mutations |
710940 |
| 3.5.5.5 | C163N/W110I |
the mutant enzyme forms about 100fold more 2-phenylpropionamide (in relation to the total amount of (R,S)-2-phenylpropionitrile converted) than the wild type, although the relative activity of this mutant for the conversion (R,S)-2-phenylpropionitrile to 2-phenylpropionic acid is only 4% of that observed for the wild type |
710940 |
| 3.5.5.5 | C163Q |
the mutation results in significantly increased amounts of amides formed using (R,S)-mandelonitrile and (R,S)-2-phenylpropionitrile as substrates |
710940 |
