EC Number   |
Protein Variants |
Reference |
|---|
   3.5.5.5 | A114F |
inactive |
710940 |
| 3.5.5.5 | A116C |
the mutant shows activity similar to the wild type enzyme |
710940 |
| 3.5.5.5 | A116F |
the mutant shows about 50% of wild type activity |
710940 |
| 3.5.5.5 | A136Y |
mutant enzyme shows reversed selectivity and preferentially produces (R)-mandelic acid with an enantiomeric excess values of 66.7% |
-, 755936 |
| 3.5.5.5 | A136Y/I168Y |
mutant enzyme produces (R)-mandelic acid with an enantiomeric excess value of 89.7%, an R-enantioselectivity higher than that obtained with the single mutations A136Y and I168Y |
755936 |
| 3.5.5.5 | A136Y/I168Y/M113G |
mutant enzyme with R-selectivity, 90.9% enantiomeric excess |
755936 |
| 3.5.5.5 | A165E |
mutant with very low activities toward (R,S)-mandelonitrile and substrate (R,S)-2-phenylpropionitrile |
710930 |
| 3.5.5.5 | A165F |
decreased degree of amide formation compared to the wild type enzyme and forms about 3% phenylglycine amide from (R,S)-phenylglycinonitrile. In contrast to the wild-type enzyme, the variant almost exclusively forms (R)-phenylglycine. This point mutation results in an almost complete stereoinversion of the reaction |
-, 755880 |
| 3.5.5.5 | A165F |
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 | A165G |
the mutant forms 4.3% amide and thus produces significantly more amide than the wild type enzyme with the substrate (R,S)-2-phenylpropionitrile |
710930 |
