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