EC Number |
Protein Variants |
Reference |
---|
1.14.13.22 | A245G/A288V |
variant retains native activity, exhibited about 4.4fold improvement in residual activity after 30°C incubation, and demonstrates about 5fold higher cyclohexanone conversion at 37°C compared to the wild-type |
764420 |
1.14.13.22 | A245G/A288V/T415C |
variant shows improved thermostability at 45°C |
764420 |
1.14.13.22 | A255C/A293C |
mutation results in an apparent Tm increase of 1.5°C |
742529 |
1.14.13.22 | A325C/L483C |
mutation results in an apparent Tm increase of 1.5°C |
742529 |
1.14.13.22 | D41N/F505Y |
site-directed mutagenesis, the mutant shows altered substrate specificity and enantioselectivity compared to the wild-type enzyme |
675581 |
1.14.13.22 | D57A |
variant retains stereospecificity for the proR hydrogen, substitution results in slow decomposition of the C4a-peroxyflavin intermediate in the presence of cyclohexanone |
764020 |
1.14.13.22 | E91Q/A115V/R280Y/N431Y/Q439P/A455V/S534R |
most stable mutant found, increase in unfolding temperature of 13 K and an approximately 33fold increase in half-life at 30°C |
764343 |
1.14.13.22 | E91Q/D95H/A115V/Q191M/R280Y/N431Y/Q439P/A455V/S534R |
increase in melting temperature of 15 K, highly diminished activity |
764343 |
1.14.13.22 | E91Q/D95H/A115V/R280Y/N431Y/Q439P/A455V/S534R |
increase in melting temperature of 13 K, highly active |
764343 |
1.14.13.22 | F246Y/K326C/L426F/F432L/T433A/L435S/S438I/F505L |
substrate specificity is markedly altered from substrate cyclohexanone toward the desired bulky substrate omeprazole sulfide despite an extremely poor activity |
763826 |