2.6.1.18	D392K	site-directed mutagenesis, slightly reduced activity compared to wild-type enzyme	759057	
2.6.1.18	E345F	site-directed mutagenesis, reduced activity compared to wild-type enzyme	759057	
2.6.1.18	E391K	site-directed mutagenesis, reduced activity compared to wild-type enzyme	759057	
2.6.1.18	G165M	best DELTADELTAG prediction, the mutant shows a 3.3fold reduction in enzymatic activity and an only a slight improvement in the Tm value, which stresses the importance of experimental evaluation of the theoretical data	759057	
2.6.1.18	G165M	site-directed mutagenesis, reduced activity compared to wild-type enzyme	759057	
2.6.1.18	G98M	site-directed mutagenesis, slightly reduced activity compared to wild-type enzyme	759057	
2.6.1.18	G98M/D392K	site-directed mutagenesis, reduced activity compared to wild-type enzyme	759057	
2.6.1.18	G98M/E345F	site-directed mutagenesis, reduced activity compared to wild-type enzyme	759057	
2.6.1.18	additional information	development of beta-phenylalanine ester synthesis method from stable beta-keto ester substrate using engineered omega-transaminase. The omega-transaminase mutants 3FCR_4M and ATA117 11Rd show great potential for further engineering experiments aiming at the synthesis of chiral (S)- and (R)-phenylalanine esters. This alternative approach results in the conversion of 32% and 13% for the (S)- and (R)-enantiomer, respectively. Furthermore, the (S)-phenylalanine ethyl ester is isolated by performing a semi-preparative synthesis	759802	
2.6.1.18	additional information	synthesis and optical resolution of beta-phenylalanine and other important aromatic beta-amino acids by biotransformation utilizing an omega-transaminase (omega-TA) from Variovorax paradoxus. Design of mutant variants of the omega-TA to gain higher process stability on the basis of predictions calculated by using the FoldX software. Thermostabilization of a nonthermostable S-selective omega-TA by FoldX-guided site-directed mutagenesis. The melting point (Tm) of the best-performing mutant is increased to 59.3°C, an increase of 4.0°C relative to the Tm value of the wild-type enzyme, whereby the mutant fully retains its specific activity	759057