EC Number |
Protein Variants |
Reference |
---|
2.6.1.18 | R414K |
19.9% of wild-type activity with substrate beta-alanine, 9.6% with substrate cadaverine, 20.5% with substrate 1,3-diaminopropane |
-, 737507 |
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 | more |
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 |