1.20.1.1	D13E/M26I/E332N/C336D	mutant obtained by directed evolution, round 3	673144	
1.20.1.1	D13E/M26I/V71I/E130K/Q132R/Q137R/I150F/E175A/Q215L/R275Q/L276Q/I313L/V315A/A319E/A325V/E332N/C336D	thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity. Mutation E175A leads to relaxation of cofactor specificity	726982	
1.20.1.1	D79A	significant differences in its kinetic constants compared to the wild-type enzyme. 2600fold decrease in catalytic efficiency. Pre-steady-state rates are approximately the same as the steady-state rates	-, 690884	
1.20.1.1	D79N	has kinetic parameters more similar to those of wild-type	690884	
1.20.1.1	E130K	increases the half-life of thermal inactivation at 45°C from around 1 min to 12.5 min	691424	
1.20.1.1	E130Q	increases the half-life of thermal inactivation at 45°C from around 1 min to 7 min	691424	
1.20.1.1	E130R	increases the half-life of thermal inactivation at 45°C from around 1 min to 9 min	691424	
1.20.1.1	E175A	increases solubility and activity, thermostability almost identical to that of the wild-type enzyme	691424	
1.20.1.1	E175A	mutant with significantly increased kcat value for NADP+	673144	
1.20.1.1	E175A	strongly decreased Km for NADP+	657956