EC Number |
Protein Variants |
Reference |
---|
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 |