EC Number   |
Protein Variants |
Reference |
|---|
   1.20.1.1 | R301K |
the mutant exhibits a slightly higher kcat than the wild type enzyme and a 20fold increased Km value for phosphonate |
-, 746256 |
| 1.20.1.1 | S295A |
mutant based on a 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, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation S295A leads to sharp decrease in activity, while kcat value is similar to wild-type |
726981 |
| 1.20.1.1 | T101A |
increases the half-life of thermal inactivation at 45°C from around 1 min to 4.5 min |
691424 |
| 1.20.1.1 | V315A |
thermostability almost identical to that of the wild-type enzyme |
691424 |
| 1.20.1.1 | V71Ia |
thermostability almost identical to that of the wild-type enzyme |
691424 |
| 1.20.1.1 | W134A |
mutant based on a 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, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation W134A leads to sharp decrease in activity, while kcat value is similar to wild-type |
-, 726981 |
| 1.20.1.1 | W134F |
mutant based on a 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, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation W134F leads to sharp decrease in activity, while kcat value is similar to wild-type |
726981 |
| 1.20.1.1 | Y139F |
mutant based on a 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, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation Y139F leads to sharp decrease in activity, while kcat value is similar to wild-type |
-, 726981 |
