EC Number   |
Protein Variants |
Reference |
|---|
    1.1.1.27 | A96L/N212K |
mutation increases Km value and eliminates substrate inhibition |
760746 |
| 1.1.1.27 | C210S |
crystallization of mutant enzyme |
286467 |
| 1.1.1.27 | D241N |
site-directed mutagenesis, the mutant hsows higher activity at pH above 5.5 compared to the wild-type enzyme |
-, 740460 |
| 1.1.1.27 | D38E |
site-directed mutagenesis, the mutant shows a twofold reduced substrate inhibition by pyruvate compared to the wild-type enzyme |
684519 |
| 1.1.1.27 | D38R |
site-directed mutagenesis, the mutant shows a threefold reduced substrate inhibition by pyruvate compared to the wild-type enzyme |
684519 |
| 1.1.1.27 | D8G |
no measurable effect on the Km value for pyruvate, increased thermal stability |
286463 |
| 1.1.1.27 | E60Q |
site-directed mutagenesis, the mutant has a similar pH prodile as the wild-type |
-, 740460 |
| 1.1.1.27 | F16Q/C81S/N85R |
catalytic efficiency is higher than that of wild-type enzyme, utilizes NAD+ better than wild-type enzyme, weakly active wth NADP+ |
670748 |
| 1.1.1.27 | F16Q/I37K/D38S/C81S/N85R |
utilizes NADP+ better than wild-type enzyme, prefers NADP+ to NAD+ |
670748 |
| 1.1.1.27 | H171C |
site-directed mutagenesis |
721235 |
