EC Number   |
Protein Variants |
Reference |
|---|
    2.2.1.7 | D430A |
the mutant shows 9 and 50% of wild type activity for D-glyceraldehyde 3-phosphate and pyruvate, respectively |
756018 |
| 2.2.1.7 | D430A |
while the kcat for D430A mutant remains relatively unchanged, the KM for pyruvate and D-glyceraldehyde 3-phosphate increases 1.9 and 2.4times, respectively. The mutant shows 97.3% and 97.5% catalytic efficiency for pyruvate and D-glyceraldehyde 3-phosphate, respectively |
-, 757477 |
| 2.2.1.7 | H299A |
the mutant shows reduced activity compared to the wild type enzyme |
756065 |
| 2.2.1.7 | H299N |
the mutant shows reduced activity compared to the wild type enzyme |
756065 |
| 2.2.1.7 | H304A |
the mutant produces a catalytically defective enzyme. The mutant shows 12.1% and 11.4% catalytic efficiency for pyruvate and D-glyceraldehyde 3-phosphate, respectively |
-, 757477 |
| 2.2.1.7 | H340A |
the mutant shows 7 and 2% of wild type activity for D-glyceraldehyde 3-phosphate and pyruvate, respectively |
756018 |
| 2.2.1.7 | H434A |
the electrostatic effects that accompany the H434A mutation have a clear destabilizing effect on substrate binding while enhancing turnover. The mutant shows 133.8% and 121.5% catalytic efficiency for pyruvate and D-glyceraldehyde 3-phosphate, respectively |
-, 757477 |
| 2.2.1.7 | H434A |
the mutant shows 30 and more than 20% of wild type activity for D-glyceraldehyde 3-phosphate and pyruvate, respectively |
-, 756018 |
| 2.2.1.7 | H48A |
mutant protein with lost activity, below 0.1% of specific activity compared with that of the wild-type |
674982 |
| 2.2.1.7 | H49A |
the mutant shows reduced activity compared to the wild type enzyme |
756065 |
