EC Number   |
Protein Variants |
Reference |
|---|
    5.3.1.1 | 170-173del |
loop deletion mutant, 800000fold decrease in kcat/Km value |
747069 |
| 5.3.1.1 | A178L |
decrease in catalytic efficiency. Crystallization data reveal a more disordered loop-6 in the structure of unliganded A178L. Liganded structures show minimal differences to wild-type |
690232 |
| 5.3.1.1 | A238S |
catalytic efficiency of the mutant enzyme is somewhat reduced, and its stability is considerably increased. The half-life at 25°C is 27 min compared to 10 min for the wild-type enzyme |
2586 |
| 5.3.1.1 | A238S |
mutant enzyme A238S has a higher thermal stability than the wild-type enzyme. The turnover number of the mutant enzyme is somewhat lower than that observed for the wild-type enzyme, the Km-value for D-glyceraldehyde 2-phosphate is somewhat higher |
2586 |
| 5.3.1.1 | C126A |
the mutant shows an approximately 5.8fold drop in kcat compared to the wild type enzyme |
714976 |
| 5.3.1.1 | C126A |
turnover number for D-glyceraldehyde 3-phosphate is 1.5fold lower than the wild-type value, KM-value for D-glyceraldehyde 3-phosphate is 1.4fold lower than the wild-type value, turnover number for dihydroxyacetone phosphate is 4.3fold lower than the wild-type value, KM-value for dihydroxyacetone phosphate is 3.7fold lower than the wild-type value |
661120 |
| 5.3.1.1 | C126M |
the mutant shows an approximately 10fold drop in catalytic activity compared to the wild type enzyme |
714976 |
| 5.3.1.1 | C126S |
mutant enzyme shows greater susceptibility to thermal denaturation than wild-type enzyme, turnover number for dihydroxyacetone phosphate is 8.3fold lower than the wild-type value, KM-value for dihydroxyacetone phosphate is 3.5fold lower than the wild-type value |
661120 |
| 5.3.1.1 | C126S |
the mutant shows an approximately 5.8fold drop in kcat compared to the wild type enzyme |
714976 |
| 5.3.1.1 | C126T |
the mutant shows an approximately 10fold drop in catalytic activity compared to the wild type enzyme |
714976 |
