EC Number   |
Protein Variants |
Reference |
|---|
    2.7.2.3 | A199V |
the mutant shows a significant decrease of the catalytic efficiency compared to the wild type enzyme |
762240 |
| 2.7.2.3 | C108S |
site-directed mutagenesis, the mutant enzyme is almost completely inactive under oxidizing conditions (DTTox), but is strongly reactivated in the presence of DTTred, suggesting that the absence of Cys108 does not alter the sensitivity of the protein to the redox environment |
738628 |
| 2.7.2.3 | C214S |
similar Vmax as wild-type, mutant behaves in a similar way as wild-type towards oxidants |
723744 |
| 2.7.2.3 | C216A |
activity comparable to wild-type, shows a similar redox profile to the wild-type. Analyses of the redox situation of the cysteine using the AMS labeling method reveal two different redox states of the enzyme molecule: wild type and three mutants, C216A, C314A and C340A, show three bands on the gel, oxidized, intermediate and reduced forms, as a function of the redox treatment |
723395 |
| 2.7.2.3 | C21S |
similar Vmax as wild-type, mutant displays slightly lower affinity toward 3-phospho-D-glycerate, mutant behaves in a similar way as wild-type towards oxidants |
723744 |
| 2.7.2.3 | C227S |
site-directed mutagenesis, the mutant is contitutively active and is totally insensitive to oxidizing treatments, and no variation of protein activity is observed after incubation with DTTred. Absence of Cys227 allows the mutant proteins to maintain a fully active conformation comparable with the reduced wild-type enzyme |
738628 |
| 2.7.2.3 | C312S |
similar Vmax as wild-type, mutant behaves in a similar way as wild-type towards oxidants |
723744 |
| 2.7.2.3 | C314A |
activity comparable to wild-type. Analyses of the redox situation of the cysteine using the AMS labeling method reveal two different redox states of the enzyme molecule: wild type and three mutants, C216A, C314A and C340A, show three bands on the gel, oxidized, intermediate and reduced forms, as a function of the redox treatment |
723395 |
| 2.7.2.3 | C314A/C340A |
redox change in activity of the double mutant is largely suppressed |
723395 |
| 2.7.2.3 | C340A |
activity comparable to wild-type, activity of the mutant C340A is almost insensitive to redox change. Analyses of the redox situation of the cysteine using the AMS labeling method reveal two different redox states of the enzyme molecule: wild type and three mutants, C216A, C314A and C340A, show three bands on the gel, oxidized, intermediate and reduced forms, as a function of the redox treatment |
723395 |
