EC Number   |
Protein Variants |
Reference  |
|---|
    1.2.1.79 | C262A |
active site mutation, nonfunctional because Cys-262 acts as a nucleophilel |
725523 |
| 1.2.1.79 | E228A |
active site mutation, nonfunctional because Glu-228 acts as a general base |
725523 |
| 1.2.1.79 | E228Q |
active site mutation, nonfunctional because Glu-228 acts as a general base |
725523 |
| 1.2.1.79 | F132A |
activity of about 1030% of the wild type enzyme, indicating a contribution of these succinic semialdehyde binding residues to the overall enzyme activity |
725523 |
| 1.2.1.79 | F425A |
inactive, suggesting that Phe-425 plays an important role in substrate binding |
725523 |
| 1.2.1.79 | I263A |
activity of about 1030% of the wild type enzyme, indicating a contribution of these succinic semialdehyde binding residues to the overall enzyme activity |
725523 |
| 1.2.1.79 | N131A |
mutation of a residue that interacts with the O4 atom or the carboxyl group of succinic semialdehyde thus abolishing enzyme activity |
725523 |
| 1.2.1.79 | N131D |
mutation of a residue that interacts with the O4 atom or the carboxyl group of succinic semialdehyde thus abolishing enzyme activity |
725523 |
| 1.2.1.79 | R139A |
activity of about 1030% of the wild type enzyme, indicating a contribution of these succinic semialdehyde binding residues to the overall enzyme activity |
725523 |
| 1.2.1.79 | R139K |
mutant enzyme exhibited an activity up to 80% that of the wild type enzyme, suggesting the significance of a positively charged residue in the binding of the carboxyl group of succinic semialdehyde |
725523 |
