EC Number   |
Protein Variants |
Reference |
|---|
    5.3.3.2 | R51K |
the ratio of maximal velocity to turnover number is 4.2% of that of the wild-type enzyme |
650979 |
| 5.3.3.2 | R7A |
mutation of highly conserved residue |
704638 |
| 5.3.3.2 | R83K |
the ratio of maximal velocity to turnover number is 104% of that of the wild-type enzyme |
650979 |
| 5.3.3.2 | S96A |
mutation of highly conserved residue |
704638 |
| 5.3.3.2 | T68A |
mutation of highly conserved residue |
704638 |
| 5.3.3.2 | W161F |
the ratio of maximal velocity to turnover number is 0.8% of that of the wild-type enzyme |
650979 |
| 5.3.3.2 | W216F |
10% activity compared to the wild type enzyme |
727623 |
| 5.3.3.2 | W256C |
the mutation enhances the enzyme activity 0.47fold |
748596 |
| 5.3.3.2 | Y104A |
0.1% of wild-type activity. Crystallization data. The M2+ metal-binding site is absent in the structure, but Mg2+ is still present and bound to C67, E87, and four water molecules |
680660 |
| 5.3.3.2 | Y104F |
0.1% of wild-type activity. Crystallization data. General fold of enzyme is similar to wild-type |
680660 |
