EC Number |
Protein Variants |
Reference |
---|
5.3.3.2 | Y104F |
0.1% of wild-type activity. Crystallization data. General fold of enzyme is similar to wild-type |
680660 |
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 | W216F |
10% activity compared to the wild type enzyme |
727623 |
5.3.3.2 | Q160E |
10-fold decrease in kcat/Km |
728667 |
5.3.3.2 | Y105F |
115% activity compared to the wild type enzyme |
727623 |
5.3.3.2 | Q160K |
130-fold decrease in kcat/Km |
728667 |
5.3.3.2 | Q160N |
150-fold decrease in kcat, kcat/Km decreases 66-fold |
728667 |
5.3.3.2 | Q160H |
23-fold decrease in kcat/Km |
728667 |
5.3.3.2 | Q160L |
28-fold decrease in kcat/Km |
728667 |
5.3.3.2 | Q154N |
active site mutant |
715286 |