EC Number   |
Protein Variants |
Reference |
|---|
   3.6.1.62 | A22V |
the differences in the kinetic parameters caused by the A22V mutation are small (less than a factor 2) |
758123 |
| 3.6.1.62 | E132A |
7.8% of wild-type activity. The E132A mutant shows a 5fold reduced affinity for Mg2+, but retains a Mn2+ affinity similar to that of the wild type |
714082 |
| 3.6.1.62 | E141A |
10% of wild-type activity. The E141A mutant demonstrates only slight variations in both Mg2+ and Mn2+ binding |
714082 |
| 3.6.1.62 | E141Q |
inactive mutant enzyme |
716742 |
| 3.6.1.62 | E144Q/E145Q |
inactive mutant enzyme |
716742 |
| 3.6.1.62 | E145A |
12.2% of wild-type activity. the E145A mutant shows 2-fold reduced affinity for Mg2+ and 6-fold reduced Mn2+ binding |
714082 |
| 3.6.1.62 | E148Q |
mutant enzyme is as stable as the wild-type enzyme |
716207 |
| 3.6.1.62 | E150Q |
mutant protein is inactive under all conditions |
715488 |
| 3.6.1.62 | E153Q |
mutant has 3 molecules in the asymmetric unit. There is clear electron density for an octahedrally coordinated Mg2+ in the structure, similar to wild-type. Mutant is severely catalytically compromised and displays a linear dependence on pH over the range studied (pH 79.5) |
735287 |
| 3.6.1.62 | E198Q |
mutant lacks clear density for a metal ion in the active site and fails to crystallize in the presence of any divalent cation |
735287 |
