EC Number   |
Metals/Ions |
Reference |
|---|
   3.1.1.74 | Ba2+ |
activates isozyme Tfu 0883 7% at 1 mM |
715944 |
| 3.1.1.74 | Ca2+ |
300 mM, about 4fold increase in specific activity. Presence of Ca2+ does not affect the secondary structure of Est1 |
751138 |
| 3.1.1.74 | Ca2+ |
activates at 1 mM |
730129 |
| 3.1.1.74 | Ca2+ |
slight activation at 1 mM |
730094 |
| 3.1.1.74 | Ca2+ |
the binding of Ca2+ induces large conformational changes in three loops, accompanied by the formation of additional interactions. The binding of Ca2+ stabilizes a region that is flexible in the Ca2+-free state but also modifies the substrate-binding groove by stabilizing an open conformation that allows the substrate to bind easily |
749726 |
| 3.1.1.74 | Ca2+ |
three calcium ions bind to S226P/R228S/S176A. Ca2+ binding induces the pocket to open, enabling the substrate to access the pocket more easily. Molecular dynamics simulations suggest that a postreaction state in the engaged form presumably exists between the experimentally observed forms, indicating that the substrate would be cleaved in the engaged form and then requires the enzyme to change to the open form to release the product, a process that Ca2+ can greatly accelerate |
749932 |
| 3.1.1.74 | Co2+ |
activates 7% at 1 mM |
715944 |
| 3.1.1.74 | Co2+ |
activates at 1 mM |
730129 |
| 3.1.1.74 | Co2+ |
activates isozyme Tfu 0882 4% and isozyme Tfu 0883 24% at 1 mM |
715944 |
| 3.1.1.74 | K+ |
activates at 1 mM |
730129 |
