EC Number   |
Metals/Ions |
Reference |
|---|
   3.5.1.B15 | Co2+ |
activates |
756516 |
| 3.5.1.B15 | Co2+ |
activates, and reactivates the metal-depleted PZase, and facilitates the deprotonation of coordinates water molecules to generate a nucleophile that catalyzes the enzymatic reaction |
757445 |
| 3.5.1.B15 | Fe2+ |
activates |
710862 |
| 3.5.1.B15 | Fe2+ |
activates, cannot reactivate the metal-depleted PZase, but facilitates the deprotonation of coordinated water molecules to generate a nucleophile that catalyzes the enzymatic reaction |
757445 |
| 3.5.1.B15 | Fe2+ |
enzyme bound |
756516 |
| 3.5.1.B15 | Fe2+ |
iron shows weak binding with the metal coordination site of the mutant proteins due to alteration in electron transfer mechanism |
757448 |
| 3.5.1.B15 | Fe2+ |
required, enzyme-bound |
757008 |
| 3.5.1.B15 | Fe2+ |
required, enzyme-bound, the metal binding site contains iron (Fe2+ ion) in coordination with one aspartate (Asp49) and three histidines residues (His51, His57, and His71) |
757293 |
| 3.5.1.B15 | Fe2+ |
required, enzyme-bound. Mutations N11K and P69T cause destabilization of the Fe2+ binding site, structure overview |
757305 |
| 3.5.1.B15 | Fe2+ |
residues D49, H51, H57, H71 comprise a metal coordinating site coordinating an Fe2+ or Zn2+ cation |
757291 |
