EC Number   |
Metals/Ions |
Reference |
|---|
   3.1.3.75 | Co2+ |
divalent metal ions required, highest activity with 1.5 mM Mg2+ |
714360 |
| 3.1.3.75 | Co2+ |
stimulates to a lesser extend than Mg2+, higher activity with phosphocholine than with phosphoethanolamine in the presence of Co2+ and Mn2+ most probably due to an allosteric effect caused by a difference in the metal-binding properties of each enzyme-substrate complex |
654549 |
| 3.1.3.75 | Cu2+ |
activates |
714874 |
| 3.1.3.75 | Cu2+ |
activates, Zn2+ and Cu2+ are better activators than Mg2+ at pH 5.0 |
714872 |
| 3.1.3.75 | Cu2+ |
activator, the wild type recombinant phosphorylcholine phosphatase has higher affinity for Zn2+ and Cu2+ than for Mg2+, Cu2+ is able to diminish almost 3times the affinity of the enzyme for p-nitrophenyl with respect to the addition of Zn2+ or Mg2+ |
696420 |
| 3.1.3.75 | Cu2+ |
dependent on divalent cations Mg2+, Zn2+ or Cu2+ |
713654 |
| 3.1.3.75 | Fe2+ |
divalent metal ions required, highest activity with 1.5 mM Mg2+ |
714360 |
| 3.1.3.75 | Mg2+ |
- |
664211, 664697, 679380, 680993, 706604 |
| 3.1.3.75 | Mg2+ |
activates, Zn2+ and Cu2+ are better activators than Mg2+ at pH 5.0 |
714872 |
| 3.1.3.75 | Mg2+ |
activator, the wild type recombinant phosphorylcholine phosphatase has higher affinity for Zn2+ and Cu2+ than for Mg2+ |
696420 |
