EC Number   |
Metals/Ions |
Reference |
|---|
    1.4.3.21 | Ca2+ |
calcium is the normal ligand of these peripheral sites. Enzyme activity is stimulated by 3 mM. Removal of the not solvent exposed calcium ion with EDTA results in a 60-90% reduction in enzyme activity |
724280 |
| 1.4.3.21 | Co2+ |
besides Cu2+ ion, some divalent metal ions such as Co2+, Ni2+, and Zn2+ are also bound to the metal site of the apoenzyme so tightly that they are not replaced by excess Cu2+ ions added subsequently. Although these noncupric metal ions can not initiate topaquinone formation under the atmospheric conditions, slow spectral changes are observed in the enzyme bound with Co2+ or Ni2+ ion under the dioxygen-saturating conditions. X-ray crystallographic analysis reveals structural identity of the active sites of Co- and Ni-activated enzymes with Cu-enzyme. Co2+ and Ni2+ ions are also capable of forming topaquinone, though much less efficiently than Cu2+ |
671976 |
| 1.4.3.21 | Co2+ |
can replace Cu2+ in the enzyme |
391910 |
| 1.4.3.21 | Co2+ |
cobalt-substituted enzyme displays nominal catalytic activity |
725549 |
| 1.4.3.21 | Co2+ |
dependent on |
703130 |
| 1.4.3.21 | Co2+ |
enzyme reconstituted with Co2+ exhibits 2.2% of the activity of the original Cu2+ -enzyme, KM-values for amine substrate and dioxygen are comparable |
655782 |
| 1.4.3.21 | Cobalt |
the Km-value for O2 of the cobalt-substituted enzyme form is approximately 70fold higher than that of the copper-containing wild-type enzyme |
654616 |
| 1.4.3.21 | copper |
- |
675286, 687276 |
| 1.4.3.21 | copper |
2 mol copper/mol enzyme dimer |
391949 |
| 1.4.3.21 | copper |
2 mol of Cu2+ per dimer |
391914 |
