EC Number   |
Metals/Ions |
Reference |
|---|
    1.14.17.1 | Cu2+ |
enzyme not activated by exogenous copper but activity decreases at high concentrations |
438633 |
| 1.14.17.1 | Cu2+ |
enzyme-bound, required for activity |
744950 |
| 1.14.17.1 | Cu2+ |
Km: 0.00003-0.0002 mM |
438624 |
| 1.14.17.1 | Cu2+ |
required |
745892 |
| 1.14.17.1 | Cu2+ |
The enzyme contains two copper centers, one performs the substrate hydroxylation, while the second is used for electron storage/transfer |
674660 |
| 1.14.17.1 | Cu2+ |
tyramine can bind to either the Cu(I) or Cu(II) forms of TbetaM |
704443 |
| 1.14.17.1 | Fe2+ |
0.0004 mM per mol of enzyme |
438608 |
| 1.14.17.1 | Mg2+ |
regulates the translation of enzyme and affects the ratio of the two glycosylated forms of the enzyme |
438637 |
| 1.14.17.1 | more |
Cu2+, Mn2+, Ni2+, Co2+, Zn2+, Pb2+, Fe2+, Fe3+ reduce translation of enzyme at concentrations above 1.5 mM, Ni2+ and Cu2+ inhibit the glycosylation |
438637 |
| 1.14.17.1 | more |
the structure of the common DOMON (dopamine beta-monooxygenase N-terminal) domain reveals a possible metal-binding site and a ligand-binding pocket, coordinating residues are Asp99, Leu100, Ala115, and Asp130 |
746431 |
