EC Number   |
Metals/Ions |
Reference |
|---|
    1.14.99.39 | copper |
contains a labile copper centre |
697922 |
| 1.14.99.39 | Cu2+ |
an N-terminal copper binding site |
746404 |
| 1.14.99.39 | Cu2+ |
CuCl2 stimulates AMO activity in vitro |
744760 |
| 1.14.99.39 | Cu2+ |
required |
744103 |
| 1.14.99.39 | Cu2+ |
the addition of CuCl2 to cell extracts results in 5- to 15-fold stimulation of ammonia-dependent O2 consumption, ammonia-dependent nitrite production, and hydrazine-dependent ethane oxidation. Two populations of AMO in cell extracts. The low, copper-independent (residual) AMO activity is completely inactivated by acetylene in the absence of exogenously added copper. The copper-dependent (activable) AMO activity is protected against acetylene inactivation in the absence of copper. However, in the presence of copper both populations of AMO are inactivated by acetylene |
698543 |
| 1.14.99.39 | Cu2+ |
the enzyme contains Cu (9.4 mol per mol enzyme), Fe (3.9 mol per mol enzyme), and Zn (0.5 to 2.6 mol per mol enzyme) |
696547 |
| 1.14.99.39 | CuCl2 |
stimulates enzyme activity in vitro |
727350 |
| 1.14.99.39 | Iron |
iron capable of forming the S = 3/2 complex is a catalytic component of ammonia monooxygenase of Nitrosomonas europaea, possibly a part of the oxygen-activating center |
697923 |
| 1.14.99.39 | Iron |
the enzyme contains Cu (9.4 mol per mol enzyme), Fe (3.9 mol per mol enzyme), and Zn (0.5 to 2.6 mol per mol enzyme) |
696547 |
| 1.14.99.39 | MgCl2 |
stimulates in vitro. Loss of enzyme activity upon lysis of Nitrosomonas europaea results from the loss of copper from the enzyme, generating a catalytically inactive, yet stable and activable, form of the enzyme |
698543 |
