EC Number   |
Metals/Ions |
Reference  |
|---|
   1.10.3.3 | more |
no support of a metal in the enzyme |
396331 |
| 1.10.3.3 | copper |
a multicopper protein, 6 atoms of copper per enzyme molecule |
439889 |
| 1.10.3.3 | copper |
10 copper atoms per enzyme molecule |
439890 |
| 1.10.3.3 | copper |
8 atoms of copper per enzyme molecule of 132000 Da |
439894 |
| 1.10.3.3 | copper |
10-12 atoms of copper per enzyme molecule of 140000 Da |
439896 |
| 1.10.3.3 | copper |
4 copper atoms per subunit, mononuclear blue copper in domain 3 and trinuclear copper between domain 1 and 3 |
439899 |
| 1.10.3.3 | copper |
measurement of intramolecular electron transfer between type I and type III copper centers in the multi-copper enzyme |
439900 |
| 1.10.3.3 | copper |
each subunit has 4 copper atoms bound as mononuclear and trinuclear species, mononuclear copper representing the type I copper is located in the 3 domain |
439902 |
| 1.10.3.3 | copper |
native enzyme contains two type 1, two type 2 and four type 3 copper ions |
439904 |
| 1.10.3.3 | more |
selective removal of copper with chelating agents, e.g. EDTA or N,N-diethyldithiocarbamate produces an inactive enzyme, CN- treatment gives fully copper-depleted apoform, indication that copper affects the enzyme stability but not the enzyme conformation |
439912 |
