EC Number   |
Metals/Ions  |
Reference |
|---|
    1.14.17.1 | copper |
contains copper |
728562 |
| 1.14.17.1 | Cu2+ |
- |
438609, 438631, 438632 |
| 1.14.17.1 | Cu2+ |
1.1 Cu2+/subunit, increasing stimulation of activity by addition of up to 1 Cu2+/subunit, further additions up to at least 4 Cu/subunit gave neither stimulation nor inhibition |
438628 |
| 1.14.17.1 | Cu2+ |
2,6-dimethylphenyl isocyanide as the isocyanide ligand demonstrated, first: the formation of a mono-DIMPI-four-coordinate complex at each copper, second: the formation of complexes containing more than one isocyanide per copper |
438635 |
| 1.14.17.1 | Cu2+ |
3 mol of copper per mol of tetramer, MW 290000 |
438623 |
| 1.14.17.1 | Cu2+ |
4 atoms of tightly bound copper per tetramer |
438602 |
| 1.14.17.1 | Cu2+ |
a copper protein |
438589, 438601, 438604, 438608, 438623, 438628 |
| 1.14.17.1 | Cu2+ |
about 8 Cu2+ per tetramer |
438601 |
| 1.14.17.1 | Cu2+ |
DBH is an ascorbate-dependent glycoprotein that requires two type 2 bound copper ions per subunit to be active. copper sites are labile and termed CuH and CuM, respectively. CuH is coordinated to three histidines and CuM to two histidines and a methionine. CuM is involved in dioxygen binding and is the site for substrate hydroxylation, and CuH is the site of electron transfer |
746431 |
| 1.14.17.1 | Cu2+ |
enzyme contains a constant amount of Cu2+, 2 mol per mol of protein, and a variable amount of Cu2+, copper content is a linear function of the purity of the enzyme |
438608 |
