EC Number   |
Metals/Ions |
Reference |
|---|
   7.2.2.9 | Ag+ |
partially activated by Ag+, 55%, of the activation compared to Cu2+ |
719816 |
| 7.2.2.9 | Ag+ |
purified CtrA2 protein, stimulation twice as efficient as by Cu2+ |
688411 |
| 7.2.2.9 | Ag+ |
purified CtrA3 protein, stimulation twice as efficient as by Cu2+ |
688411 |
| 7.2.2.9 | Ag+ |
stimulates |
719771 |
| 7.2.2.9 | Ag+ |
the enzyme is activated by silver ions with an apparent affinity in the micromolar range (40% activation at 0.005 mM compared to Cu+) |
719971 |
| 7.2.2.9 | Co2+ |
activity slightly above background as measured in the absence of any such ion |
688411 |
| 7.2.2.9 | copper |
the enzyme contains two Cu(I)-binding sites. Copper binding within the His-Met-loop stabilizes Cu(I) and protects it from oxidation, which may further aid the transfer of copper from ATP7A to acceptor proteins |
719946 |
| 7.2.2.9 | Cu |
demonstration of facile copper transfer between domain 1 and domain 4 |
667829 |
| 7.2.2.9 | Cu |
in HepG2 cells, elevated copper levels stimulates trafficking of ATP7B to pericanalicular vesicles. Mechanism of biliary copper excretion involves ATP7B-mediated vesicular sequestration of copper rather than direct copper translocation across the canalicular membrane |
668712 |
| 7.2.2.9 | Cu+ |
Cu+ stimulates catalytic activity of ATP7B, inducing the hydrolysis of ATP via formation of an acyl-phosphate intermediate, a step necessary for subsequent transport of copper across membranes. Neither Cu2+ nor other divalent metals such as Zn2+ or Cd2+ stimulate the formation of phospho-intermediate |
698990 |
