EC Number   |
Metals/Ions |
Reference |
|---|
   7.2.2.8 | Ag+ |
full-length CopA has submicromolar affinity for Ag+, but is inhibited by concentrations above 0.001 mM. Deletion of both metal-binding domains has no effect on affinity but results in loss of this inhibition. Individual deletions implicate the N-terminal metal-binding domains in causing the inhibition at concentrations above 0.001 mM |
721480 |
| 7.2.2.8 | Ag+ |
isoform CtrA2 and CtrA3 are activated by Ag+ (with Ag+ being twice as effective as Cu+ in case of isoform CtrA2) |
688411 |
| 7.2.2.8 | Ag+ |
stimulating |
656102 |
| 7.2.2.8 | copper |
- |
751261 |
| 7.2.2.8 | copper |
CopB exhibits metal-stimulated ATPase activity in response to Cu+, but not Cu2+. Cu+ is coordinated by four sulfur ligands, likely derived from conserved cysteine and methionine residues. The enzyme does bind Cu2+, the binding site is not the prototypical P1B-ATPase transmembrane site and does not involve sulfur coordination |
752057 |
| 7.2.2.8 | copper |
enzyme binds Cu(I) witrh subfemtomolar affinity |
750917 |
| 7.2.2.8 | copper |
the four most N-terminal metal-binding domains in ATP7B, upon stoichiometric copper addition, adopt a more compact arrangement with higher thermal stability than in the absence of copper. No stable complex was found in solution between the metal-binding domains and the nucleotide-binding domain of ATP7B |
749805 |
| 7.2.2.8 | Cu+ |
100% activity at 0.02 mM Cu+ |
680804 |
| 7.2.2.8 | Cu+ |
Cu+ binding to the N-metal binding domain is required to produce an active conformation of the enzyme, whereby additional Cu+ bound to an alternate (transmembrane transport) site initiates faster cycles |
698784 |
| 7.2.2.8 | Cu+ |
full-length CopA has submicromolar affinity for Cu+, but is inhibited by concentrations above 0.001 mM. Deletion of both metal-binding domains has no effect on affinity but results in loss of this inhibition. Individual deletions implicate the N-terminal metal-binding domains in causing the inhibition at concentrations above 0.001 mM |
721480 |
