EC Number   |
Metals/Ions |
Reference |
|---|
   7.2.2.12 | Ag+ |
activates ATPase activity |
246928 |
| 7.2.2.12 | Cd2+ |
activates at 0.00003 mM, the level of activation does not change much until a concentration of 0.001 mM |
718974 |
| 7.2.2.12 | Cd2+ |
activation energy of binding is similar for both Pb2+ and Cd2+ |
667635 |
| 7.2.2.12 | Cd2+ |
isoform HMA4 reaches maximal ATPase activity when all internal high-affinity Cd2+ binding sites are occupied |
750670 |
| 7.2.2.12 | Cd2+ |
ligands and perhaps binding geometry of Pb(II) at the N-terminal metal site in ZntA are different from that of Zn(II) and Cd(II) |
667659 |
| 7.2.2.12 | Cd2+ |
the putative Zn2+/Cd2+-ATPase is truncated at the N-terminus and is activated in vitro by copper but not by zinc or cadmium. When expressed in Escherichia coli, however, the putative enzyme can be isolated as a full-length protein and the ATPase activity is increased by the addition of Zn2+ and Cd2+ as well as by Cu2+ |
719741 |
| 7.2.2.12 | Cs2+ |
ZntA confers resistance specifically to Pb2+, Zn2+, and Cd2+ in Escherichia coli. Wild-type ZntA binds two metal ions with high affinity, one in the N-terminal domain and another in the transmembrane domain |
667735 |
| 7.2.2.12 | Cu2+ |
activates at 0.00003 mM |
718974 |
| 7.2.2.12 | Cu2+ |
enhances phosphorylation, it cannot activate the ATPase |
246928 |
| 7.2.2.12 | Cu2+ |
the putative Zn2+/Cd2+-ATPase is truncated at the N-terminus and is activated in vitro by copper but not by zinc or cadmium. When expressed in Escherichia coli, however, the putative enzyme can be isolated as a full-length protein and the ATPase activity is increased by the addition of Zn2+ and Cd2+ as well as by Cu2+ |
719741 |
