EC Number   |
Metals/Ions |
Reference |
|---|
   2.7.13.3 | Ag+ |
CusS forms a homodimer with four Ag(I) binding sites per dimeric complex, binding site structure, overview |
740082 |
| 2.7.13.3 | Ag+ |
specifically activated by silver |
704305 |
| 2.7.13.3 | Ag+ |
the periplasmic sensor domain of CusS directly interacts with Ag(I) ions and undergoes a conformational change upon metal binding. Metal binding also enhances the tendency of the domain to dimerize. No molecules of Ag+ per enzyme molecule for the purified enzyme, and 3.82 molecules of Ag+ per enzyme molecule after dialysis against Ag+, Ni2+, Zn2+, and Cu+ ions |
740103 |
| 2.7.13.3 | Cl- |
activates, the signal input domain of Hik2 responds to environmental Cl- concentration, key for induction of activity |
740465 |
| 2.7.13.3 | Cu+ |
0.14 molecules of Cu+ per enzyme molecule for the purified enzyme, and 0.23 molecules of Cu+ per enzyme molecule after dialysis against Ag+, Ni2+, Zn2+, and Cu+ ions |
740103 |
| 2.7.13.3 | Cu2+ |
essential cofactor |
705817 |
| 2.7.13.3 | Cu2+ |
specifically activated by 0.01 mM copper |
704305 |
| 2.7.13.3 | Fe |
enzyme contains 2-labile 1-2 iron-sulphur [4Fe-4S]2+ clusters of the FNR-type |
662894 |
| 2.7.13.3 | Fe2+ |
the Fe(II) heme-bound inactive form has kcat and Km(ATP) values of 0.0067/s and 0.078 mM, respectively, suggesting that its low activity reflects a low affinity for ATP relative to that of the Fe(III) form. The heme-free form exhibits low activity, with kcat and Km(ATP) values of 0.005/s and 0.0336 mM, respectively, suggesting that the heme iron complex is essential for high catalytic activity |
740070 |
| 2.7.13.3 | Fe2+ |
the presence of iron ions alone or in combination with H2O2 or dithiothreitol leads to significantly increased phosphorylation levels of SenS. 0.005 mM Fe2+ is able to enhance the phosphorylation level of SenS by a factor of 10 relative to the basal level, a combination of FeCl2 and H2O2 increases autophosphorylation activity by a factor of 20 |
690397 |
