EC Number   |
Metals/Ions |
Reference |
|---|
   3.4.19.12 | Cu2+ |
0.2 mol per mol of protein, native isozyme ISOT-S |
646107 |
| 3.4.19.12 | divalent cations |
most divalent cations, except Mg2+ and Ca2+ are inhibitory |
646096 |
| 3.4.19.12 | Ni2+ |
0.5 mol per mol of protein, native isozyme ISOT-S |
646107 |
| 3.4.19.12 | Zn2+ |
0.9 mol per mol of protein, native isozyme ISOT-S |
646107 |
| 3.4.19.12 | Zn2+ |
absolutely required, apoenzyme is inactive |
646107 |
| 3.4.19.12 | Zn2+ |
AMSH contains the JAMM motif, i.e. JAB1/MPN/Mov34 metalloenzyme motif, in the active site |
665794 |
| 3.4.19.12 | Zn2+ |
both isozymes contain each two Zn2+-binding sites: one essential for proteolytic activity with high affinity as part of a cryptic nitrilo-triacetate-resistant pocket, a second which is enclosed with an excess of Zn2+ |
646107 |
| 3.4.19.12 | Zn2+ |
isozyme ISOT-S: Ni2+ can substitute by 90% for Zn2+, Cu2+ by 10% |
646107 |
| 3.4.19.12 | Zn2+ |
removal and reconstitution methods, overview |
646107 |
| 3.4.19.12 | Zn2+ |
the Zn2+ bound to binding site 1 can be removed slowly by dialysis against 1,10-phenanthroline at pH 5.5, or rapidly by treatment at pH 3.0 in presence of 6 M urea followed by gel filtration at neutral pH |
646107 |
