EC Number   |
Metals/Ions |
Reference  |
|---|
   3.4.24.27 | Zinc |
zinc metalloproteinase |
31137, 31141, 31142 |
| 3.4.24.27 | Ca2+ |
there are two adjacent calcium ions seemingly firmly bound inside the surface of the molecule by chelation to five acidic groups: Asp138, Glu177, Asp185, Glu190 and Asp191, two additional calcium binding sites are at exposed surface regions, one chelated by Asp57 and possibly also by Asp59 and the other chelated by Asp200 |
31146 |
| 3.4.24.27 | Zinc |
the three zinc ligands are two histidines and glutamic acid |
31146 |
| 3.4.24.27 | Ca2+ |
contains 4 structural calcium ions |
649825 |
| 3.4.24.27 | Zn2+ |
zinc-metallopeptidase |
649825 |
| 3.4.24.27 | Co2+ |
2fold activation at 0.4 mM |
650286 |
| 3.4.24.27 | Zn2+ |
Zn-dependent |
650286 |
| 3.4.24.27 | Zn2+ |
zinc-containing neutral metalloendoprotease |
650540 |
| 3.4.24.27 | NaCl |
activity is remarkably enhanced by 1-5 M neutral salts |
651745 |
| 3.4.24.27 | Co2+ |
active zinc ion in thermolysin can be substituted by Co2+, doubles activity |
651789 |
