EC Number   |
Metals/Ions |
Reference |
|---|
   3.4.24.21 | Ca2+ |
activates, a positive regulator of BMP-1 |
753172 |
| 3.4.24.21 | Co2+ |
activation of apoenzyme, can replace Zn2+ as catalytic ion yielding 140% of the activity of the zinc-containing enzyme, pentavalent metal coordination |
31060, 31062 |
| 3.4.24.21 | Cu2+ |
activation of apoenzyme, can replace Zn2+ as catalytic ion yielding 37% of the activity of the zinc-containing enzyme, pentavalent metal coordination |
31060, 31062 |
| 3.4.24.21 | K+ |
secretion of nephrosin can be stimulated by high concentrations of extracellular potassium |
651861 |
| 3.4.24.21 | more |
in mature, unbound astacins, a conserved tyrosine acts as an additional zinc ligand, which is swung out upon substrate or inhibitor binding in a tyrosine switch motion |
733445 |
| 3.4.24.21 | more |
inhibitor coordinates the catalytic zinc ion via carbonyl oxygen of glycine and O atom of hydroxamic acid |
753328 |
| 3.4.24.21 | more |
metal content |
31053 |
| 3.4.24.21 | more |
no apoenzyme activation by Ni2+ or Hg2+ with their octahedral and tetrahedral coordination |
31060, 31062 |
| 3.4.24.21 | more |
no other metal than Co2+, Zn2+ or Cu2+ detectable by atomic absorption spectroscopy |
31062 |
| 3.4.24.21 | Zn2+ |
a zinc metalloprotease |
734008 |
