EC Number   |
Metals/Ions |
Reference |
|---|
   3.5.1.104 | more |
the enzyme requires divalent cations |
730006 |
| 3.5.1.104 | Ni2+ |
activates |
730006 |
| 3.5.1.104 | Zn2+ |
0.05 mM, 5.5fold increase in activity |
689736 |
| 3.5.1.104 | Zn2+ |
a zinc metalloenzyme |
752966 |
| 3.5.1.104 | Zn2+ |
a zinc metalloenzyme, active site metal |
752784 |
| 3.5.1.104 | Zn2+ |
a zinc metalloenzyme, active site-bound |
754478 |
| 3.5.1.104 | Zn2+ |
divalent metal binding site, one site per enzyme monomer, essential for the enzyme's catalytic activity, structure analysis, detailed overview |
730914 |
| 3.5.1.104 | Zn2+ |
lower dependence on zinc or nickel ions for deacetylation of peptidoglycan by the enzyme than other metal ions, Mn2+, Mg2+, and Ca2+ |
730006 |
| 3.5.1.104 | Zn2+ |
the zinc ion of the metalloenzyme is coordinated by a conserved binding triad of amino acids consisting of one aspartate and two histidine residues, determination of the metal-binding site, which is essential for the enzyme's catalytic activity, one metal site per monomer, structure and quantum chemical calculations of models, overview. The metal ion occupies a tetrahedral environment with binding to one of the carboxylic oxygen of Asp14, His86, His90 and a water molecule |
730914 |
