EC Number   |
Metals/Ions |
Reference |
|---|
   3.2.1.17 | Cu2+ |
1.0 mM, activity is increased by 54% |
682650 |
| 3.2.1.17 | Cu2+ |
activates |
171095 |
| 3.2.1.17 | Mg2+ |
highest activity at 50 mM Mg2+ |
751265 |
| 3.2.1.17 | Mg2+ |
increases activity in phage T4 e lysozyme |
171053 |
| 3.2.1.17 | Mg2+ |
no effect: ghost lysozyme |
171052 |
| 3.2.1.17 | Mg2+ |
required, strong temperature dependences of apparent affinities to Mg2+ due to low thermal stability of the apoform and relatively high unfavorable enthalpies of Mg2+ association, the primary Mg2+ site of the enzyme is different from its Ca2+-binding site. The Ca2+/Mg2+ selectivity of Mg2+-site of EQL is below an order of magnitude. The enzyme exhibits a distinct Mg2+-specific site, probably arising as an adaptation to the extracellular environment, overview |
718376 |
| 3.2.1.17 | MgCl2 |
activates at 2-5 mM |
729775 |
| 3.2.1.17 | MgCl2 |
activates, maximal activity at 0.035 M |
664651 |
| 3.2.1.17 | Mn |
the reaction of the covalent (Mn(CO)3(H2O)2)+lysozyme adduct with NiS4 and NiN2S2 complexes generates binuclear NiMn complexes |
679189 |
| 3.2.1.17 | more |
no increase in activity at high ionic strength |
729437 |
