3.2.1.17	Ag+	activates	171081	
3.2.1.17	Ca2+	34% activation at 5 mM, 150% activation at 10 mM, 280% at 5 mM of recombinant enzyme. 58% Inhibition at 10 mM, 97% at 50 mM of native enzyme, 66% inhibition at 20 mM, 97% at 50 mM of recombinant enzyme	729618	
3.2.1.17	Ca2+	activates	171081	
3.2.1.17	Ca2+	binding sites	171098, 171100, 171109, 171110	
3.2.1.17	Ca2+	highest activity at 50 mM Ca2+	751265	
3.2.1.17	Ca2+	required, strong temperature dependences of apparent affinities to Ca2+ due to low thermal stability of the apoform, the primary Mg2+ site of the enzyme is different from its Ca2+-binding site, Ca2+-binding sites are generally able to bind Mg2+., overview	718376	
3.2.1.17	CaCl2	activates at 2-5 mM	729775	
3.2.1.17	CaCl2	activates, maximal activity at 0.035 M	664651	
3.2.1.17	Co2+	increases the formation of lysozyme dimers	680207	
3.2.1.17	Cu2+	0.01 mM, activity is enhanced to 128% of control	679957	
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 Ni–Mn complexes	679189	
3.2.1.17	additional information	no increase in activity at high ionic strength	729437	
3.2.1.17	Na+	activates the native enzyme 3.43fold at 50 mM, the recombinant enzyme 4.3fold at 100 mM, inhibition of native, not recombinant, enzyme at 200 mM	729618	
3.2.1.17	Na+	activates, best at 75 mM	718120	
3.2.1.17	NaCl	activates	171081	
3.2.1.17	NaCl	activates at 10-70 mM	729775	
3.2.1.17	NaCl	activity increases as the NaCl concentration is increased from 0 to 0.1 M and then decreases from its maximum activity at 0.1 M NaCl with further increase in NaCl concentrations	664651	
3.2.1.17	Ni	the reaction of the covalent (Mn(CO)3(H2O)2)+–lysozyme adduct with NiS4 and NiN2S2 complexes generates binuclear Ni–Mn complexes	679189	
3.2.1.17	Zn2+	0.01 mM, activity is enhanced to 135% of control	679957