6.5.1.2	Ca2+	10fold lower activation than Mn2+, maximal activity at 2 mM	672811	
6.5.1.2	Ca2+	40% of activity obtained with Mg2+	651212	
6.5.1.2	Ca2+	60% as active as Mg2+ in activation as reported in one study, no activity in another	1909, 1910	
6.5.1.2	Ca2+	activates wild-type enzyme and mutant enzyme DELTA582-667	661789	
6.5.1.2	Ca2+	in presence of Ca2+ MtuLigA is able to carry out the first two steps of ligation reaction that is the transfer of AMP to enzyme from NAD+ and further transfer of it to substrate to form DNA-adenylate intermediate. Ca2+ can not support nick closure activity	677062	
6.5.1.2	Ca2+	supports formation of DNA-adenylate intermediate	653379	
6.5.1.2	Ca2+	the enzyme requires a divalent cation like Ca2+, optimal activity at about 20 mM Ca2+	714854	
6.5.1.2	Co2+	25% of the activity with Mg2+	653388	
6.5.1.2	Co2+	can partially substitute for Mg2+	652175	
6.5.1.2	Co2+	no activity observed in the presence of	728580	
6.5.1.2	Cu2+	30% of activity obtained with Mg2+	651212	
6.5.1.2	K+	-	1910	
6.5.1.2	K+	25 mM, stimulates activity	651073	
6.5.1.2	K+	activates at 1-150 mM	1971	
6.5.1.2	K+	highest activity below 10 mM	651212	
6.5.1.2	K+	stimulates	1910	
6.5.1.2	K+	stimulates at low concentrations	1909	
6.5.1.2	KCl	enzymatic activity increased in the presence of monovalent cations, maximal activity at 25 mM NaCl	728580	
6.5.1.2	KCl	no activity is detected in the absence of KCl. Maximum activity at 3.2 M KCl, close to the intracellular KCl concentration of Haloferax volcanii cells	672808	
6.5.1.2	KCl	stimulation by 300 mM KCl, in 10% w/v polyethylene glycol 6000 solution or 150-300 mM KCl in 15% polyethylene glycol 6000 solution. Stimulation of intermolecular blunt end ligation by 150-250 mM KCl in 15% polyethylene glycol 600 solution	1970	
6.5.1.2	Mg2+	1-10 mM, required	653388	
6.5.1.2	Mg2+	10fold lower activation than Mn2+, maximal activity at 1 mM	672811	
6.5.1.2	Mg2+	5 mM	653379	
6.5.1.2	Mg2+	best metal-activator of wild-type enzyme and mutant enzyme DELTA582-667	661789	
6.5.1.2	Mg2+	divalent cation required, optimal concentration: 10 mM	677062	
6.5.1.2	Mg2+	highest activity at 5 mM	652175	
6.5.1.2	Mg2+	Mg2+ activates at 4.0 mM	690424	
6.5.1.2	Mg2+	optimal concentration: 1-3 mM	1909, 1910	
6.5.1.2	Mg2+	optimal concentration: 5-9 mM	1971	
6.5.1.2	Mg2+	optimum concentration at 5 mM	694991	
6.5.1.2	Mg2+	or Mn2+ required, maximal activity at 10-15 mM	661248	
6.5.1.2	Mg2+	required	650967, 651073, 651212	
6.5.1.2	Mg2+	required for activity, maximal activity occurs with 10-20 mM MgCl2 in the presence of 30 mM each of KCl and (NH4)2SO4	715672	
6.5.1.2	Mg2+	requires divalent cations, Mn2+ or Mg2+	1909, 1910, 1971	
6.5.1.2	Mg2+	the enzyme requires a divalent cation like Mg2+, optimal activity at about 20 mM Mg2+	714854	
6.5.1.2	MgCl2	highest activity: 10 mM MgCl2	728580	
6.5.1.2	Mn2+	1-10 mM, required	653388	
6.5.1.2	Mn2+	5 mM, most effective metal cofactor	653379	
6.5.1.2	Mn2+	50% of activity obtained with Mg2+	651212	
6.5.1.2	Mn2+	activates wild-type enzyme and mutant enzyme DELTA582-667	661789	
6.5.1.2	Mn2+	activation at 0.2-1.0 mM, inhibition at higher concentration	1910	
6.5.1.2	Mn2+	can partially substitute for Mg2+	652175	
6.5.1.2	Mn2+	optimal concentration: 3-6 mM	1971	
6.5.1.2	Mn2+	or Mg2+ required, maximal activity at 1 mM	661248	
6.5.1.2	Mn2+	preference for Mn2+ as cofactor, maximal activity at 1 mM	672811	
6.5.1.2	Mn2+	requires divalent cations, Mn2+ or Mg2+	1909, 1910, 1971	
6.5.1.2	Mn2+	the enzyme requires a divalent cation like Mn2+, maximal activity at 3 mM Mn2+	714854	
6.5.1.2	additional information	Ca2+, Zn2+ and Cu2+ have no effect on activity	652175	
6.5.1.2	additional information	no zinc binding motif as known from most bacterial DNA-ligases	652175	
6.5.1.2	additional information	no zinc-binding motif as known for bacterial DNA-ligase	650937	
6.5.1.2	Na+	inhibitory	651212	
6.5.1.2	NaCl	enzymatic activity increased in the presence of monovalent cations, maximal activity at 5 mM NaCl	728580	
6.5.1.2	NaCl	stimulation of intermolecular cohesive-end ligation by 200 mM NaCl, in 10% w/v polyethylene glycol 6000 solution, or 100-200 mM NaCl in 15% polyethylene glycol 6000 solution. Stimulation of intermolecular blunt end ligation by 100-150 mM NaCl in 15% polyethylene glycol 600 solution	1970	
6.5.1.2	NH4+	-	1910	
6.5.1.2	NH4+	10 mM, stimulates activity	651073	
6.5.1.2	NH4+	activates at 1-150 mM	1971	
6.5.1.2	NH4+	highest activity below 10 mM	651212	
6.5.1.2	NH4+	stimulates	1910	
6.5.1.2	NH4+	stimulates at low concentrations	1909	
6.5.1.2	NH4+	stimulates enzyme activity at 10 mM	748783	
6.5.1.2	NH4Cl	enzymatic activity increased in the presence of monovalent cations, maximal activity at 10 mM NaCl	728580	
6.5.1.2	Ni2+	10% of activity obtained with Mg2+	651212	
6.5.1.2	Ni2+	no activity observed in the presence of	728580	
6.5.1.2	Ni2+	supports formation of DNA-adenylate intermediate	653379	
6.5.1.2	Rb+	stimulates	1910	
6.5.1.2	Zn2+	0.24 mol per mol protein	651073	
6.5.1.2	Zn2+	1 mol per mol of enzyme, Cys406, Cys409, Cys422 and Cys427 form a zinc binding motif	650967	
6.5.1.2	Zn2+	5% of activity obtained with Mg2+	651212	
6.5.1.2	Zn2+	bound to the C-terminal fragment	652786	
6.5.1.2	Zn2+	no effect	653388	
6.5.1.2	Zn2+	slight activation	1909, 1910	
6.5.1.2	Zn2+	zinc binding motif, Cys437, Cys440, Cys455, Cys460	649444	
6.5.1.2	Zn2+	zinc binding motiv, C408, C411, C432 and C426	653376