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	K+	stimulates at low concentrations	1909	
6.5.1.2	Mg2+	optimal concentration: 1-3 mM	1909, 1910	
6.5.1.2	NH4+	stimulates at low concentrations	1909	
6.5.1.2	Zn2+	slight activation	1909, 1910	
6.5.1.2	K+	-	1910	
6.5.1.2	K+	stimulates	1910	
6.5.1.2	Mg2+	requires divalent cations, Mn2+ or Mg2+	1909, 1910, 1971	
6.5.1.2	Mn2+	activation at 0.2-1.0 mM, inhibition at higher concentration	1910	
6.5.1.2	Mn2+	requires divalent cations, Mn2+ or Mg2+	1909, 1910, 1971	
6.5.1.2	NH4+	-	1910	
6.5.1.2	NH4+	stimulates	1910	
6.5.1.2	Rb+	stimulates	1910	
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	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	K+	activates at 1-150 mM	1971	
6.5.1.2	Mg2+	optimal concentration: 5-9 mM	1971	
6.5.1.2	Mn2+	optimal concentration: 3-6 mM	1971	
6.5.1.2	NH4+	activates at 1-150 mM	1971	
6.5.1.2	Zn2+	zinc binding motif, Cys437, Cys440, Cys455, Cys460	649444	
6.5.1.2	additional information	no zinc-binding motif as known for bacterial DNA-ligase	650937	
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	K+	25 mM, stimulates activity	651073	
6.5.1.2	NH4+	10 mM, stimulates activity	651073	
6.5.1.2	Zn2+	0.24 mol per mol protein	651073	
6.5.1.2	Ca2+	40% of activity obtained with Mg2+	651212	
6.5.1.2	Cu2+	30% of activity obtained with Mg2+	651212	
6.5.1.2	K+	highest activity below 10 mM	651212	
6.5.1.2	Mg2+	required	650967, 651073, 651212	
6.5.1.2	Mn2+	50% of activity obtained with Mg2+	651212	
6.5.1.2	Na+	inhibitory	651212	
6.5.1.2	NH4+	highest activity below 10 mM	651212	
6.5.1.2	Ni2+	10% of activity obtained with Mg2+	651212	
6.5.1.2	Zn2+	5% of activity obtained with Mg2+	651212	
6.5.1.2	Co2+	can partially substitute for Mg2+	652175	
6.5.1.2	Mg2+	highest activity at 5 mM	652175	
6.5.1.2	Mn2+	can partially substitute for Mg2+	652175	
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	Zn2+	bound to the C-terminal fragment	652786	
6.5.1.2	Zn2+	zinc binding motiv, C408, C411, C432 and C426	653376	
6.5.1.2	Ca2+	supports formation of DNA-adenylate intermediate	653379	
6.5.1.2	Mg2+	5 mM	653379	
6.5.1.2	Mn2+	5 mM, most effective metal cofactor	653379	
6.5.1.2	Ni2+	supports formation of DNA-adenylate intermediate	653379	
6.5.1.2	Co2+	25% of the activity with Mg2+	653388	
6.5.1.2	Mg2+	1-10 mM, required	653388	
6.5.1.2	Mn2+	1-10 mM, required	653388	
6.5.1.2	Zn2+	no effect	653388	
6.5.1.2	Mg2+	or Mn2+ required, maximal activity at 10-15 mM	661248	
6.5.1.2	Mn2+	or Mg2+ required, maximal activity at 1 mM	661248	
6.5.1.2	Ca2+	activates wild-type enzyme and mutant enzyme DELTA582-667	661789	
6.5.1.2	Mg2+	best metal-activator of wild-type enzyme and mutant enzyme DELTA582-667	661789	
6.5.1.2	Mn2+	activates wild-type enzyme and mutant enzyme DELTA582-667	661789	
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	Ca2+	10fold lower activation than Mn2+, maximal activity at 2 mM	672811	
6.5.1.2	Mg2+	10fold lower activation than Mn2+, maximal activity at 1 mM	672811	
6.5.1.2	Mn2+	preference for Mn2+ as cofactor, maximal activity at 1 mM	672811	
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	Mg2+	divalent cation required, optimal concentration: 10 mM	677062	
6.5.1.2	Mg2+	Mg2+ activates at 4.0 mM	690424	
6.5.1.2	Mg2+	optimum concentration at 5 mM	694991	
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	Mg2+	the enzyme requires a divalent cation like Mg2+, optimal activity at about 20 mM Mg2+	714854	
6.5.1.2	Mn2+	the enzyme requires a divalent cation like Mn2+, maximal activity at 3 mM Mn2+	714854	
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	Co2+	no activity observed in the presence of	728580	
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	MgCl2	highest activity: 10 mM MgCl2	728580	
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	NH4Cl	enzymatic activity increased in the presence of monovalent cations, maximal activity at 10 mM NaCl	728580	
6.5.1.2	Ni2+	no activity observed in the presence of	728580	
6.5.1.2	NH4+	stimulates enzyme activity at 10 mM	748783