6.5.1.3	Mg2+	required	1910, 1983, 1995	
6.5.1.3	Mg2+	divalent cation required	1985	
6.5.1.3	Mg2+	-	1987, 1997	
6.5.1.3	Mg2+	Km: 0.4 mM, inhibition above 10 mM	1995	
6.5.1.3	Mg2+	requires metal ions for structure and catalysis	650172	
6.5.1.3	Mn2+	only marginal activity	650172	
6.5.1.3	additional information	no detectable activity with Ca2+, Sr2+, Ba2+, Zn2+, Co2+, Cd2+, Pb2+, Co(NH3)6 3+, or spermine	650172	
6.5.1.3	Mg2+	nucleotidyl transfer Mg2+ dependent	652246	
6.5.1.3	Mg2+	optimum activity at 5 mM	653392	
6.5.1.3	Mn2+	optimum activity at 1 mM	653392	
6.5.1.3	Mg2+	Mg2+ or Mn2+ required	662241	
6.5.1.3	Mn2+	Mg2+ or Mn2+ required	662241	
6.5.1.3	Mg2+	magnesium ion interacts with the beta and gamma-phosphate groups and is almost perfectly octahedrally coordinated by six phosphate and water oxygen atoms	662636	
6.5.1.3	Mg2+	activates, optimum: 5-10 mM	662976	
6.5.1.3	Mn2+	activates, showing slightly higher activity than Mg2+	662976	
6.5.1.3	Mg2+	the active site contains two metal ions, consistent with the two-magnesium ion catalytic mechanism	674568	
6.5.1.3	Mg2+	L1 ligase is an obligate metalloenzyme that is highly specific for Mg2+. It is selected in the presence of 60 mM MgCl2 and functions optimally in Mg2+ concentrations as high as 100 mM	677128	
6.5.1.3	Mg2+	dependent on	747437	
6.5.1.3	Mn2+	the enzyme prefers manganese as the metal cofactor for nick sealing	749172	
6.5.1.3	Mg2+	enzyme activity is optimal at 5 mM Mg2+	749277	
6.5.1.3	Mn2+	enzyme activity is optimal at 2.5 mM Mn2+	749277	
6.5.1.3	additional information	calcium, cobalt, copper, cadmium, nickel, and zinc are ineffective	749277