6.5.1.3	Mg2+	-	1987, 1997	
6.5.1.3	Mg2+	activates, optimum: 5-10 mM	662976	
6.5.1.3	Mg2+	dependent on	747437	
6.5.1.3	Mg2+	divalent cation required	1985	
6.5.1.3	Mg2+	enzyme activity is optimal at 5 mM Mg2+	749277	
6.5.1.3	Mg2+	Km: 0.4 mM, inhibition above 10 mM	1995	
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+	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+	Mg2+ or Mn2+ required	662241	
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	Mg2+	required	1910, 1983, 1995	
6.5.1.3	Mg2+	requires metal ions for structure and catalysis	650172	
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	Mn2+	activates, showing slightly higher activity than Mg2+	662976	
6.5.1.3	Mn2+	enzyme activity is optimal at 2.5 mM Mn2+	749277	
6.5.1.3	Mn2+	Mg2+ or Mn2+ required	662241	
6.5.1.3	Mn2+	only marginal activity	650172	
6.5.1.3	Mn2+	optimum activity at 1 mM	653392	
6.5.1.3	Mn2+	the enzyme prefers manganese as the metal cofactor for nick sealing	749172	
6.5.1.3	additional information	calcium, cobalt, copper, cadmium, nickel, and zinc are ineffective	749277	
6.5.1.3	additional information	no detectable activity with Ca2+, Sr2+, Ba2+, Zn2+, Co2+, Cd2+, Pb2+, Co(NH3)6 3+, or spermine	650172