4.1.1.45	Cd2+	activates	665303	
4.1.1.45	Cd2+	requires transition metal divalent cations for substrate activation	678136	
4.1.1.45	Co2+	-	678137	
4.1.1.45	Co2+	1.0 mM, increases activity to 130%	679800	
4.1.1.45	Co2+	activates	665303	
4.1.1.45	Co2+	after purification, Co2+-reconstituted ACMSD exhibits the highest activity and the greatest stability	680375	
4.1.1.45	Co2+	Co-substituted ACMSD shows a comparable activity to the native enzyme	691974	
4.1.1.45	Co2+	requires transition metal divalent cations for substrate activation	678136	
4.1.1.45	Fe2+	0.1 mM, increases activity to 124%	679800	
4.1.1.45	Fe2+	activates	665303	
4.1.1.45	Fe2+	requires transition metal divalent cations for substrate activation	678136	
4.1.1.45	MgCl2	slightly stimulates	4567	
4.1.1.45	Mn2+	-	680375	
4.1.1.45	Mn2+	activates	665303	
4.1.1.45	Mn2+	requires transition metal divalent cations for substrate activation	678136	
4.1.1.45	additional information	Fe3+, Cu2+ not activating	665303	
4.1.1.45	additional information	not influenced by 1 mM Mg2+, Mn2+, Ni2+ or Ca2+	679800	
4.1.1.45	additional information	the addition of one to ten equivalents of Co2+, Cu2+, Fe2+, or Zn2+ to purified ACMSD does not increase enzyme activity	749250	
4.1.1.45	additional information	the pure enzyme is 100% active in the absence of any metal ion	679800	
4.1.1.45	Zn2+	-	703670	
4.1.1.45	Zn2+	contains zinc	726993	
4.1.1.45	Zn2+	essential cofactor	691974	
4.1.1.45	Zn2+	native active site metal	678137	
4.1.1.45	Zn2+	requires transition metal divalent cations for substrate activation	678136	
4.1.1.45	Zn2+	the activity of ACMSD is proportional to the zinc content of the enzyme	749250