2.7.1.180	Ca2+	presence of a Ca2+ ion in metal site 1 in the apo form of mutant Ftp_EcY60N, the Ca2+ ion serves a role in properly positioning substrate and protein residues	757628	
2.7.1.180	Cd2+	highly activates by 4fold	762233	
2.7.1.180	Co2+	activates	762233	
2.7.1.180	Mg2+	dependent on	725516	
2.7.1.180	Mg2+	dependent on, metal-dependent enzyme	757628	
2.7.1.180	Mg2+	dependent on, metal-dependent enzyme, bimetal center in the crystal structure of Escherichia coli Ftp	757628	
2.7.1.180	Mg2+	required	761498	
2.7.1.180	Mg2+	required for catalysis, Mg2+ does not play a major role in stabilizing the interaction of the protein with FAD, Mg2+ in the preferred divalent cation	762233	
2.7.1.180	Mg2+	required, dependent on, Mg2+ ion is directly involved in catalysis. A single metal ion is bound in the wild-type enzyme and mutant Ftp_EcE169K structures. The inhibited mutant Ftp_EcY60N contains a bimetal Mg2+ center	757628	
2.7.1.180	Mn2+	activates	762233	
2.7.1.180	additional information	divalent cations are essential for ApbE activity, and their removal by EDTA abolishes the activity. ApbE is also able to use other divalent cations, such as Mn2+ and Co2+, obtaining a similar activity compared to Mg2+. The coordination sphere of ApbE enzymes largely determines the specificity of the enzyme for the divalent cation	762233	
2.7.1.180	additional information	identification of a bimetal center in the crystal structure of Escherichia coli Ftp (Ftp_Ec)	757628