1.14.14.10	Mg2+	the enzyme shows little preference for Mg-nitrilotriacetate over Co-nitrilotriacetate, Ni-nitrilotriacetate, and Zn-nitrilotriacetate	717545	
1.14.14.10	Mn2+	Mn2+ ions are able to replace Mg2+ but lead to a higher uncoupled NADH oxidation and enzyme activity is reduced to 70% of that with MgCl2	715329	
1.14.14.10	additional information	no nitrilotriacetate consumption is observed with Ca2+,Fe2+, Fe3+, Zn2+, Cu2+, or Ni2+	715329	
1.14.14.10	additional information	the enzyme contains less than 0.15 atom of Fe per mol of protein, indicating that neither Fe-sulfur clusters nor cytochromes are present	715329	
1.14.14.10	Ni2+	nitrilotriacetate is only a substrate when complexed with cations such as Mg2+, Al3+, Cu2+, Ni2+, Zn2+, Fe2+ or Co2+	717545	
1.14.14.10	Zn2+	nitrilotriacetate is only a substrate when complexed with cations such as Mg2+, Al3+, Cu2+, Ni2+, Zn2+, Fe2+ or Co2+	717545