1.2.1.46	Ca2+	is required for the stabilization of the tetrameric structure of dlFalDH and for its optimal functionality	690569	
1.2.1.46	Ca2+	plays an important role in the active centre of DL-FDH and for the sensing purpose	690106	
1.2.1.46	Cu2+	the protein contains 1.3 mol of Cu2+. The highest activity, 22fold increase, is found in the protein produced in the presence of 0.025 mM Cu2+	762739	
1.2.1.46	Fe2+	a 20fold increase in activity is found in the protein produced in the presence of 0.025 mM Fe2+	762739	
1.2.1.46	additional information	independent of Mg2+	288246	
1.2.1.46	additional information	the presence or absence of metal ions (0.1 mM) in the reaction mixture does not affect the enzyme activity	762739	
1.2.1.46	Zinc	active-site zinc-liganding amino acids: Cys-47 and His-68	288253	
1.2.1.46	Zinc	structural zinc-liganding amino acids: Cys-97, Cys-100, Cys-103, Cys-111	288253	
1.2.1.46	Zinc	zinc metalloenzyme, 2 zinc atoms per subunit, one participates in catalytic activity, the other is involved in maintaining the native conformation of the enzyme	288250	
1.2.1.46	Zn2+	-	667724	
1.2.1.46	Zn2+	contains zinc	762614, 763486	
1.2.1.46	Zn2+	required	741521, 743745	
1.2.1.46	Zn2+	the protein contains 1.5 mol of Zn2+. An increase in activity is found in the protein produced in the presence of 0.025 mM Zn2+	762739	
1.2.1.46	Zn2+	two ions bound per subunit	655673, 656507