3.5.4.4	Ba2+	-	686577	
3.5.4.4	CoSO4	-	209631	
3.5.4.4	Fe2+	the activity found in the enzymes expressed with added Zn(II) and added Fe(II) are 2fold higher than when expressed with Ni(II) or without additional metal	727779	
3.5.4.4	Fe3+	-	209627, 209630	
3.5.4.4	Hg2+	-	686577	
3.5.4.4	K+	-	209616	
3.5.4.4	Li+	-	209613	
3.5.4.4	lithium ion	-	686577	
3.5.4.4	Mg2+	91% inhibition	686577	
3.5.4.4	Mg2+	activates	686612	
3.5.4.4	MgCl2	-	209631	
3.5.4.4	additional information	metal-dependent enzyme. The metal can not be removed from the enzyme nor can the nature of the catalytic metal be established. Dialysis of the wild-type enzyme for 3 days against a dipicolinic acid containing buffer fails to show any lowering enzyme activity, again indicating that chelation is not able to remove the bound metal in the active site. The catalytic metal is not removed by EDTA	727779	
3.5.4.4	additional information	no effect on activity of Ca2+, Mg2+	697462	
3.5.4.4	additional information	there are no significant changes in ADA activity in the presence of cadmium acetate, potassium dichromate, lead acetate, zinc chloride, copper sulfate, cobalt chloride, and manganese chloride	713127	
3.5.4.4	Na+	-	209616	
3.5.4.4	Ni2+	-	686577	
3.5.4.4	Ni2+	the activity found in the enzymes expressed with added Zn(II) and added Fe(II) are 2fold higher than when expressed with Ni(II) or without additional metal	727779	
3.5.4.4	Sn2+	-	209630	
3.5.4.4	Zn2+	-	686577, 699553	
3.5.4.4	Zn2+	ADA contains a tightly bound Zn2+ which is required for activity, the stability of the protein is decreased significantly in the absence of Zn2+	712858	
3.5.4.4	Zn2+	coordinated by His15, His17, His214, and Asp295	669783	
3.5.4.4	Zn2+	the activity found in the enzymes expressed with added Zn(II) and added Fe(II) are 2fold higher than when expressed with Ni(II) or without additional metal	727779	
3.5.4.4	Zn2+	zinc-metalloenzyme, binding structure	669846