3.4.11.20	Ca2+	activates	665073	
3.4.11.20	Ca2+	activates the inactive, Zn2+-free apoenzyme	647083	
3.4.11.20	Cd2+	activates	665073	
3.4.11.20	Cd2+	activates the inactive, Zn2+-free apoenzyme	647083	
3.4.11.20	Co2+	activates	665073	
3.4.11.20	Co2+	activates the inactive, Zn2+-free apoenzyme	647083	
3.4.11.20	Co2+	reactivates 1,10-phenanthroline inactivated apoenzyme	95176	
3.4.11.20	Cu2+	activates	665073	
3.4.11.20	Cu2+	activates the inactive, Zn2+-free apoenzyme	647083	
3.4.11.20	Mn2+	activates	665073	
3.4.11.20	Mn2+	activates the inactive, Zn2+-free apoenzyme	647083	
3.4.11.20	additional information	no activation of the inactive, Zn2+-free apoenzyme by Mg2+ and Fe2+	647083	
3.4.11.20	additional information	the enzyme is a metalloenzyme, the apoenzyme is inactive	665073	
3.4.11.20	Ni2+	activates	665073	
3.4.11.20	Ni2+	activates the inactive, Zn2+-free apoenzyme	647083	
3.4.11.20	Zinc	a zinc protein, contains 1.0 gatom of zinc/mol of a subunit	647083, 647085	
3.4.11.20	Zinc	activates the inactive, Zn2+-free apoenzyme	647083	
3.4.11.20	Zinc	zinc-binding sites: His386, His390 and Glu409	647085	
3.4.11.20	Zn2+	-	718071, 718321	
3.4.11.20	Zn2+	activates, required for activity and stability, zinc is bound by residues His386, His390, and Glu409	665073	
3.4.11.20	Zn2+	treatment with 1,10-phenanthroline in order to deplete metal ions, results in a residual activity of about 8% compared to the initial activity. Activity is partially restored by the addition of divalent metal cations with Zn2+ being the most potent	731736