2.3.2.5	Ca2+	contains a calcium ion	720244	
2.3.2.5	Co2+	enzyme inactivated by 1,10-phenanthroline or dipicolinic acid can be restored partially by Co2+ or Mn2+	659288	
2.3.2.5	Mn2+	enzyme inactivated by 1,10-phenanthroline or dipicolinic acid can be restored partially by Co2+ or Mn2+	659288	
2.3.2.5	additional information	human glutaminyl cyclase and bacterial zinc aminopeptidase share a common fold and active site. Glutaminyl cyclase does not appear to require zinc for enzymatic activity	658350	
2.3.2.5	additional information	substrate specificity for substrates with uncharged backbone and for Gln-Ala and Gln-Glu, does not change significantly by salt addition. With the positively charged substrates Gln-Arg-Gly-Ile-NH2 and Gln-Lys-Arg-Leu-NH2 addition of salt reveals a positive effect on catalysis	658233	
2.3.2.5	additional information	substrate specificity for substrates with uncharged backbone does not change significantly by salt addition. For substrates such as Gln-Ala and Gln-Glu, addition of KCl decreases specificity. With the positively charged substrates Gln-Arg-Gly-Ile-NH2 and Gln-Lys-Arg-Leu-NH2 addition of salt reveals a positive effect on catalysis	658233	
2.3.2.5	additional information	the enzyme is metal-independent	735370	
2.3.2.5	Zinc	contains one zinc ion per protein molecule	660450	
2.3.2.5	Zinc	stoichiometric amounts of zinc bound to protein. Depletion of zinc has no significant effect on protein structure, metal has a catalytic role	671982	
2.3.2.5	Zn	equimolar protein-bound zinc	685085	
2.3.2.5	Zn2+	-	702268, 704085	
2.3.2.5	Zn2+	0.5 mol of zinc per mole of enzyme	735370	
2.3.2.5	Zn2+	active site bound and involved in catalysis	759909	
2.3.2.5	Zn2+	contains zinc	718944, 735749, 736239	
2.3.2.5	Zn2+	enzyme inactivated by 1,10-phenanthroline or dipicolinic acid can be fully restored by addition of Zn2+ in the presence of equimolar concentrations of EDTA	659288	
2.3.2.5	Zn2+	involved in catalysis, the Zn2+ ion located at the active site of QC polarizes the gamma-amide group of the substrate Gln residue and stabilizes the oxyanion formed by the nucleophilic attack of the alpha-nitrogen on the scissile gamma-carbonyl carbon	759909	
2.3.2.5	Zn2+	required	758906, 759074, 760123	
2.3.2.5	Zn2+	required for catalysis	759510	
2.3.2.5	Zn2+	the active site is coordinated to three conserved residues and one water molecule, which is replaced by an imidazole nitrogen upon binding of inhibitor	660382	
2.3.2.5	Zn2+	the enzyme contains a catalytic zinc ion	718904	
2.3.2.5	Zn2+	the enzyme contains one zinc ion	719915