3.5.1.104	Ca2+	activates	730006	
3.5.1.104	Co2+	0.05 mM, 30fold increase in activity	689736	
3.5.1.104	Co2+	1 mM, 10% increase in activity	687500	
3.5.1.104	Co2+	activates, best metal ion	733581	
3.5.1.104	Fe2+	abolishes the acnB-pgdA transcript binding leading to destabilization of the enzyme's mRNA	729936	
3.5.1.104	Mg2+	activates	730006	
3.5.1.104	Mn2+	best activating metal ion	730006	
3.5.1.104	additional information	metal site models show an intrinsic preference for zinc, but also significant flexibility of the site so that binding of other ions can eventually occur, e.g. Fe2+, Co2+, Cu2+, Mg2+, quantum chemical calculations, overview	730914	
3.5.1.104	additional information	metallo-dependent enzyme	733581	
3.5.1.104	additional information	SpPgdA is a metalloenzyme using a His-His-Asp zinc-binding triad with a nearby aspartic acid and histidine acting as the catalytic base and acid, respectively	689736	
3.5.1.104	additional information	the enzyme requires divalent cations	730006	
3.5.1.104	Ni2+	activates	730006	
3.5.1.104	Zn2+	0.05 mM, 5.5fold increase in activity	689736	
3.5.1.104	Zn2+	a zinc metalloenzyme	752966	
3.5.1.104	Zn2+	a zinc metalloenzyme, active site metal	752784	
3.5.1.104	Zn2+	a zinc metalloenzyme, active site-bound	754478	
3.5.1.104	Zn2+	divalent metal binding site, one site per enzyme monomer, essential for the enzyme's catalytic activity, structure analysis, detailed overview	730914	
3.5.1.104	Zn2+	lower dependence on zinc or nickel ions for deacetylation of peptidoglycan by the enzyme than other metal ions, Mn2+, Mg2+, and Ca2+	730006	
3.5.1.104	Zn2+	the zinc ion of the metalloenzyme is coordinated by a conserved binding triad of amino acids consisting of one aspartate and two histidine residues, determination of the metal-binding site, which is essential for the enzyme's catalytic activity, one metal site per monomer, structure and quantum chemical calculations of models, overview. The metal ion occupies a tetrahedral environment with binding to one of the carboxylic oxygen of Asp14, His86, His90 and a water molecule	730914