3.4.11.3	Ca2+	inhibitory effect of EDTA plus 1,10-phenanthroline can be completely reversed by Zn2+. Ca2+ and Mg2+ increase the potency of Zn2+ for this process	667507	
3.4.11.3	Ca2+	reversal of EDTA inhibition	35910	
3.4.11.3	Cl-	stimulation	35911	
3.4.11.3	Co2+	inhibition at high concentration	35898, 35908, 35910	
3.4.11.3	Co2+	reverses EDTA inhibition	28290, 35897, 35902, 35907	
3.4.11.3	Co2+	stimulates	35912, 35915, 35918	
3.4.11.3	Cu2+	partly reverses EDTA inhibition	35897	
3.4.11.3	Mg2+	inhibitory effect of EDTA plus 1,10-phenanthroline can be completely reversed by Zn2+. Ca2+ and Mg2+ increase the potency of Zn2+ for this process	667507	
3.4.11.3	Mn2+	reversal of EDTA inhibition, inhibition at high concentration	28290, 35910	
3.4.11.3	Ni2+	stimulation, reverses EDTA inhibition	35918	
3.4.11.3	Zinc	contains the characteristic Zn2+-coordination sequence element, HEXXH-(18-64X)-E	651116	
3.4.11.3	Zinc	enzyme contains 1 mol of zinc per mol of enzyme, contains the consensus HEXXH(X)18E motif of zinc-metallopeptidase proteins	651074	
3.4.11.3	Zn2+	2 mol Zn2+ per subunit	35900	
3.4.11.3	Zn2+	active site-bound	754389	
3.4.11.3	Zn2+	complete inhibition of the enzyme activity by 0.1 mM EDTA and 0.1 mM 1,10-phenanthroline can be prevented in the presence of 0.04-0.1 mM ZnCl2	667549	
3.4.11.3	Zn2+	inhibitory effect of EDTA plus 1,10-phenanthroline can be completely reversed by Zn2+. Ca2+ and Mg2+ increase the potency of Zn2+ for this process	667507	
3.4.11.3	Zn2+	insulin-regulated aminopeptidase (IRAP) is a membrane-bound zinc metallopeptidase	752375	
3.4.11.3	Zn2+	IRAP is a zinc-dependent aminopeptidase	753121	
3.4.11.3	Zn2+	metalloenzyme	35897, 35900, 35916, 35918	
3.4.11.3	Zn2+	required	753723, 753769, 753943, 754445	
3.4.11.3	Zn2+	required, zinc metalloprotease	755404	
3.4.11.3	Zn2+	reverses EDTA inhibition	28290, 35897, 35902, 35916, 35918