3.4.15.1	CaCl2	activates in absence of Cl-, maximal activity at 0.3 mM	81235	
3.4.15.1	Cl-	the activity of the C-domain of sACE depends highly on chloride ion concentration and is inactive in its absence, whereas the N-domain can be completely activated at relatively low concentrations of this anion and is still active in the absence of chloride	708830	
3.4.15.1	Co2+	activates, but to a lesser extent than Zn2+	755273	
3.4.15.1	Co2+	activation	81260, 81285, 81287	
3.4.15.1	Co2+	CoCl2 stimulates	81269	
3.4.15.1	CoCl2	0.1-1.0 mM, 2fold activation	650873	
3.4.15.1	KBr	activation is lower than with NaCl	81264	
3.4.15.1	KI	activation is lower than with NaCl	81264	
3.4.15.1	Mn2+	activates, but to a lesser extent than Zn2+	755273	
3.4.15.1	additional information	enzyme is not affected by addition of 0.1-1.0 mM CaCl2, Mn2Cl2, MgCl2 or 0.1 mM ZnCl2	650873	
3.4.15.1	Na+	at pH 7 increasing concentrations of NaCl result in a faster rate of conversion which reaches a plateau at 150-200 mM NaCl. The activation by NaCl at pH 7 is the result of a 330% increase in kcat/Km which is solely attributable to a lowering of the Km. At pH 8, maximal activity is achieved in absence of NaCl, weak inhibitory effect on hydrolysis of angiotensin I as salt concentrations increase from 0 to 200 mM	668570	
3.4.15.1	Na+	maximum activity at 75 mM NaCl	731940	
3.4.15.1	Na+	rats exposed to a high-sodium diet show an enhanced ACE activity	732968	
3.4.15.1	Na2SO4	activates in absence of Cl-	81235	
3.4.15.1	NaCl	-	81254	
3.4.15.1	NaCl	500 mM, 50% inhibition	81286	
3.4.15.1	NaCl	activates	709304, 81250, 81255, 81257, 81269	
3.4.15.1	NaCl	activates in absence of Cl-	81235	
3.4.15.1	NaCl	maximal activation at 20 mM NaCl, hydroysis of angiotensin I	81236	
3.4.15.1	NaCl	maximal activation at 620 mM NaCl, hydrolysis of hippuryl-His-Leu	81236	
3.4.15.1	NaCl	required	81263, 81274	
3.4.15.1	NaCl	stimulates hydrolysis of hippuryl-His-Leu in concentration-dependent manner between 0 and 300 mM	81244	
3.4.15.1	NaF	activation is lower than with NaCl	81264	
3.4.15.1	Zinc	-	81209, 81211, 81241	
3.4.15.1	Zinc	0.3 mM ZnCl2 completely reverses the inhibition caused by 0.1 mM EDTA	81254	
3.4.15.1	Zinc	a single Zn atom is bound per molecule of enzyme	81278	
3.4.15.1	Zinc	contains 0.8 gatom of zinc per mol of enzyme	81211	
3.4.15.1	Zinc	contains 0.9 gatom of zinc per mol of enzyme	81211	
3.4.15.1	Zinc	contains 1.2 gatom of zinc per mol of enzyme	81211	
3.4.15.1	Zinc	contains approximately 1 gatom of zinc per mol of enzyme	81259, 81270, 81272	
3.4.15.1	Zinc	contains approximately one molar equivalent of bound zinc	81209	
3.4.15.1	Zinc	contains zinc	81215, 81225, 81226, 81284, 81287	
3.4.15.1	Zinc	required	81241	
3.4.15.1	Zinc	XcACE activity depends on zinc binding. Hydrolysis of 7-methoxycoumarin-4-yl-diacetyl-SDKP-N3 (2,4-dinitrophenyl)L-2,3-diaminopropionyl-OH is abolished after zinc chelation with EDTA and dialysis but is restored by zinc addition	679999	
3.4.15.1	Zn2+	-	707443, 707653, 732308	
3.4.15.1	Zn2+	a highly ordered Zn2+ is bound at the active site	668218	
3.4.15.1	Zn2+	ACE is a metallopeptidase. An activated water molecule complexed to Zn2+ acts as the nucleophile to attack the carbonyl group of the targeted peptide bond	708830	
3.4.15.1	Zn2+	ACE is a zinc dipeptidyl carboxypeptidase	755554	
3.4.15.1	Zn2+	ACE is a zinc-metalloprotease	710612	
3.4.15.1	Zn2+	activates	709470	
3.4.15.1	Zn2+	activates enzymatic activity	732845	
3.4.15.1	Zn2+	assay in the presence of zinc and chloride	764572	
3.4.15.1	Zn2+	catalytically important	710213	
3.4.15.1	Zn2+	contains zinc	696268	
3.4.15.1	Zn2+	required	709786	
3.4.15.1	Zn2+	required, activates	755273	
3.4.15.1	Zn2+	the enzyme is a Zn2+ peptidyldipeptidase	755108	
3.4.15.1	Zn2+	zinc metallopeptidase	701190