3.4.15.1	cetyltrimethylammonium bromide	0.1 and 1 mM	732845	
3.4.15.1	cetyltrimethylammonium bromide	CTAB, activates at 0.1-1.0 mM	755273	
3.4.15.1	Cl-	-	81241, 81260, 81287	
3.4.15.1	Cl-	activates	650267, 81212, 81214, 81250, 81264, 81270, 81284	
3.4.15.1	Cl-	activation, optimal NaCl concentration for the brain enzyme in hydrolysis of LVVYPWTQRY is 10 mM, optimal concentration for hydrolysis of angiotensin I is 200 mM	653416	
3.4.15.1	Cl-	assay in the presence of zinc and chloride	764572	
3.4.15.1	Cl-	kcat increases with increasing KCl concentrations, reaches a maximum at about 300 mM KCl, and the begins to decrease. At relatively low concentrations chloride anions activate the C-domain of the enzyme, but at high concentrations chloride inhibits the enzyme activity. Presence of at least two chloride-binding sites in the C-domain of bovine enzyme: binding of chloride to one of the sites causes activation of the enzyme, whereas chloride binding to the second site results in inhibition of the enzymatic activity	667760	
3.4.15.1	Cl-	nonessential activator over the pH range 5.0-10.0	81233	
3.4.15.1	Cl-	required	81213, 81247, 81251, 81259	
3.4.15.1	Cl-	required for hydrolysis of angiotensin I, not required for hydrolysis of bradykinin	81241