3.4.21.63	Ca2+	19% activation at 5 mM, no activation at 2 mM	753873	
3.4.21.63	Ca2+	activates 26% at 1 mM	754496	
3.4.21.63	Ca2+	activates 35% at 1 mM	680260	
3.4.21.63	Ca2+	activates 82.6% at 10 mM	752341	
3.4.21.63	Ca2+	stimulates recombinant and native enzyme	682690	
3.4.21.63	Co2+	activates 21.1% at 10 mM	752341	
3.4.21.63	Cu2+	activates 47% at 1 mM	754408	
3.4.21.63	Cu2+	activation	29491	
3.4.21.63	Fe2+	13% activation at 2 mM, 40% at 5 mM	753873	
3.4.21.63	Fe2+	activates 1.74fold at 5 mM	717055	
3.4.21.63	K+	activates 15% at 10 mM	754276	
3.4.21.63	K+	activates about 10% at 5 mM	717055	
3.4.21.63	Mg2+	20% activation at 5 mM, no activation at 2 mM	753873	
3.4.21.63	Mg2+	activates 17% at 1 mM	754496	
3.4.21.63	Mg2+	activates 19% at 1 mM	680260	
3.4.21.63	Mg2+	activates 5% at 10 mM	754276	
3.4.21.63	Mg2+	activates 52.2% at 10 mM	752341	
3.4.21.63	Mg2+	stimulates recombinant and native enzyme	682690	
3.4.21.63	Mn2+	21% activation at 2 mM, 14% at 5 mM	753873	
3.4.21.63	Mn2+	activates 13% at 1 mM	754408	
3.4.21.63	Mn2+	activates 14.5% at 10 mM	754276	
3.4.21.63	additional information	a metal-ion-independent serine protease	754496	
3.4.21.63	additional information	no effect on activity by Ca2+	754276	
3.4.21.63	additional information	no effect on enzyme activity by 5 mM Pb2+. Effect of metal salts on enzyme production, overview	717055	
3.4.21.63	additional information	no metal ions examined show stimulatory effect	29487	
3.4.21.63	additional information	no or poor effects by 10 mM of K+, Ba2+, Cu2+, and Fe2+	752341	
3.4.21.63	additional information	no significant effect with Mn2+ and Cu2+ at 2-5 mM	753873	
3.4.21.63	Na+	14% activation at 2 mM, no activation at 5 mM	753873	
3.4.21.63	Na+	activates about 10% at 5 mM	717055	
3.4.21.63	NaCl	activates at up to 12% w/v, the enzyme is stable up to 20% w/v, thermal stability of the enzyme is substantially improved by NaCl	753842	
3.4.21.63	NaCl	over 20% relative activity of the enzyme remains in the presence of 3.0 mo/l NaCl after 7 days, but its Km and Vmax are only mildly influenced. The salt-tolerant mechanisms of the enzyme might be due to more salt bridges, higher proportion of ordered secondary structures and stronger hydrophobic amino acid residues in the interior	754496	
3.4.21.63	Ni2+	activates 12% at 1 mM	754408	
3.4.21.63	Zn2+	the enzyme has a zinc-binding motif and is a gluzincin	731961