3.4.21.62	Ca2+	-	688387, 689851, 690033	
3.4.21.62	Ca2+	as found in other Bacillus subtilisins, the structure of wild-type Savinase contains 2 calcium ion-binding sites	29435	
3.4.21.62	Ca2+	bound calcium ions play a key role in protecting against autolysis and thermal denaturation	649692, 652805	
3.4.21.62	Ca2+	Ca2+-binding loop is required for folding of subtilisin but does not seriously contribute to the stabilization of subtilisin in a native structure	707480	
3.4.21.62	Ca2+	calcium ion binds weakly to the Ca-7 site in the unautoprocessed form, but is trapped upon autoprocessing. The Ca-7 site is required to promote the autoprocessing reaction by stabilizing the autoprocessed form, in which the new N-terminus of the mature domain is structurally disordered	688371	
3.4.21.62	Ca2+	calcium-loaded state of five ions bound to each of the two subtilisin molecules. Three of the binding sites have two side chains of an acidic residue coordinating the calcium ion, whereas the other two binding sites have either a main-chain carbonyl, or only one acidic residue side chain coordinating the calcium ion	710507	
3.4.21.62	Ca2+	enzyme activity and/or stability depends on the presence of divalent cations, probably Ca2+ ions, near the surface of the enzyme	707260	
3.4.21.62	Ca2+	five binding sites, important for correct folding	678747	
3.4.21.62	Ca2+	importance of calcium in the medium after enzyme induction, both for stability of the proteinase and cell health. The two calcium binding sites have apparent binding constants in the mM range. Binding of calcium to the weaker of those two sites only affects resistance of the enzyme against irreversible thermal inactivation. Kinetics	752829	
3.4.21.62	Ca2+	in the presence of calcium the half-life at 55°C and 60°C are 3.6fold and 3.48fold higher for the native enzyme compared to that in the absence of added calcium. In the presence of 10 mM calcium the half-life of the enzyme at 60°C increases by 6.06fold, 5.20fold and 2.92fold when coupled with oxidized sucrose polymers OSP400, OSP70 and polyglutaraldehyde, respectively	686432