3.4.21.12	Eglin c	very effective inhibitor	2653	
3.4.21.12	Eglin c	-	2653	
3.4.21.12	guanidine hydrochloride	1% residual activity in the presence of 4 mM guanidine hydrochloride	1048	
3.4.21.12	methoxysuccinyl-Ala-Ala-Pro-L-boroPhe	the carboxylate of the C-terminal amino acid residue is replaced with B(OH)2. Boron-11 pure quadrupole resonance investigation indicates close to tetrahedral boron coordination in the active site of the enzyme/inhibitor complex	117726	
3.4.21.12	methoxysuccinyl-Ala-Ala-Pro-L-boroVal	the carboxylate of the C-terminal amino acid residue is replaced with B(OH)2. Boron-11 pure quadrupole resonance investigation indicates tetrahedral boron coordination in the active site of the enzyme/inhibitor complex	117725	
3.4.21.12	additional information	-	2	
3.4.21.12	additional information	mechanism	2	
3.4.21.12	additional information	lyophilization induces a structural change in the enzyme that is not reversed by redissolution in water. The structural change reduces the mobility of the active-site histidine residue and the catalytic activity of the enzyme. The application of mild pressure to solutions of the altered enzyme reverses the lyophilization-induced structural change and restores the mobility of the histidine residue and the enzyme's catalytic activity	2	
3.4.21.12	N-terminal 166 amino acid Pro region of alpha-lytic protease	dual role of folding and inhibition	101143	
3.4.21.12	N-Tert-butyloxycarbonylalanylpropylvaline boronic acid	-	46343	
3.4.21.12	SDS	42% residual activity in the presence of 1% (w/v) SDS	124	
3.4.21.12	Turkey ovomucoid third domain	OMTKY3, very weak inhibitor, different mutations in the inhibitory protein are found to affect the inhibitory effect	20986	
3.4.21.12	Turkey ovomucoid third domain	Turkey Ovomucoid Third Domain (OMTKY3) inhibits the enzyme much more weakly (by about 1000000times) than eglin C. A variant of OMTKY3 with five mutations K13A/P14E/L18A/R21T/N36D inhibits 10000times more strongly than the wild type inhibitor	20986	
3.4.21.12	Urea	12% residual activity in the presence of 4 mM urea	116