3.4.23.22	Abz-Thr-Ile-Nle-4-nitro-Phe-Gln-Arg-NH2 + H2O	-	Cryphonectria parasitica	Abz-Thr-Ile-Nle + 4-nitro-Phe-Gln-Arg-NH2	-	?	381296	
3.4.23.22	casein + H2O	splits 29.0% of the peptide bonds	Cryphonectria parasitica	?	-	?	15445	
3.4.23.22	FVNQHLCGSHLVEALYLVCGERGFFYTPKA + H2O	i.e. oxidized insulin B chain, cleavage site specificity	Cryphonectria parasitica	FVN + Gln + HLCGSHL + VEALY + LVCGERGF + FYTPKA	-	?	384732	
3.4.23.22	kappa-casein + H2O	reaction contributes to milk-clotting activity, cleavage site specificity for Ser104-Phe105	Cryphonectria parasitica	?	-	?	369626	
3.4.23.22	additional information	clots milk, not: benzyloxycarbonyl-L-Glu-L-Tyr	Cryphonectria parasitica	?	-	?	89	
3.4.23.22	additional information	the enzyme prefers protein substrates with hydrophobic amino acid residues at P1 and P1' positions	Cryphonectria parasitica	?	-	?	89	
3.4.23.22	Oxidized B-chain of insulin + H2O	the Phe24-Phe25 bond is hydrolyzed at a maximal rate followed by hydrolysis of the Tyr16-Leu17 and Gln4-His5 bonds. The Leu11-Val12 and Asn3-Gln4 bonds are hydrolyzed at slower rates. The Leu11-Val12 bond appears to be considerably more resistant to hydrolysis in the peptide 5-16 than in the intact oxidized B-chain. The Leu15-Tyr16 bond is very slowly hydrolyzed in the peptide 5-16, no hydrolysis in the intact oxidized B-chain. Phe25 is slowly hydrolyzed from the peptide 25-30 and the bond involving Gly20-Glu21 is slowly hydrolyzed in peptide 12-24 and/or peptide 17-24	Cryphonectria parasitica	?	-	?	15386	
3.4.23.22	Pepsin + H2O	splits 8.0% of the peptide bonds	Cryphonectria parasitica	?	-	?	16318	
3.4.23.22	Rennin + H2O	splits 10.2% of the peptide bonds	Cryphonectria parasitica	?	-	?	16319