3.4.22.B69	Abz-KLRFSKQ-EDDnp + H2O	-	Plasmodium falciparum	?	-	?	431510	
3.4.22.B69	Abz-KLRSSKQ-EDDnp + H2O	-	Plasmodium falciparum	?	-	?	418378	
3.4.22.B69	Abz-KLRSXKQ-EDDnp + H2O	-	Plasmodium falciparum	Abz-KLRS + XKQ-EDDnp	-	?	431511	
3.4.22.B69	Abz-KLRXSKQ-EDDnp + H2O	-	Plasmodium falciparum	Abz-KLR + XSKQ-EDDnp	-	?	431512	
3.4.22.B69	Abz-KLXSSKQ-EDDnp + H2O	-	Plasmodium falciparum	Abz-KLX + SSKQ-EDDnp	-	?	431514	
3.4.22.B69	Abz-KXRSSKQ-EDDnp + H2O	-	Plasmodium falciparum	Abz-KXR + SSKQ-EDDnp	-	?	431521	
3.4.22.B69	Abz-MISLMKRPPGFSPFRSSRI-NH2 + H2O	the peptide corresponds to the Met375 to Ile393 sequence of high molecular weight kininogen. The enzyme preferentially accommodates at the S1 subsite the positively charged residue Arg, followed by Gln. At the P2 position, the enzyme shows a clear preference for the hydrophobic aliphatic residue Leu over Phe. The subsite S3 of FP-2 shows a broad specificity with slight preference of Lys in the P3 position	Plasmodium falciparum	?	the generated fragments are KRPPGFSPFR (Lys-bradykinin, 63%), RPPGFSPFR (bradykinin, 30%), and MKRPPGFSPFR (Met-Lys-bradykinin, 7%)	?	431533	
3.4.22.B69	Abz-XLRSSKQ-EDDnp + H2O	-	Plasmodium falciparum	Abz-XLR + SSKQ-EDDnp	-	?	431553	
3.4.22.B69	benzyloxycarbonyl-Leu-Arg-7-amido-4-methylcoumarin + H2O	-	Plasmodium falciparum	benzyloxycarbonyl-Leu-Arg + 7-amino-4-methylcoumarin	-	?	362766	
3.4.22.B69	benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O	-	Plasmodium falciparum	benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin	-	?	361886