3.4.23.49	2-aminobenzoyl-A-(L)R-(D)R-A-3-[(2,4-dinitrophenyl)amino]-L-alanyl-Gly	-	54268	
3.4.23.49	Al3+	1 mM, 47% residual activity	264	
3.4.23.49	amprenavir	-	1608	
3.4.23.49	Aprotinin	classical protease inhibitors are ineffective against CroP activity, but the serine protease inhibitor aprotinin displays inhibitory potency in the micromolar range. Aprotinin acts as a competitive inhibitor of CroP activity and interferes with the cleavage of the murine cathelicidin-related antimicrobial peptide. Structural model of the aprotinin-omptin complex in which Lys15 of aprotinin forms salt bridges with conserved negatively charged residues of the omptin active site, molecular docking, overview. Aprotinin inhibits CRAMP proteolytic degradation by CroP. Docking model of the aprotinin-omptin complex. Lys15 of aprotinin interacts with Glu27 and Asp208 (OmpT numbering), which are the two negatively charged residues that form the S1 specificity pocket of omptins	405	
3.4.23.49	Aprotinin	ability of EHEC EDL933 cells to cleave the FRET substrate in the presence of increasing concentrations of aprotinin, about 90% inhibition at 0.2 mM. Docking model of the aprotinin-omptin complex. Lys15 of aprotinin interacts with Glu27 and Asp208 (OmpT numbering), which are the two negatively charged residues that form the S1 specificity pocket of omptin	405	
3.4.23.49	Aprotinin	inhibits CroP in a competitive manner	405	
3.4.23.49	Aprotinin	inhibits OmpT in a competitive manner	405	
3.4.23.49	arginine	-	532	
3.4.23.49	atazanavir sulfate	-	239975	
3.4.23.49	benzamidine	-	579