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	
3.4.23.49	calf thymus histone H2B	growth inhibitory activity against bacterial gene expressing Escherichia coli with calculated 50% growth inhibitory concentrations of 3.8 microM. Histone H2B penetrates the cell membrane of JCM5491 OmpT+ cells	86661	
3.4.23.49	calf thymus histone H3	growth inhibitory activity against bacterial gene expressing Escherichia coli with calculated 50% growth inhibitory concentrations of 10 microM. Histones H3 and H4 remain on the cell surface and subsequently disrupt the cell membrane structure with bleb formation in a manner similar to general antimicrobial peptides	86662	
3.4.23.49	calf thymus histone H4	growth inhibitory activity against bacterial gene expressing Escherichia coli with calculated 50% growth inhibitory concentrations of 12.7 microM. Histones H3 and H4 remain on the cell surface and subsequently disrupt the cell membrane structure with bleb formation in a manner similar to general antimicrobial peptides	86663	
3.4.23.49	Co2+	-	23	
3.4.23.49	Cu2+	-	19	
3.4.23.49	Cu2+	CuCl2	19	
3.4.23.49	Cu2+	1 mM, 77% residual activity	19	
3.4.23.49	Cu2+	enzyme binding study	19	
3.4.23.49	CuCl2	significant inhibition at 1 mM	347	
3.4.23.49	darunavir	-	1901	
3.4.23.49	diisopropyl fluorophosphates	-	11341	
3.4.23.49	diisopropylfluorophosphate	-	299	
3.4.23.49	diisopropylfluorophosphate	significant inhibition only at high concentrations	299	
3.4.23.49	Fe2+	-	25	
3.4.23.49	fosamprenavir	-	167956	
3.4.23.49	guanidine hydrochloride	50 mM, 40% residual activity	1048	
3.4.23.49	indinavir	-	1036	
3.4.23.49	lipopolysaccharide	i.e. LPS, rough, dependent on, interacts with the beta-barrel in the outer membrane, function and mechanism overview, smooth LPS sterically inhibits the enzyme via its O-side chain	890	
3.4.23.49	Mg2+	enzyme binding study	6	
3.4.23.49	additional information	not: EDTA, phenylmethylsulfonyl fluoride	2	
3.4.23.49	additional information	molecular docking study with protease inhibitors, overview. No interaction with lopinavir and tipranavir	2	
3.4.23.49	NaCl	optimal activity in absence of NaCl, 80% inhibition by 0.15 M NaCl	42	
3.4.23.49	nelfinavir	-	1193	
3.4.23.49	pepstatin	-	396	
3.4.23.49	pepstatin A	5 mM, complete loss of activity	309	
3.4.23.49	phenylmethylsulfonyl fluoride	-	257	
3.4.23.49	phenylmethylsulfonyl fluoride	poor inhibitor, only at high concentrations	257	
3.4.23.49	ritonavir	-	996	
3.4.23.49	saquinavir	-	997	
3.4.23.49	SDS	0.02%, complete loss of activity	124	
3.4.23.49	tosyl-L-phenylalanine chloromethyl ketone	-	9281	
3.4.23.49	Tween 20	up to 1%, 80% residual activity	555	
3.4.23.49	Urea	50 mM, 72% residual activity	116	
3.4.23.49	Zn	-	932	
3.4.23.49	Zn2+	-	14	
3.4.23.49	Zn2+	uncompetitive, pH-dependent; ZnCl2	14	
3.4.23.49	Zn2+	ZnCl2	14	
3.4.23.49	Zn2+	enzyme binding study	14	
3.4.23.49	ZnCl2	significant inhibition at 1 mM	271