3.4.22.71	(Z)-3-(2,5-dimethoxyphenyl)-2-(4-methoxyphenyl) acrylonitrile	potential of this inhibitor for the treatment of Staphylococcus aureus infections	35474	
3.4.22.71	(Z)-3-(2,5-dimethoxyphenyl)-2-(4-methoxyphenyl) acrylonitrile	50% inhibition with 0.0101 mg/ml	35474	
3.4.22.71	berberine chloride	potential of this inhibitor for the treatment of Staphylococcus aureus infections	23056	
3.4.22.71	beta-sitosterol-3-O-glucopyranoside	potential of this inhibitor for the treatment of Staphylococcus aureus infections	23760	
3.4.22.71	coptisine	coptisine can bind to the active pocket of SrtB, residues Arg115, Asn116, and Ile182 play a vital role in the interaction of SrtB with coptisine. Coptisine can reduce the adhesion of Staphylococcus aureus to human lung epithelial cells	11195	
3.4.22.71	galangin	IC50 for recombinant SrtB(DELTA30): 0.03837 mM, no antibacterial activity against Staphylococcus aureus	2110	
3.4.22.71	galangin-3-methyl ether	IC50 for recombinant SrtB(DELTA30): 0.1136 mM, no antibacterial activity against Staphylococcus aureus	23762	
3.4.22.71	isorhamnetin	IC50 for recombinant SrtB(DELTA30): 0.04335 mM, no antibacterial activity against Staphylococcus aureus	1977	
3.4.22.71	kaempferol	IC50 for recombinant SrtB(DELTA30): 0.02455 mM, no antibacterial activity against Staphylococcus aureus	408	
3.4.22.71	additional information	aryl (beta-amino)ethyl ketones inhibit sortase enzymes. Inhibition of sortases occurs through an irreversible, covalent modification of their active site cysteine. Sortases specifically activate this class of molecules via beta-elimination, generating a reactive olefin intermediate that covalently modifies the cysteine thiol	2