EC Number |
Inhibitors |
Structure |
---|
3.4.22.71 | more |
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 |
|
3.4.22.71 | quercetin |
IC50 for recombinant SrtB(DELTA30): 0.03328 mM, no antibacterial activity against Staphylococcus aureus |
|
3.4.22.71 | kaempferol |
IC50 for recombinant SrtB(DELTA30): 0.02455 mM, no antibacterial activity against Staphylococcus aureus |
|
3.4.22.71 | myricetin |
IC50 for recombinant SrtB(DELTA30): 0.03689 mM, no antibacterial activity against Staphylococcus aureus |
|
3.4.22.71 | morin |
IC50 for recombinant SrtB(DELTA30): 0.00854 mM, no antibacterial activity against Staphylococcus aureus |
|
3.4.22.71 | phloretin |
compound shows little anti-Staphylococcus aureus activity, but significantly inhibit SrtB activity in vitro. Phloretin reduces human alveolar epithelial cell damage caused by Staphylococcus aureus. Phloretin directly localizes in the active pocket of SrtB and blocks substrate binding |
|
3.4.22.71 | isorhamnetin |
IC50 for recombinant SrtB(DELTA30): 0.04335 mM, no antibacterial activity against Staphylococcus aureus |
|
3.4.22.71 | galangin |
IC50 for recombinant SrtB(DELTA30): 0.03837 mM, no antibacterial activity against Staphylococcus aureus |
|
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 |
|
3.4.22.71 | berberine chloride |
potential of this inhibitor for the treatment of Staphylococcus aureus infections |
|