EC Number |
Inhibitors |
Structure |
---|
3.4.22.71 | (Z)-3-(2,5-dimethoxyphenyl)-2-(4-methoxyphenyl) acrylonitrile |
potential of this inhibitor for the treatment of Staphylococcus aureus infections |
|
3.4.22.71 | (Z)-3-(2,5-dimethoxyphenyl)-2-(4-methoxyphenyl) acrylonitrile |
50% inhibition with 0.0101 mg/ml |
|
3.4.22.71 | berberine chloride |
potential of this inhibitor for the treatment of Staphylococcus aureus infections |
|
3.4.22.71 | beta-sitosterol-3-O-glucopyranoside |
potential of this inhibitor for the treatment of Staphylococcus aureus infections |
|
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 | galangin |
IC50 for recombinant SrtB(DELTA30): 0.03837 mM, no antibacterial activity against Staphylococcus aureus |
|
3.4.22.71 | galangin-3-methyl ether |
IC50 for recombinant SrtB(DELTA30): 0.1136 mM, no antibacterial activity against Staphylococcus aureus |
|
3.4.22.71 | isorhamnetin |
IC50 for recombinant SrtB(DELTA30): 0.04335 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 | 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 |
|