SULT1B1 Inhibitors

SULT1B1 inhibitors predominantly function by binding to the active site of the SULT1B1 enzyme, thereby preventing its normal sulfation activity. Compounds like quercetin, a naturally occurring flavonoid, can compete with substrates at the binding site of various sulfotransferases, including SULT1B1. Likewise, the NSAIDs, including mefenamic acid, naproxen, and indomethacin, have shown inhibitory tendencies toward some sulfotransferase enzymes. They function by mimicking the substrate and thus occupying the enzyme's active site.

Furthermore, compounds such as salicylic acid and bisphenol A can interfere with sulfation processes, thereby influencing SULT1B1 activity. Natural compounds like naringenin and endogenous compounds like DHEA (dehydroepiandrosterone) showcase their inhibitory effects through competitive binding to the active sites of certain SULTs. Other notable inhibitors include tamoxifen and daunorubicin, which, while not primary inhibitors of SULTs, can exhibit inhibitory effects on certain sulfotransferase members. Estradiol, an endogenous steroid hormone, can also hinder certain SULTs by competing for the active site.