SULT1C1 Inhibitors

Chemical inhibitors of SULT1C1 include a variety of compounds that interfere with its sulfotransferase function. Triclosan, for instance, binds to the sulfotransferase domain of SULT1C1, effectively blocking the enzyme's ability to transfer sulfo groups to its substrates. Similarly, pentachlorophenol operates as a competitive inhibitor, occupying the active site of SULT1C1 and obstructing the sulfonation of the enzyme's natural substrates. This type of inhibition ensures that SULT1C1 is unable to interact with its intended molecules for the transfer of sulfo groups. 2,6-Dichloro-4-nitrophenol also exerts its inhibitory effect by competing with substrates for the active site, while Bisphenol A binds to the catalytic site, thereby disrupting the normal sulfonation process. The flavonoid quercetin inhibits SULT1C1 by similarly binding to its active site and interfering with the enzyme's sulfo group transfer activity.

Further inhibitory actions are seen with dibutyl phthalate, which interacts with the substrate-binding region of SULT1C1, potentially reducing its sulfotransferase function. Resveratrol and curcumin both inhibit SULT1C1 by occupying its active site, necessary for substrate sulfonation, thus preventing the enzyme from performing its role. Additionally, 3,3'-Diindolylmethane alters the enzyme's structure allosterically, reducing its activity, and kaempferol binds to the active site, blocking access for substrates. Chrysin competes with natural substrates for the catalytic site of SULT1C1, leading to a decrease in sulfotransferase activity. Lastly, genistein binds directly to SULT1C1, obstructing the site where the sulfo group transfer to substrates would normally occur, thus effectively inhibiting the enzyme's function. Each of these chemicals employs a distinct mechanism to inhibit the activity of SULT1C1, yet all achieve the common result of impeding the enzyme's ability to catalyze the transfer of sulfo groups to its substrates.