SULT1C3 Inhibitors

SULT1C3 Inhibitors target pathways and enzymes that can indirectly influence the functional context of SULT1C3. Given SULT1C3's role in sulfation processes, modulation of sulfotransferase activity or alterations in the metabolism of its substrates could impact its enzymatic function. Compounds like Pentachlorophenol, Quercetin, and Triclosan are known to inhibit sulfotransferase activities, which could reduce the sulfation capacity of enzymes like SULT1C3. Flavonoids and polyphenols such as Chlorogenic Acid, Curcumin, Chrysin, Daidzein, and Resveratrol have been shown to modulate various sulfotransferase enzymes, influencing SULT1C3's function in the metabolism of hormones, neurotransmitters, and xenobiotics.

Phenobarbital's induction of metabolizing enzymes and Methimazole's inhibitory effects on sulfotransferases could indirectly affect the activity of SULT1C3 by altering the availability of substrates or co-factors. Inhibitors of PAPS synthase, critical for providing the sulfonate donor in sulfation reactions, could also impact SULT1C3's activity by limiting the availability of this essential co-factor. Silymarin group, mixture of isomers, known for its liver-protective properties, and compounds affecting liver enzyme activities, might also have indirect implications for SULT1C3 function. These compounds, while not directly targeting SULT1C3, are important for understanding the complex processes of sulfation, metabolism, and detoxification in which SULT1C3 is involved. They offer valuable tools for research into the roles of sulfotransferase enzymes in physiological and pathological processes, including metabolism, hormone regulation, and the detoxification of xenobiotics.