SULT1C4 inhibitors are a class of chemical compounds that specifically target and inhibit the activity of the sulfotransferase enzyme SULT1C4. This enzyme is part of the larger sulfotransferase (SULT) family, which plays a critical role in the metabolism and detoxification of a variety of endogenous and exogenous compounds. SULT1C4 is primarily involved in the sulfation of small molecules, including hormones, xenobiotics, drugs, and other bioactive compounds. Sulfation, the process by which a sulfate group from the donor molecule 3'-phosphoadenosine-5'-phosphosulfate (PAPS) is transferred to hydroxyl or amine groups of substrates, enhances the solubility of these molecules, facilitating their metabolism and excretion. This biochemical process can also regulate the biological activity of substrates, making sulfation a key regulatory step in hormone action and detoxification pathways. Inhibitors of SULT1C4 disrupt this enzyme's ability to sulfate its substrates, leading to changes in their metabolic fate and biological activity.
The mechanism of action of SULT1C4 inhibitors typically involves competitive binding to the enzyme's active site, where they prevent either the substrate or the cofactor PAPS from engaging in the sulfation reaction. Some inhibitors may act by binding allosterically, causing conformational changes that reduce the enzyme's catalytic efficiency. By blocking SULT1C4, these inhibitors affect the enzyme's role in detoxification and the regulation of bioactive molecules, which can have downstream consequences on cellular metabolism and hormone regulation. Research into SULT1C4 inhibitors provides key insights into the specific substrates and physiological roles of this enzyme, furthering our understanding of how sulfotransferases contribute to maintaining cellular homeostasis. This class of inhibitors also highlights the broader importance of enzyme-mediated modifications in regulating molecular pathways, particularly those related to the metabolism of xenobiotics, hormones, and other essential compounds.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Pentachlorophenol | 87-86-5 | sc-257975 | 1 g | $32.00 | ||
Known to inhibit sulfotransferases and may bind to the active site of SULT1C4, preventing the transfer of sulfate groups. | ||||||
Quercetin | 117-39-5 | sc-206089 sc-206089A sc-206089E sc-206089C sc-206089D sc-206089B | 100 mg 500 mg 100 g 250 g 1 kg 25 g | $11.00 $17.00 $108.00 $245.00 $918.00 $49.00 | 33 | |
Flavonoid that can inhibit sulfotransferase activity by competing with the substrates for the active site of the enzyme. | ||||||
Chlorpyrifos | 2921-88-2 | sc-217887 | 250 mg | $92.00 | ||
Organophosphate that can inhibit sulfotransferase activity and may modify the conformation of SULT1C4, reducing its activity. | ||||||
Bisphenol A | 80-05-7 | sc-391751 sc-391751A | 100 mg 10 g | $300.00 $490.00 | 5 | |
Can interact with sulfotransferase enzymes and potentially inhibit SULT1C4 by binding to its active site. | ||||||
Triclosan | 3380-34-5 | sc-220326 sc-220326A | 10 g 100 g | $138.00 $400.00 | ||
Antimicrobial agent that can inhibit various sulfotransferases, possibly by binding directly to the active site of SULT1C4. | ||||||
Methotrexate | 59-05-2 | sc-3507 sc-3507A | 100 mg 500 mg | $92.00 $209.00 | 33 | |
Folate analog that can inhibit sulfotransferase activity, potentially through competition with the sulfate donor or substrates. | ||||||
Quinidine | 56-54-2 | sc-212614 | 10 g | $102.00 | 3 | |
Antiarrhythmic agent that can inhibit sulfotransferase enzymes, possibly by altering the enzyme's tertiary structure. | ||||||
Desipramine hydrochloride | 58-28-6 | sc-200158 sc-200158A | 100 mg 1 g | $65.00 $115.00 | 6 | |
Tricyclic antidepressant that can inhibit sulfotransferase activity, potentially by binding to the active site of SULT1C4. | ||||||
Dibenz[a,h]anthracene | 53-70-3 | sc-257317 | 100 mg | $250.00 | ||
Polycyclic aromatic hydrocarbon that may inhibit sulfotransferase activity by non-competitive inhibition or allosteric modification. | ||||||