Chemical inhibitors of Selenoprotein R target the protein's active site or its essential cofactors, thereby impeding its biological function. Methimazole acts by reducing the overall oxidative stress within the cell through the inhibition of thyroid hormone synthesis, leading to a decreased necessity for the methionine-R-sulfoxide reductase activity of Selenoprotein R. Methylmercury(II) chloride and Thimerosal, by binding to thiol groups in proteins, alter the structure and function of enzymes like Selenoprotein R that rely on thiol groups for their catalytic activity. Cadmium chloride and Lead(II) acetate disrupt metal ion homeostasis, which is essential for Selenoprotein R's function, by either outcompeting necessary cofactors or by directly interfering with the protein's metal-binding sites.
Arsenic trioxide and Disulfiram target the vicinal thiols in Selenoprotein R, forming stable complexes or binding to crucial cysteine residues, which obstructs the thiol-disulfide exchange mechanism central to Selenoprotein R's activity. Auranofin inhibits Selenoprotein R by covalently modifying or binding to its cysteine residues. Chloroquine, by increasing endosomal pH and inhibiting lysosomal degradation, can cause an accumulation of oxidized proteins, adding to the substrate load for Selenoprotein R and hampering its function due to substrate excess. Primaquine generates reactive oxygen species, leading to an increased oxidative burden that can overwhelm the protein. Sodium selenite at high concentrations inhibits selenoproteins, including Selenoprotein R, by inducing oxidative stress or by being inappropriately incorporated into the protein, which ultimately impairs the protein's antioxidant capability and inhibits its function.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Methimazole | 60-56-0 | sc-205747 sc-205747A | 10 g 25 g | $70.00 $112.00 | 4 | |
Methimazole inhibits the enzyme thyroid peroxidase, which is essential for the biosynthesis of thyroid hormones. Selenoprotein R is involved in reducing methionine-R-sulfoxide back to methionine, an action requiring a reducing environment that is maintained by cellular redox homeostasis. Lowered thyroid hormone production reduces metabolic rate and oxidative stress, which can diminish the requirement for Selenoprotein R activity, leading to its functional inhibition. | ||||||
Cadmium chloride, anhydrous | 10108-64-2 | sc-252533 sc-252533A sc-252533B | 10 g 50 g 500 g | $56.00 $183.00 $352.00 | 1 | |
Cadmium chloride disrupts essential metal ion homeostasis in the cell. Selenoprotein R requires specific metal cofactors for proper function and the disruption of metal ion homeostasis by cadmium can inhibit its activity by outcompeting necessary cofactors or directly binding to the active site. | ||||||
Lead(II) Acetate | 301-04-2 | sc-507473 | 5 g | $85.00 | ||
Lead(II) acetate can competitively inhibit enzymes by displacing essential metal ions from their active sites. Since Selenoprotein R's enzymatic activity depends on metal ion cofactors, lead's action can inhibit the proper function of the enzyme. | ||||||
Arsenic(III) oxide | 1327-53-3 | sc-210837 sc-210837A | 250 g 1 kg | $89.00 $228.00 | ||
Arsenic trioxide interacts with vicinal thiols in proteins to form stable ring structures, inhibiting enzymes that rely on thiol-based mechanisms. Selenoprotein R, which uses a thiol-based mechanism for its catalytic action, can be inhibited by the binding of arsenic to its active site. | ||||||
Auranofin | 34031-32-8 | sc-202476 sc-202476A sc-202476B | 25 mg 100 mg 2 g | $153.00 $214.00 $4000.00 | 39 | |
Auranofin inhibits thiol-dependent antioxidant enzymes. It can inhibit Selenoprotein R by binding to its thiol groups, thus preventing the thiol-disulfide exchange that is central to its enzymatic mechanism. | ||||||
Chloroquine | 54-05-7 | sc-507304 | 250 mg | $69.00 | 2 | |
Chloroquine raises endosomal pH and can inhibit lysosomal degradation. By inhibiting the degradation pathways, it may lead to an accumulation of oxidized proteins, which increases the substrate load for Selenoprotein R, potentially overwhelming its activity and causing functional inhibition due to excess substrate. | ||||||
8-(4-Amino-1-methylbutylamino)-6-methoxyquinoline | 90-34-6 | sc-483239 | 1 g | $360.00 | 1 | |
Primaquine generates reactive oxygen species in its action as an antimalarial. This can lead to oxidative stress, which may overwhelm the antioxidant capacity of Selenoprotein R, leading to its inhibition due to excessive oxidative substrate accumulation. | ||||||
Sodium selenite | 10102-18-8 | sc-253595 sc-253595B sc-253595C sc-253595A | 5 g 500 g 1 kg 100 g | $49.00 $183.00 $316.00 $98.00 | 3 | |
Sodium selenite at high concentrations can be toxic and result in the non-specific inhibition of many selenoproteins, including Selenoprotein R, by incorporating inappropriately into proteins or by inducing oxidative stress that overwhelms the protein's antioxidant capability. | ||||||
Disulfiram | 97-77-8 | sc-205654 sc-205654A | 50 g 100 g | $53.00 $89.00 | 7 | |
Disulfiram inhibits aldehyde dehydrogenase and can bind to sulfhydryl groups in proteins, thus it can inhibit Selenoprotein R by binding to crucial cysteine residues required for its activity, preventing its normal function. | ||||||