CBR4 inhibitors are a class of chemical compounds designed to selectively target and inhibit the activity of Carbonyl Reductase 4 (CBR4), a member of the short-chain dehydrogenase/reductase family of enzymes. These enzymes are involved in the metabolism of a wide range of biologically active and endogenous compounds, including steroid hormones, retinoids, and prostaglandins. CBR4 specifically plays a role in the reduction of carbonyl groups to their corresponding alcohols, an important step in cellular metabolism that affects various metabolic pathways. Inhibitors of CBR4 are meticulously structured to bind to the active site of the enzyme, thereby obstructing its catalytic function. The inhibition process typically involves the formation of a stable complex between the inhibitor and the CBR4 enzyme, which prevents the enzyme from interacting with its natural substrates. The design of CBR4 inhibitors is often guided by the detailed understanding of the enzyme's structure, substrate specificity, and kinetics, allowing for the development of inhibitors that are both potent and selective.
The specificity of CBR4 inhibitors is critical, as off-target effects are minimized, ensuring that the inhibition is confined to the intended enzyme without affecting other members of the reductase family. This specificity is achieved through the unique interaction between the inhibitor and the amino acids within the active site of CBR4, which may involve hydrogen bonding, hydrophobic interactions, and van der Waals forces. The inhibitors often possess functional groups that mimic the natural substrates of the enzyme or transition-state analogs that provide an enhanced affinity for the active site. This targeted inhibition of CBR4 affects the enzyme's role in cellular redox reactions and the metabolism of certain molecules which rely on the reduction of carbonyl groups. By doing so, CBR4 inhibitors can influence the cellular concentrations of specific metabolites, which in turn may affect various biological processes where these metabolites are involved. Although the development and study of these inhibitors are complex and require sophisticated techniques such as X-ray crystallography, computational modeling, and kinetic analysis, the detailed understanding of the CBR4 enzyme's structure and function facilitates the rational design of these inhibitors.
Items 1 to 10 of 11 total
Display:
Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
---|---|---|---|---|---|---|
N-Ethylmaleimide | 128-53-0 | sc-202719A sc-202719 sc-202719B sc-202719C sc-202719D | 1 g 5 g 25 g 100 g 250 g | $22.00 $68.00 $210.00 $780.00 $1880.00 | 19 | |
N-Ethylmaleimide is an organic compound that can modify cysteine residues in proteins, thereby affecting their function. For CBR4, which may rely on the structural integrity of its cysteine residues for activity, alkylation by N-Ethylmaleimide could lead to a functional inhibition of the protein. | ||||||
α-Iodoacetamide | 144-48-9 | sc-203320 | 25 g | $250.00 | 1 | |
Iodoacetamide is an alkylating agent known to modify cysteine residues. In the context of CBR4, alkylation of critical cysteine residues could inhibit its enzymatic activity by preventing the formation of its active site or disrupting its catalytic mechanism. | ||||||
Ellagic Acid, Dihydrate | 476-66-4 | sc-202598 sc-202598A sc-202598B sc-202598C | 500 mg 5 g 25 g 100 g | $57.00 $93.00 $240.00 $713.00 | 8 | |
Ellagic acid is a natural phenol antioxidant found in various fruits and vegetables. It has been shown to inhibit reductase enzymes by binding to the enzyme's active site. CBR4's reductase activity could be directly inhibited by ellagic acid, resulting in decreased functional activity. | ||||||
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 | |
Quercetin is a flavonoid that exhibits antioxidant properties and acts as an inhibitor of reductase enzymes. It could bind to the active site of CBR4 and interfere with its catalytic process, leading to inhibition of its function. | ||||||
Vitamin K3 | 58-27-5 | sc-205990B sc-205990 sc-205990A sc-205990C sc-205990D | 5 g 10 g 25 g 100 g 500 g | $25.00 $35.00 $46.00 $133.00 $446.00 | 3 | |
Menadione is a synthetic chemical compound with quinone structure, which is known to act as an oxidizing agent. It could potentially oxidize critical thiol groups in CBR4, disrupting its normal reductase activity and leading to functional inhibition. | ||||||
Curcumin | 458-37-7 | sc-200509 sc-200509A sc-200509B sc-200509C sc-200509D sc-200509F sc-200509E | 1 g 5 g 25 g 100 g 250 g 1 kg 2.5 kg | $36.00 $68.00 $107.00 $214.00 $234.00 $862.00 $1968.00 | 47 | |
Curcumin, a bioactive compound in turmeric, has been shown to inhibit various enzymes involved in the redox cycle. Its interaction with CBR4 could inhibit the protein's reductase activity by altering its active site or redox status. | ||||||
Phenylarsine oxide | 637-03-6 | sc-3521 | 250 mg | $40.00 | 4 | |
Phenylarsine oxide is a trivalent arsenical compound known to bind vicinal dithiols and inhibit proteins relying on dithiol-dependent catalytic activities. By binding to such sites on CBR4, it could inhibit the protein's function. | ||||||
Auranofin | 34031-32-8 | sc-202476 sc-202476A sc-202476B | 25 mg 100 mg 2 g | $150.00 $210.00 $1899.00 | 39 | |
Auranofin is a gold-containing compound that inhibits thiol-dependent enzymes. It could bind irreversibly to thiol groups in CBR4, leading to a loss of its reductase activity and consequent inhibition. | ||||||
Bacitracin | 1405-87-4 | sc-252399 | 5 g | $87.00 | 1 | |
Bacitracin is a peptide antibiotic that can chelate metal ions. Should CBR4 require a metal cofactor for its activity, bacitracin could sequester the metal ion, thereby inhibiting the protein's function. | ||||||
Allopurinol | 315-30-0 | sc-207272 | 25 g | $128.00 | ||
Allopurinol is a structural analog of hypoxanthine. It acts as an inhibitor of xanthine oxidase, and by analogy, could competitively inhibit CBR4 if it shares similar substrate specificity, leading to a decrease in its activity. |