CYB561D1 Inhibitors
CYB561D1 inhibitors encompass a diverse range of chemical compounds that exert their inhibitory effects through various biochemical mechanisms, each impacting CYB561D1's functional activity. Plumbagin and Vitamin K3, both influencing redox cycling, diminish the electron donor capacity necessary for CYB561D1 activity, effectively reducing its function. Ellagic acid and Imatinib extend their inhibitory reach by targeting kinases that regulate redox-sensitive pathways, indirectly leading to a compromised redox state which is critical for CYB561D1's electron transfer. Similarly, Amiodarone and Ketoconazole's inhibition of cytochrome P450 enzymes restricts substrate availability for CYB561D1, thus indirectly lessening its electron transfer ability. Phenethyl isothiocyanate modifies redox-sensitive pathways, likely resulting in the limitation of electron availability for CYB561D1's catalytic cycle, indirectly impeding its operation.
The functional activity of CYB561D1 is further subdued by chemical compounds that indirectly affect the intracellular redox balance, which is vital for CYB561D1's role. Allopurinol's inhibition of xanthine oxidase and Methimazole's effect on thyroid peroxidase both lead to an altered redox state, potentially impairing CYB561D1's ability to facilitate electron transfer. Disulfiram's interaction with acetaldehyde metabolism leads to a change in NADH levels, consequently influencing CYB561D1's redox potential and diminishing its function. Cantharidin's inhibition of protein phosphatases disrupts multiple signaling pathways and, by extension, impacts CYB561D1 activity by altering the redox balance. Caprolactam's interaction with redox systems, although less characterized, is presumed to perturb the redox balance, thereby reducing CYB561D1's functional efficiency. Collectively, these inhibitors target the redox balance and electron transfer properties that are central to CYB561D1's function, resulting in the inhibition of its activity through a variety of indirect yet interconnected biochemical pathways.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Plumbagin | 481-42-5 | sc-253283 sc-253283A | 100 mg 250 mg | $52.00 $62.00 | 6 | |
Plumbagin, a naphthoquinone found in the roots of the plant Plumbago zeylanica, has been found to interact with redox cycling and inhibit electron transport chains. By altering the redox state, plumbagin diminishes the electron donor capacity necessary for CYB561D1 function, indirectly inhibiting its activity. | ||||||
Ellagic Acid, Dihydrate | 476-66-4 | sc-202598 sc-202598A sc-202598B sc-202598C | 500 mg 5 g 25 g 100 g | $58.00 $95.00 $245.00 $727.00 | 8 | |
Ellagic acid, a polyphenol found in various fruits and vegetables, inhibits the activity of dual-specificity tyrosine phosphorylation-regulated kinases (DYRKs). Since CYB561D1 has been associated with cellular redox homeostasis, the inhibition of these kinases can lead to disrupted redox balance, indirectly impairing CYB561D1's functional activity. | ||||||
Amiodarone | 1951-25-3 | sc-480089 | 5 g | $318.00 | ||
Amiodarone is a benzofuran-derived compound known to inhibit cytochrome P450 enzymes, which play a role in the endogenous synthesis of several redox-active molecules. The inhibition of these enzymes can reduce the substrate availability for CYB561D1, consequently diminishing its activity. | ||||||
Ketoconazole | 65277-42-1 | sc-200496 sc-200496A | 50 mg 500 mg | $63.00 $265.00 | 21 | |
Ketoconazole is known to inhibit cytochrome P450 enzymes, which are involved in oxidative reactions crucial for the proper functioning of redox-sensitive proteins like CYB561D1. By diminishing the activity of these enzymes, ketoconazole indirectly reduces CYB561D1's electron transfer capacity. | ||||||
Imatinib | 152459-95-5 | sc-267106 sc-267106A sc-267106B | 10 mg 100 mg 1 g | $26.00 $119.00 $213.00 | 27 | |
Imatinib, a tyrosine kinase inhibitor, impairs the phosphorylation of proteins involved in multiple signaling pathways. This impairment can indirectly lead to a reduced supply of electrons from the substrates of CYB561D1, as tyrosine phosphorylation is pivotal in many redox reactions where CYB561D1 might participate. | ||||||
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 | $26.00 $36.00 $47.00 $136.00 $455.00 | 3 | |
Vitamin K3 undergoes redox cycling and can deplete cellular antioxidants, leading to oxidative stress. This stress can alter the redox state that CYB561D1 relies on, thus indirectly inhibiting its activity by overwhelming its electron transfer capacity. | ||||||
Phenethyl isothiocyanate | 2257-09-2 | sc-205801 sc-205801A | 5 g 10 g | $104.00 $183.00 | 2 | |
Phenethyl isothiocyanate, a compound found in cruciferous vegetables, is known to modify redox-sensitive pathways. It can alter the intracellular redox state, leading to a potential decrease in the activity of redox-dependent proteins like CYB561D1 by limiting the availability of electrons for its catalytic cycle. | ||||||
Allopurinol | 315-30-0 | sc-207272 | 25 g | $131.00 | ||
Allopurinol, a xanthine oxidase inhibitor, reduces the production of uric acid, a process that involves electron transfer reactions. Allopurinol's action can lead to an altered redox state in the cell, indirectly diminishing the functional activity of redox-dependent proteins like CYB561D1 by disrupting their electron transfer processes. | ||||||
Disulfiram | 97-77-8 | sc-205654 sc-205654A | 50 g 100 g | $53.00 $89.00 | 7 | |
Disulfiram, an inhibitor of acetaldehyde dehydrogenase, interferes with the cellular redox state by blocking the oxidation of acetaldehyde, which can lead to increased NADH levels. This change can influence the redox potential required for CYB561D1 activity, thus indirectly inhibiting its function. | ||||||
Methimazole | 60-56-0 | sc-205747 sc-205747A | 10 g 25 g | $70.00 $112.00 | 4 | |
Methimazole works by inhibiting the enzyme thyroid peroxidase. This inhibition can lead to an altered intracellular redox state, which could potentially impact the functioning of redox-dependent proteins like CYB561D1, diminishing its activity. | ||||||