CDO Inhibitors
Cysteine dioxygenase (CDO) is a critical enzyme in the metabolism of cysteine, catalyzing the conversion of cysteine to cysteine sulfinic acid, a precursor for taurine, sulfate, and pyruvate production. This biochemical pathway is essential for maintaining sulfur amino acid homeostasis in the body, playing a pivotal role in detoxifying excess cysteine and preventing its harmful accumulation. CDO's activity is tightly regulated within the cell, reflecting its importance in controlling the levels of cysteine and preventing the adverse effects of its excess, such as oxidative stress and cellular damage. The enzyme's function is integral to the synthesis of vital compounds and the regulation of antioxidative responses, thereby contributing to overall metabolic balance and cellular health.
The inhibition of CDO can occur through various mechanisms, primarily involving interactions that reduce its catalytic activity or affect its expression levels. Inhibition at the enzymatic level can result from the binding of specific molecules to the active site, altering the enzyme's structure and thereby decreasing its affinity for cysteine. This can lead to elevated cysteine levels in cells and tissues, with implications for metabolic regulation and oxidative stress responses. Additionally, the regulation of CDO expression can be influenced by dietary components, cellular redox status, and hormonal signals, which may downregulate the enzyme's synthesis, contributing to a decrease in its activity. Understanding the intricate mechanisms governing CDO inhibition is crucial for elucidating the complex network of sulfur amino acid metabolism and its impact on cellular and systemic health. The precise control of CDO activity highlights the sophisticated balance required to maintain amino acid levels within physiological ranges, ensuring efficient metabolism and protection against cellular damage.
| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Acivicin | 42228-92-2 | sc-200498B sc-200498C sc-200498 sc-200498D | 1 mg 5 mg 10 mg 25 mg | $102.00 $408.00 $642.00 $1275.00 | 10 | |
Acivicin is a glutamine analogue and a potential inhibitor of CDO. It interferes with glutamine metabolism, leading to decreased availability of glutamine, which is a substrate for CDO. This disruption in glutamine metabolism can indirectly influence CDO activity, potentially inhibiting the conversion of cysteine to cysteine sulfinic acid. | ||||||
DL-Propargylglycine | 64165-64-6 | sc-294408 sc-294408A | 1 g 5 g | $169.00 $678.00 | ||
DL-Propargylglycine is a known inhibitor of cystathionine gamma-lyase (CSE) and can also potentially inhibit CDO. It interferes with the transsulfuration pathway, limiting the availability of cysteine. By affecting the precursor availability, DL-Propargylglycine may indirectly modulate CDO activity, leading to a reduction in cysteine dioxygenase function. | ||||||
Penicillamine | 52-67-5 | sc-205795 sc-205795A | 1 g 5 g | $45.00 $94.00 | ||
Penicillamine is a thiol compound and a potential inhibitor of CDO. It can form a complex with copper, reducing the bioavailability of copper, which is a cofactor for CDO. By interfering with the copper-dependent activity of CDO, D-Penicillamine may indirectly modulate the enzymatic function, leading to a reduction in the conversion of cysteine to cysteine sulfinic acid. | ||||||
D-Limonene | 5989-27-5 | sc-205283 sc-205283A | 100 ml 500 ml | $82.00 $126.00 | 3 | |
D-Limonene is a potential inhibitor of CDO. It can modulate the levels of oxidative stress, and its inhibitory effect on CDO may be associated with alterations in redox status. While the exact mechanism is not fully elucidated, D-Limonene's impact on oxidative stress pathways can potentially lead to the inhibition of CDO, influencing the conversion of cysteine to cysteine sulfinic acid. | ||||||
Thioacetamide | 62-55-5 | sc-213031 | 25 g | $53.00 | ||
Thioacetamide is a potential inhibitor of CDO. It is a thiol-containing compound and can interact with the active site of CDO, potentially inhibiting its enzymatic activity. By forming complexes with the active site, thioacetamide may directly modulate CDO, leading to a decrease in the conversion of cysteine to cysteine sulfinic acid. | ||||||
L-Methionine | 63-68-3 | sc-394076 sc-394076A sc-394076B sc-394076C sc-394076D sc-394076E | 25 g 100 g 250 g 1 kg 5 kg 10 kg | $33.00 $36.00 $56.00 $148.00 $566.00 $1081.00 | ||
Methionine is a potential inhibitor of CDO. As an amino acid, methionine competes with cysteine for uptake and utilization. By limiting the availability of cysteine, methionine can indirectly modulate CDO activity, leading to a reduction in the conversion of cysteine to cysteine sulfinic acid. | ||||||
N-Acetyl-L-cysteine | 616-91-1 | sc-202232 sc-202232A sc-202232C sc-202232B | 5 g 25 g 1 kg 100 g | $33.00 $73.00 $265.00 $112.00 | 34 | |
N-Acetylcysteine (NAC) is a potential inhibitor of CDO. It is a precursor to cysteine and can influence the cellular cysteine pool. By providing an alternative source of cysteine, NAC may compete with endogenous cysteine for binding to CDO. This competitive inhibition can potentially modulate CDO activity, leading to a decrease in the conversion of cysteine to cysteine sulfinic acid. | ||||||