15-LO Inhibitors

Ebselen (CAS 60940-34-3) is an organoselenium compound with antioxidant attributes. It serves as an inhibitor of 15-Lipoxygenase (15-LO), an enzyme that metabolizes polyunsaturated fatty acids. Ebselen binds to the active site of 15-LO, disrupting its enzymatic function. This inhibition affects the generation of pro-inflammatory mediators and modifies various biochemical pathways. The compound primarily achieves this by covalently altering critical cysteine residues in the enzyme.

NDGA is known to inhibit the enzymatic activity of 15-LO. It interferes with the catalytic conversion of fatty acids, thereby reducing the formation of lipid mediators.

Luteolin blocks the catalytic site of 15-LO, inhibiting its ability to convert polyunsaturated fatty acids into bioactive lipid mediators.

ETYA acts as a potent inhibitor of 15-lipoxygenase, characterized by its unique ability to engage in specific molecular interactions that stabilize the enzyme's active site. The presence of its acyl chain promotes hydrophobic interactions, enhancing binding efficiency. This interaction alters the enzyme's kinetic parameters, leading to a significant reduction in product formation. Additionally, ETYA's structural features may influence substrate accessibility, further modulating enzymatic activity and metabolic pathways.

PD-146176 functions as a selective inhibitor of 15-lipoxygenase, exhibiting unique binding dynamics that disrupt the enzyme's catalytic mechanism. Its distinct structural motifs facilitate specific interactions with key amino acid residues, altering the enzyme's conformation. This results in modified reaction kinetics, characterized by a decrease in substrate turnover. Furthermore, PD-146176's hydrophobic regions may influence the enzyme's substrate affinity, impacting overall metabolic flux.

Baicalein is thought to block the active site of 15-LO, which inhibits its ability to catalyze the oxidation of fatty acids.

Curcumin is reported to downregulate the mRNA levels of 15-LO, thus affecting its overall expression and enzymatic activity.

ETI acts as a potent modulator of 15-lipoxygenase, showcasing unique molecular interactions that stabilize the enzyme's inactive form. Its specific binding sites induce conformational changes, effectively hindering substrate access. The compound's distinct electronic properties enhance its affinity for critical active site residues, leading to altered reaction kinetics. Additionally, ETI's steric bulk may influence enzyme-substrate complex formation, further impacting metabolic pathways.

2-TEDC serves as a selective inhibitor of 15-lipoxygenase, characterized by its ability to form stable complexes with the enzyme. This compound exhibits unique steric and electronic features that facilitate specific interactions with key amino acid residues, disrupting the enzyme's catalytic activity. Its presence alters the dynamics of substrate binding and promotes a shift in the enzyme's conformational landscape, ultimately affecting lipid metabolism and signaling pathways.

Quercetin competes for the active site of 15-LO and is thought to inhibit its enzymatic activity by reducing the availability of the substrate.