Date published: 2025-9-22

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CYP4A31 Inhibitors

CYP4A31 inhibitors are a class of chemical compounds that specifically target and inhibit the activity of the cytochrome P450 4A31 (CYP4A31) enzyme. The CYP4A31 enzyme is part of the larger cytochrome P450 family, which is a group of heme-thiolate monooxygenases involved in the oxidative metabolism of various endogenous and exogenous substrates. The CYP4A subfamily, in particular, is primarily known for its role in the ω-hydroxylation of fatty acids, especially those of medium to long-chain lengths. These fatty acids can include various forms of arachidonic acid and other biologically significant molecules. By inhibiting CYP4A31, these compounds can interfere with the enzyme's ability to catalyze these hydroxylation reactions, leading to a cascade of metabolic alterations within cellular processes, particularly those associated with lipid metabolism. The specificity of CYP4A31 inhibitors lies in their structural compatibility with the active site of the enzyme, allowing them to effectively block the binding and subsequent metabolism of natural substrates. This inhibition is typically achieved through either reversible or irreversible binding mechanisms, depending on the nature of the inhibitor. Reversible inhibitors may form transient complexes with the enzyme, often through non-covalent interactions such as hydrogen bonding, van der Waals forces, or electrostatic interactions. In contrast, irreversible inhibitors form covalent bonds with key residues in the enzyme's active site, permanently inactivating the enzyme. The development and study of these inhibitors require a deep understanding of the enzyme's structure, substrate specificity, and the dynamics of enzyme-ligand interactions. Through detailed kinetic analyses and computational modeling, researchers can elucidate the precise mechanisms by which these inhibitors exert their effects, thereby contributing to the broader understanding of fatty acid metabolism and its regulatory pathways.

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