Cyp2c55 Inhibitors

Chemical inhibitors of Cyp2c55 utilize various mechanisms to impede the function of the enzyme. Miconazole, ketoconazole, clotrimazole, and fluconazole are antifungal azoles that inhibit the enzyme by binding to the heme iron within its active site. This key interaction hinders the enzyme's capacity to metabolize its substrates, effectively interrupting its normal biological functions. Similarly, sulfaphenazole acts as a selective competitive inhibitor, occupying the active site and thus blocking the access of substrates. This competitive binding directly prevents the enzyme from processing other molecules it would typically metabolize.

Ticlopidine metabolizes into intermediates that covalently bind to Cyp2c55, leading to irreversible inhibition and a lasting reduction in enzyme activity. Phenylbutazone follows a competitive route of inhibition, taking up space within the catalytic site and precluding the metabolism of other substrates. Alternatively, methoxsalen operates as a mechanism-based inhibitor, forming a covalent bond with the enzyme's active site, which results in permanent inhibition. Omeprazole also achieves irreversible binding but through a different intermediate, sulphenamide, which interacts with the enzyme's heme group. Chloramphenicol and isoniazid inhibit Cyp2c55 by binding to the enzyme's active site, obstructing its normal interactions with substrates. Lastly, 1-aminobenzotriazole serves as a nonspecific inhibitor, covalently attaching to the heme iron of Cyp2c55, leading to an irreversible cessation of its enzymatic activity. Each chemical's interaction with Cyp2c55 ultimately disrupts the enzyme's metabolic role within the biological system.