CYP2D10 Inhibitors

Chemical inhibitors of CYP2D10 include a variety of compounds that engage with the enzyme in a manner that impairs its normal function, which is to metabolize various substrates. Quinidine, for example, is a known competitive inhibitor that binds to the active site of CYP2D10, directly interfering with the enzyme's activity. This binding precludes the access of endogenous substrates to the active site, thus inhibiting their metabolism. Similarly, fluoxetine and paroxetine also act as competitive inhibitors; by occupying the active site of CYP2D10, they prevent the enzyme from engaging with its natural substrates, which effectively blocks the metabolic reaction that CYP2D10 would normally facilitate. Another compound, ajmalicine, employs a similar mechanism of inhibition, directly interacting with CYP2D10's active site to diminish its metabolic capacity.

Further expanding the list of inhibitors, amiodarone and haloperidol execute their inhibitory effects by directly binding to CYP2D10, which results in a reduction of the enzyme's capacity to metabolize its substrates. Ritonavir, diphenhydramine, and chlorpheniramine also inhibit CYP2D10 through direct binding, which leads to a decrease in the enzyme's metabolic activity. This direct interaction is a common theme among the diverse chemical inhibitors of CYP2D10, as seen with bupropion and sertraline, which are competitive inhibitors that occupy the active site of the enzyme, thereby inhibiting its function. Methadone rounds out this group of inhibitors, employing a similar mechanism to bind directly to CYP2D10's active site, leading to a decrease in the enzyme's ability to metabolize its substrates. Each of these chemicals acts as a direct inhibitor of CYP2D10 by engaging with the enzyme in a way that leads to a reduction or cessation of its normal metabolic function.