Cyp2c70 Inhibitors

Chemical inhibitors of Cyp2c70 employ various mechanisms to hinder the protein's enzymatic activity, which is pivotal in metabolizing a range of substrates. Miconazole, for instance, executes its inhibitory action by binding to the heme iron within Cyp2c70, obstructing the enzyme's ability to engage in its natural metabolic processes. A similar mode of inhibition is utilized by Ketoconazole, which disrupts the electron transfer mechanism essential for the catalytic activity of Cyp2c70. Fluconazole and Sertraline, engage in competitive inhibition, where they compete with natural substrates for the active site of Cyp2c70, thereby diminishing the enzyme's activity. This competitive inhibition is also the method by which Fluoxetine operates, binding to the active site and decreasing the metabolic activity of Cyp2c70.

Continuing with this theme, Sulconazole limits Cyp2c70's function by blocking substrate access to the enzyme's active site, effectively reducing the catalytic efficiency. Clotrimazole and Tioconazole share a similar inhibitory effect; they bind directly to the active site of Cyp2c70, preventing substrate modification and thereby inhibiting the enzyme's function. Econazole interacts with the heme group of Cyp2c70 which is vital for its metabolic function, leading to inhibition. Voriconazole impedes the catalytic capacity of Cyp2c70, hindering the enzyme's typical bioconversion reactions. Itraconazole also binds to the active site of the enzyme, which obstructs the substrate metabolism. Lastly, Paroxetine binds to the active site of Cyp2c70, leading to a reduction in the enzyme's capacity to process its substrates, which results in inhibition of the protein's enzymatic activity. Each inhibitor, though diverse in structure, converges on the common endpoint of diminishing the metabolic capabilities of Cyp2c70 through direct interaction with either the active site or necessary cofactors involved in the enzyme's function.