ArticleMolecular pharmacology2026
Mechanism-based inactivation of human aldehyde oxidase by erlotinib: Mechanistic insights from structural analogs and molecular docking.
Article in Molecular pharmacology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Aldehyde oxidase (AOX1) is a cytosolic molybdo-flavoenzyme that metabolizes azaheterocyclic drugs. Erlotinib and gefitinib are azaheterocyclic drugs. We deployed structural analogs to investigate the molecular interaction between these drugs and AOX1. Erlotinib, O-desmethylerlotinib, and O-didesmethylerlotinib, but not gefitinib, O-desmethylgefitinib, or O-desmorpholinopropylgefitinib, decreased carbazeran 4-oxidation by liver cytosol (human, rat, and mouse) and human recombinant AOX1. Erlotinib, O-desmethylerlotinib, and O-didesmethylerlotinib exhibited time- and concentration-dependent inactivation with unbound inactivation potency (K
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