Dual oxidase 1 (DUOX1)

Dual oxidase 1 (DUOX1) is an NADPH oxidase family enzyme that catalyzes the generation of hydrogen peroxide (H₂O₂), primarily at the apical surface of epithelial cells in tissues including the thyroid gland and respiratory tract[1][2][3]. DUOX1 plays a fundamental role in the biosynthesis of thyroid hormones—by providing H₂O₂ as an electron acceptor for thyroid peroxidase—and is also involved in innate immune responses via regulated production of reactive oxygen species for defense against pathogens[1][2][3]. It forms an essential heterocomplex with DUOXA1, a maturation factor that is crucial for proper folding, cellular trafficking, and enzymatic activation. DUOX1 activity is dependent on intracellular calcium ions (via EF-hand domains), and is subject to regulation by post-translational modifications. Structural studies have revealed that DUOX1 functions as part of multi-subunit assemblies that switch between active and inactive (e.g., dimer-of-dimers) conformations, with the active form enabling electron transfer and H₂O₂ production[1][2]. Overactivity or dysregulation of DUOX1 can contribute to oxidative stress-related tissue damage, inflammation, and has been linked to several diseases, especially those of the thyroid and respiratory tract[1][2]. No approved therapeutic drugs selectively target DUOX1, but its roles make it a candidate target for new therapies in inflammatory and thyroid-related disorders.

Other names

Dual oxidase 1DUOX1DUOXLNOX1THOX1NOXEF1Large NOX 1Long NOX 1NADPH thyroid oxidase 1Thyroid oxidase 1flavoprotein NADPH oxidasenicotinamide adenine dinucleotide phosphate oxidase

Enzymatic inhibition of hydrogen peroxide generation (theoretical/experimental; no approved drugs)