Beta-carotene 15,15'-oxygenase 1 (BCO1)

Beta-carotene 15,15'-oxygenase 1 (BCO1) is a critical enzyme responsible for the first step of Vitamin A (retinol) biosynthesis from dietary provitamin A carotenoids (UniProt Q9HAY2). It specifically catalyzes the symmetrical oxidative cleavage of beta-carotene into two molecules of retinal, which are subsequently converted to retinol or retinoic acid (NCBI Gene 53630). This enzyme is primarily expressed in the intestinal epithelium and the liver, serving as a gatekeeper for systemic Vitamin A levels. Genetic variations in the BCO1 gene, such as the rs12934922 polymorphism, are known to significantly affect an individual's ability to convert carotenoids, leading to conditions such as hypercarotenemia or subclinical Vitamin A deficiency (PubMed 19103647). Beyond nutrition, BCO1 is investigated for its role in ocular health, particularly in age-related macular degeneration, and its potential influence on lipid metabolism and cardiovascular health (PubMed 24659105). While few drugs currently target BCO1 directly, it remains a key focus for personalized nutrition and the development of therapies aimed at modulating retinoid signaling pathways.

Other names

Beta-carotene monooxygenase 1BCMO1BCDO1Carotene dioxygenase 1Beta-carotene 15,15'-monooxygenase

BCO1 catalyzes the symmetrical oxidative cleavage of the central 15,15' double bond of beta-carotene, utilizing molecular oxygen to produce two molecules of all-trans-retinal.