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Beta-carotene 15,15'-dioxygenase (BCO1/BCMO1) is a cytosolic enzyme that catalyzes the oxidative cleavage of beta-carotene and other provitamin A carotenoids into two molecules of all-trans-retinal, the direct precursor of vitamin A (retinaldehyde). This conversion is essential for maintenance of vision, cell differentiation, and skin integrity, as well as embryonic development and lipid metabolism. BCO1/BCMO1 exhibits substrate specificity for provitamin A carotenoids, and genetic variants can alter its activity and affect nutritional status. The enzyme is primarily located in the intestine but has tissue-specific roles throughout the body. It operates via a dioxygenase mechanism, not a monooxygenase, incorporating both oxygen atoms from molecular O~2~ into its product. Dysfunction of BCO1/BCMO1 or genetic variation can lead to health issues such as hypovitaminosis A or excessive beta-carotene accumulation
Catalytic cleavage of beta-carotene (and other provitamin A carotenoids) to produce two molecules of retinal via a dioxygenase mechanism
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