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Beta-carotene 15,15'-dioxygenase 1 (BCO1) is an enzyme that catalyzes the symmetric, dioxygenase-mediated cleavage of dietary beta-carotene at the central 15,15’-double bond, yielding two molecules of retinal (vitamin A aldehyde). BCO1 is encoded by the BCO1 gene in humans. The primary biological role of BCO1 is to initiate the metabolic conversion of provitamin A carotenoids to vitamin A, which is essential for vision, embryogenesis, cell differentiation, and skin and mucous membrane health. BCO1 activity directly regulates vitamin A homeostasis; its dysregulation or genetic variation may contribute to disorders of vitamin A deficiency or toxicity. Recent evidence suggests a role for BCO1 in modulating cancer cell stemness and metastasis, notably in neuroblastoma, potentially through interaction with cell differentiation pathways and microRNA regulation.
Enzymatic centric cleavage of beta-carotene to retinal, a precursor of vitamin A
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