Substrate specificity of purified recombinant human β-carotene 15,15′-oxygenase (BCO1)

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Abstract

Background: The human enzyme β-carotene 15,15′-oxygenase (BCO1) produces vitamin A from carotenoids in food. Results: BCO1 catalyzes the oxidative cleavage of the 15-15′ double bond of major dietary provitamin A carotenoids, β-apocarotenals, and lycopene. Conclusion: BCO1 reacts only with carotenoids and apocarotenoids that yield retinal or acycloretinal. Significance: Elucidating the substrate specificity of BCO1 is crucial for understanding how humans metabolize carotenoids. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.

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Seña, C. D., Narayanasamy, S., Riedl, K. M., Curley, R. W., Schwartz, S. J., & Harrison, E. H. (2013). Substrate specificity of purified recombinant human β-carotene 15,15′-oxygenase (BCO1). Journal of Biological Chemistry, 288(52), 37094–37103. https://doi.org/10.1074/jbc.M113.507160

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