Abstract
Background: Isomerase activity for Synechocystis apocarotenoid oxygenase (ACO) has not been verified biochemically. Results: ACO exclusively produces all-trans-retinal from all-trans-apo-8β-cells-carotenol and is inhibited by linear polyoxyethylene detergents. Conclusion: ACO cleaves but does not isomerize all-trans-8β-cells-apocarotenol. Significance: This study clarifies the activity of and influence of detergent on ACO, a classical non-isomerizing member of the carotenoid cleavage enzyme family. © 2014 by The American Society for Biochemistry and Molecular Biology, Inc.
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CITATION STYLE
Sui, X., Kiser, P. D., Che, T., Carey, P. R., Golczak, M., Shi, W., … Palczewski, K. (2014). Analysis of carotenoid isomerase activity in a prototypical carotenoid cleavage enzyme, apocarotenoid oxygenase (ACO). Journal of Biological Chemistry, 289(18), 12286–12299. https://doi.org/10.1074/jbc.M114.552836
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