Analysis of carotenoid isomerase activity in a prototypical carotenoid cleavage enzyme, apocarotenoid oxygenase (ACO)

28Citations
Citations of this article
52Readers
Mendeley users who have this article in their library.

This article is free to access.

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.

Cite

CITATION STYLE

APA

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

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free