Abstract.
Apo-carotenoid compounds such as retinol (vitamin A) are involved in a variety of cellular processes and are found in all kingdoms of life. Instead of being synthesized from small precursors, they are commonly produced by oxidative cleavage and subsequent modification of larger carotenoid compounds. The cleavage reaction is catalyzed by a family of related enzymes, which convert specific substrate double bonds to the corresponding aldehydes or ketones. The individual family members differ in their substrate preference and the position of the cleaved double bond, giving rise to a remarkable number of products starting from a limited number of carotenoid substrate molecules. The recent determination of the structure of a member of this family has provided insight into the reaction mechanism, showing how substrate specificity is achieved. This review will focus on the biochemistry of carotenoid oxygenases and the structural determinants of the cleavage reaction.
Article PDF
Similar content being viewed by others
Avoid common mistakes on your manuscript.
Author information
Authors and Affiliations
Corresponding author
Additional information
Received 19 April 2006; received after revision 26 May 2006; accepted 15 June 2006
Rights and permissions
About this article
Cite this article
Kloer, D.P., Schulz, G.E. Structural and biological aspects of carotenoid cleavage. Cell. Mol. Life Sci. 63, 2291–2303 (2006). https://doi.org/10.1007/s00018-006-6176-6
Published:
Issue Date:
DOI: https://doi.org/10.1007/s00018-006-6176-6