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Structural and biological aspects of carotenoid cleavage

Structural and biological aspects of carotenoid cleavage 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Cellular and Molecular Life Sciences Springer Journals

Structural and biological aspects of carotenoid cleavage

Cellular and Molecular Life Sciences , Volume 63 (20) – Aug 11, 2006

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References (80)

Publisher
Springer Journals
Copyright
Copyright © 2006 by Birkhäuser Verlag, Basel
Subject
Life Sciences; Biomedicine general; Life Sciences, general; Biochemistry, general; Cell Biology
ISSN
1420-682X
eISSN
1420-9071
DOI
10.1007/s00018-006-6176-6
pmid
16909205
Publisher site
See Article on Publisher Site

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.

Journal

Cellular and Molecular Life SciencesSpringer Journals

Published: Aug 11, 2006

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