Carotenoids and their cleavage products: biosynthesis and functions

Nat Prod Rep. 2011 Apr;28(4):663-92. doi: 10.1039/c0np00036a. Epub 2011 Feb 14.


This review focuses on plant carotenoids, but it also includes progress made on microbial and animal carotenoid metabolism to better understand the functions and the evolution of these structurally diverse compounds with a common backbone. Plants have evolved isogenes for specific key steps of carotenoid biosynthesis with differential expression profiles, whose characteristic features will be compared. Perhaps the most exciting progress has been made in studies of carotenoid cleavage products (apocarotenoids) with an ever-expanding variety of novel functions being discovered. This review therefore covers structural, molecular genetic and functional aspects of carotenoids and apocarotenoids alike. Apocarotenoids are specifically tailored from carotenoids by a family of oxidative cleavage enzymes, but whether there are contributions to their generation from chemical oxidation, photooxidation or other mechanisms is largely unknown. Control of carotenoid homeostasis is discussed in the context of biosynthetic and degradative reactions but also in the context of subcellular environments for deposition and sequestration within and outside of plastids. Other aspects of carotenoid research, including metabolic engineering and synthetic biology approaches, will only be covered briefly.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Bacteria / chemistry
  • Carotenoids* / biosynthesis
  • Carotenoids* / chemistry
  • Carotenoids* / genetics
  • Carotenoids* / metabolism
  • Daucus carota / chemistry
  • Daucus carota / metabolism
  • Fungi / chemistry
  • Geranylgeranyl-Diphosphate Geranylgeranyltransferase / genetics
  • Geranylgeranyl-Diphosphate Geranylgeranyltransferase / metabolism*
  • Molecular Structure
  • Plants* / chemistry
  • Plants* / enzymology
  • Plants* / genetics


  • Carotenoids
  • Geranylgeranyl-Diphosphate Geranylgeranyltransferase