Phytochemistry Reviews

, Volume 5, Issue 2–3, pp 359–372 | Cite as

Cytochrome P450-dependent fatty acid hydroxylases in plants

  • S. Kandel
  • V. Sauveplane
  • A. Olry
  • L. Diss
  • I. Benveniste
  • F. Pinot
Original paper


In plants, hydroxy-fatty acid production is mainly the result of enzymatic reactions catalyzed by cytochrome P450 dependent fatty acid hydroxylases. One can distinguish ω-hydroxylases that catalyze the hydroxylation of the terminal methyl of aliphatics acids (ω position) and sub-terminal or in-chain hydroxylases that oxidize carbons in the chain (ω-n position). Since both types of enzymes were discovered about three decades ago, the majority of investigations have focused on the CYP94 and CYP86 families, which mediate ω-hydroxylations. The activities of ω-hydroxylases in cutin synthesis have been clearly established, but the studies of LCR (LACERATA) and att1 (aberrant induction of type three genes), which are the first Arabidopsis thaliana mutants with alterations in coding sequences of CYP86A8 and CYP86A2, show that these types of ω-hydroxylases can be involved in many aspects of plant development. The existence of different ω-hydroxylases in plants with distinct regulation patterns suggests that these enzymes mediate diverse biological processes. Much less information concerning in-chain hydroxylases is available despite the fact that they were initially reported along with ω-hydroxylases. This lack of information might be explained by the very few examples of sub-terminal hydroxy-fatty acids described in plants. We present here the best characterized fatty acid hydroxylases and we discuss their possible roles in plant defense and development, fatty acid catabolism, plant reproduction and detoxification.


Cuticle Defense Lipid metabolism Oxidation Signal 



Kandel S. is grateful to the French Ministry of Research for supporting her PhD thesis.


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Copyright information

© Springer Science+Business Media B.V. 2006

Authors and Affiliations

  • S. Kandel
    • 1
  • V. Sauveplane
    • 1
  • A. Olry
    • 1
  • L. Diss
    • 1
  • I. Benveniste
    • 1
  • F. Pinot
    • 1
    • 2
  1. 1.IBMP-CNRS UPR 2357 Département Réponse Métabolique à l’Environment BiotiqueStrasbourg CedexFrance
  2. 2.IBMP, Université Louis Pasteur - CNRS UPR 2357, Institut de BotaniqueStrasbourg CedexFrance

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