Formation of plant cuticle: evidence for the occurrence of the peroxygenase pathway

Plant J. 2003 Oct;36(2):155-64. doi: 10.1046/j.1365-313x.2003.01865.x.


Cuticle plays a major role as a protective barrier in plants. Despite its physiological importance, the mode of formation of this complex structure remains poorly understood. In particular, none of the putative enzymes involved in the biosynthesis of the cutin, the matrix of cuticle, have been cloned. We have shown previously that peroxygenase is able to catalyze in vitro the epoxidation step required for the biosynthesis of C18 cutin monomers. In the present work, we have confirmed in planta that this oxidase is indeed a key enzyme involved in the formation of cutin. Thus, in maize leaves, the specific inactivation of peroxygenase by organophosphorothioates resulted in a dramatic decrease of cuticular epoxide content, as visualized by a specific histochemical technique that was accompanied by a reduced thickness of the cuticle. A strict correlation could also be established between the extent of inhibition of the peroxygenase and the modification of the cuticle triggered by a family of structurally related inhibitors. Importantly, these effects were restricted to plants that contain a cutin originating from C18 monomers. The altered cuticle of maize, treated with the peroxygenase inhibitor, was characterized by an increased permeability to pesticides. In addition, such plants became largely susceptible to infection by fungi, implying that the cuticle represents a crucial target for the modulation of the response in plant-pathogen interactions.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Herbicides / pharmacology
  • Kinetics
  • Membrane Lipids / biosynthesis
  • Mixed Function Oxygenases / drug effects
  • Mixed Function Oxygenases / metabolism*
  • Plant Leaves / enzymology
  • Plant Structures / enzymology
  • Soybeans / enzymology*
  • Zea mays / enzymology*


  • Herbicides
  • Membrane Lipids
  • cutin
  • Mixed Function Oxygenases
  • peroxygenase