Premium
Biosynthesis of cutin monomers: involvement of a lipoxygenase/peroxygenase pathway
Author(s) -
Blée Elizabeth,
Schuber Francis
Publication year - 1993
Publication title -
the plant journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.058
H-Index - 269
eISSN - 1365-313X
pISSN - 0960-7412
DOI - 10.1046/j.1365-313x.1993.04010113.x
Subject(s) - cutin , chemistry , biochemistry , biosynthesis , oleic acid , enzyme , lipoxygenase , fatty acid , epoxide hydrolase , monomer , stereochemistry , organic chemistry , microsome , polymer
Cutin is synthesized from oxygenated fatty acids derived preponderantly from oleic acid. The enzymatic pathways involved in the biosynthesis of such cutin monomers have been studied, i.e. 18‐hydroxyoleic acid, 9,10‐epoxy‐18‐hydroxystearic acid (the major constituent) and 9,10,18‐trihydroxystearic acid. This was approached by studying (i) the substrate specificity and stereoselectivity of purified peroxygenase, which epoxidizes unsaturated fatty acids, and fatty acid epoxide hydrolase, i.e. two enzyme activities that have been found recently in higher plants, and (ii) the transformation of oleic acid into cutin monomers by a cell free system, i.e. soybean microsomes. These two enzymes, along with a ω‐hydroxylating activity, can account for the biosynthesis of the oleic acid‐derived cutin monomers and their precursors. A new biosynthetic scheme is proposed, whose pathways take into account the dynamic aspects of the expression of the different enzyme activities involved. Importantly, since peroxygenase, for its activity, is strictly dependent on fatty acid hydroperoxides, which act as co‐substrates, the biosynthesis of cutin monomers is also dependent on the activity of lipoxygenases.