New pathway to polyketides in plants

Stefan Eckermann, Gudrun Schröder, Jürgen Schmidt, Dieter Strack, Ru A. Edrada, Yrjö Helariutta, Paula Elomaa, Mika Kotilainen, Ilkka Kilpeläinen, Peter Proksch, Teemu H. Teeri and Joachim Schröder ()
Additional contact information
Stefan Eckermann: Institut für Biologie II, Universität Freiburg
Gudrun Schröder: Institut für Biologie II, Universität Freiburg
Jürgen Schmidt: Institut für Pflanzenbiochemie
Dieter Strack: Institut für Pflanzenbiochemie
Ru A. Edrada: Lehrstuhl für Pharmazeutische Biologie
Yrjö Helariutta: Institute of Biotechnology, Viikki Biocenter, University of Helsinki
Paula Elomaa: Institute of Biotechnology, Viikki Biocenter, University of Helsinki
Mika Kotilainen: Institute of Biotechnology, Viikki Biocenter, University of Helsinki
Ilkka Kilpeläinen: Institute of Biotechnology, Viikki Biocenter, University of Helsinki
Peter Proksch: Lehrstuhl für Pharmazeutische Biologie
Teemu H. Teeri: Institute of Biotechnology, Viikki Biocenter, University of Helsinki
Joachim Schröder: Institut für Biologie II, Universität Freiburg

Nature, 1998, vol. 396, issue 6709, 387-390

Abstract: Abstract The repertoire of secondary metabolism (involving the production of compounds not essential for growth) in the plant kingdom is enormous, but the genetic and functional basis for this diversity is hard to analyse as many of the biosynthetic enzymes are unknown. We have now identified a key enzyme in the ornamental plant Gerbera hybrida (Asteraceae) that participates in the biosynthesis of compounds that contribute to insect and pathogen resistance. Plants transformed with an antisense construct of gchs2, a complementary DNA encoding a previously unknown function1,2, completely lack the pyrone derivatives gerberin and parasorboside. The recombinant plant protein catalyses the principal reaction in the biosynthesis of these derivatives: GCHS2 is a polyketide synthase that uses acetyl-CoA and two condensation reactions with malonyl-CoA to form the pyrone backbone of thenatural products. The enzyme also accepts benzoyl-CoA to synthesize the backbone of substances that have become of interest as inhibitors of the HIV-1 protease3,4,5. GCHS2 is related to chalcone synthase (CHS) and its properties define a new class of function in the protein superfamily. It appears that CHS-related enzymes are involved in the biosynthesis of a much larger range of plant products than was previously realized.

Date: 1998
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DOI: 10.1038/24652

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