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Comparative evolutionary analysis of methylthioalkylmalate synthase genes and enzymes in the capparales

JÜRGEN KROYMANN
Max Planck Institute for Chemical Ecology
Department of Genetics & Evolution
Winzerlaer Strasse 10
Beutenberg Campus
D-07743 Jena
kroymann@ice.mpg.de
http://www.ice.mpg.de

Glucosinolates (mustard oil glycosides) are a diverse group of plant secondary compounds found in the order capparales. Glucosinolates contribute to plant resistance against herbivorous insects and other pests, but they also influence the quality of agriculturally important crops. Their biosynthesis occurs in three independent stages, side chain elongation of a precursor amino acid, formation of the glucosinolate core structure, and side chain modification. Methylthioalkylmalate synthase (MAM) enzymes encoded at the GS-Elong locus are responsible for the committed step in glucosinolate side chain elongation, the condensation of a 2-oxo acid derived from methionine homologues with acetyl-CoA. Glucosinolate side chain elongation is highly variable in two families of the capparales, Brassicaceae and Capparaceae.

The project will investigate the genetic and biochemical basis of variation in glucosinolate side-chain elongation in the capparales. Experiments will involve sequencing of the GS-Elong locus from a variety of species and biochemical characterization of MAM proteins encoded at the locus.

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