Structure, function and evolution of 4-coumarate:Coenzyme A ligase

JÜRGEN EBEL
Department Biologie I - Botanik
Menzinger Str. 67
D-80638 München
j.ebel@lrz.uni-muenchen.de
www.botanik.biologie.uni-muenchen.de/botphys/staff/ebel/homepage.htm

4-Coumarate:Coenzyme A ligase (4CL) is a member of the superfamily of adenylate-forming enzymes and is of central importance for phenylpropanoid metabolism in green land plants. Phenylpropanoid metabolism forms products of diverse functions in mosses, ferns, and seed plants. The family of adenylate-forming enzymes includes, besides 4CL, other acyl-CoA ligases, oxido reductases, and nonribosomal peptide synthetases. The objectives of this project are to answer questions as to the evolutionary origin of 4CL, to structural principles of the enzyme that are decisive for catalytic specificity towards differently ring-substituted cinnamic acids, and to the three-dimensional structure of 4CL (cooperation with Dr. M. T. Stubbs, Halle). The experimental systems include soybean (Glycine max L.) and Physcomitrella patens.

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