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Published on June 9, 2006; 10.1104/pp.106.082024

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Received April 13, 2006
Returned for revision May 8, 2006
Accepted May 24, 2006

CYP71B15 (PAD3) catalyzes the final step in camalexin biosynthesis

Regina Schuhegger , Majse Nafisi , Madina Mansourova , Bent Larsen Petersen , Carl Erik Olsen , Ales Svatos , Barbara Ann Halkier , and Erich Glawischnig *

Lehrstuhl für Genetik, Technische Universität München, Am Hochanger 8, D-85350 Freising, Germany
Center for Molecular Plant Physiology (PlaCe), Thorvaldsensvej 40, DK-1871 Frederiksberg C, Denmark
Max Planck Institute for Chemical Ecology, Hans-Knöll-Str. 8, Beutenberg Campus, D-07745 Jena, Germany

* Corresponding author; email: egl{at}wzw.tum.de.

Camalexin represents the main phytoalexin in Arabidopsis. The camalexin deficient pad3 mutant has been widely used to assess the biological role of camalexin although the exact substrate of the cytochrome P450 enzyme 71B15 encoded by PAD3 remained elusive. 2-(indol-3-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid (dihydrocamalexic acid) was identified as likely intermediate in camalexin biosynthesis downstream of indole-3-acetaldoxime as it accumulated in leaves of silver nitrate induced pad3 mutant plants and it complemented the camalexin deficient phenotype of a cyp79b2/cyp79b3 double knockout mutant. Recombinant CYP71B15 heterologously expressed in yeast catalyzed the conversion of dihydrocamalexic acid to camalexin with preference of the S-enantiomer. Arabidopsis microsomes isolated from leaves of CYP71B15 overexpressing and induced wild type plants were capable of the same reaction but not microsomes from induced leaves of pad3 mutants. In conclusion, CYP71B15 catalyzes the final step in camalexin biosynthesis.




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