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DOI: 10.1055/s-0030-1249930
© Georg Thieme Verlag KG Stuttgart · New York
The Molecular Cloning of Dihydroartemisinic Aldehyde Reductase and its Implication in Artemisinin Biosynthesis in Artemisia annua
Publikationsverlauf
received October 29, 2009
revised March 10, 2010
accepted April 9, 2010
Publikationsdatum:
19. Mai 2010 (online)
![](https://www.thieme-connect.de/media/plantamedica/201015/lookinside/thumbnails/10.1055-s-0030-1249930-1.jpg)
Abstract
A key point in the biosynthesis of the antimalarial drug artemisinin is the formation of dihydroartemisinic aldehyde which represents the key difference between chemotype specific pathways. This key intermediate is the substrate for several competing enzymes, some of which increase the metabolic flux towards artemisinin, and some of which – as we show in the present study – may have a negative impact on artemisinin production. In an effort to understand the biosynthetic network of artemisinin biosynthesis, extracts of A. annua flowers were investigated and found to contain an enzyme activity competing in a negative sense with artemisinin biosynthesis. The enzyme Red1 is a broad substrate oxidoreductase belonging to the short chain dehydrogenase/reductase family with high affinity for dihydroartemisinic aldehyde and valuable monoterpenoids. Spatial and temporal analysis of cDNA revealed Red1 to be trichome specific. The relevance of Red1 to artemisinin biosynthesis is discussed.
Key words
Artemisia annua L. - Asteraceae - red1 - dihydroartemisinic aldehyde - reductase - dehydrogenase - trichome
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Prof. Dr. Oliver Kayser
Technische Universität Dortmund
Fakultät Bio- und Chemieingenieurwesen
AG Technische Biochemie
Gebäude G3, Büro 5.10 Emil-Figge-Str. 68
44227 Dortmund
Germany
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eMail: oliver.kayser@bci.tu-dortmund.de