A glandular trichome-specific monoterpene alcohol dehydrogenase from Artemisia annua
Autor: | Janice F. Schmidt, Darwin W. Reed, Patrick S. Covello, Devin R. Polichuk, Yansheng Zhang |
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Rok vydání: | 2010 |
Předmět: |
Carveol
Artemisia annua Dehydrogenase Cyclohexane Monoterpenes Plant Science Horticulture Biochemistry trichome chemistry.chemical_compound Biosynthesis Oils Volatile Molecular Biology Secoisolariciresinol dehydrogenase Alcohol dehydrogenase Molecular Structure biology Alcohol Dehydrogenase food and beverages General Medicine biology.organism_classification Trichome chemistry dehydrogenase Seeds Monoterpenes biology.protein Artemisia monoterpene |
Zdroj: | Phytochemistry. 71:1264-1269 |
ISSN: | 0031-9422 |
Popis: | The major components of the isoprenoid-rich essential oil of Artemisia annua L. accumulate in the subcuticular sac of glandular secretory trichomes. As part of an effort to understand isoprenoid biosynthesis in A. annua, an expressed sequence tags (EST) collection was investigated for evidence of genes encoding trichome-specific enzymes. This analysis revealed a gene denoted Adh2, that encodes an alcohol dehydrogenase and shows a high expression level in glandular trichomes relative to other tissues. The gene product, ADH2, shows up to 61% amino acid identity to members of the short chain alcohol dehydrogenase/reductase (SDR) superfamily, including Forsythia x intermedia secoisolariciresinol dehydrogenase (49.8% identity). Through in vitro biochemical analysis, ADH2 was found to show a strong preference for monoterpenoid secondary alcohols including carveol, borneol and artemisia alcohol. These results indicate a role for ADH2 in monoterpenoid ketone biosynthesis in A. annua glandular trichomes. |
Databáze: | OpenAIRE |
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