A glandular trichome-specific monoterpene alcohol dehydrogenase from Artemisia annua

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DOIResolve DOI: http://doi.org/10.1016/j.phytochem.2010.04.026
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TypeArticle
Journal titlePhytochemistry
Volume71
Issue11-12
Pages12641269; # of pages: 6
SubjectArtemisia annua; monoterpene; trichome; dehydrogenase
AbstractThe 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.
Publication date
LanguageEnglish
AffiliationNRC Plant Biotechnology Institute; National Research Council Canada
Peer reviewedYes
NRC number50159
NPARC number19025830
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Record identifier25b3729e-78d4-4861-8c75-0f2b5718ccf7
Record created2012-04-17
Record modified2016-05-09
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