Biochemical characterization and identification of a cinnamyl alcohol dehydrogenase from Artemisia annua

Copyright © 2012 Elsevier Ireland Ltd. All rights reserved.

Bibliographische Detailangaben
Veröffentlicht in:Plant science : an international journal of experimental plant biology. - 1985. - 193-194(2012) vom: 28. Sept., Seite 85-95
1. Verfasser: Li, Xing (VerfasserIn)
Weitere Verfasser: Ma, Dongming, Chen, Jianlin, Pu, Gaobin, Ji, Yunpeng, Lei, Caiyan, Du, Zhigao, Liu, Benye, Ye, Hechun, Wang, Hong
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2012
Zugriff auf das übergeordnete Werk:Plant science : an international journal of experimental plant biology
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Aldehydes Artemisinins Lactones Plant Growth Regulators Alcohol Oxidoreductases EC 1.1.- cinnamyl alcohol dehydrogenase EC 1.1.1.195 mehr... artemisin Y1R67R7XWU
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245 1 0 |a Biochemical characterization and identification of a cinnamyl alcohol dehydrogenase from Artemisia annua 
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520 |a It is well known in the literature that cinnamyl alcohol dehydrogenase (CAD) reduces hydroxycinnamyl aldehydes, such as coumaryl, coniferyl, and sinapyl aldehydes, to their corresponding alcohols in the presence of NADPH, and these alcohols act as the precursors of lignin biosynthesis. Here, we report the isolation of a cDNA encoding an NADP(+)-dependent CAD, designated as AaCAD, from the cDNA library using glandular secretory trichomes of Artemisia annua as the source of mRNA. A phylogenetic analysis indicated that AaCAD was clustered with AtCAD4 and AtCAD5, which were involved in monolignol biosynthesis from Arabidopsis. Semi-quantitative RT-PCR showed that the AaCAD transcript was abundant mostly in leaf and root, followed by flower, and lowest in stem. Functional and enzymatic assays showed that the recombinant enzyme was able to reversibly reduce a variety of common CADs substrates, namely geranial, cinnamyl aldehyde, sinapyl aldehyde, coniferyl aldehyde, and a sesquiterpenoid artemisinic aldehyde, to geraniol, cinnamyl alcohol, sinapyl alcohol, coniferyl alcohol, and artemisinic alcohol respectively. Besides, considering that AaCAD was identified from the glandular secretory trichomes of A. annua, and that the recombinant enzyme exhibited reductase activity by using artemisinic aldehyde as substrate, some possible role of AaCAD in artemisinin biosynthesis is also discussed 
650 4 |a Journal Article 
650 4 |a Research Support, Non-U.S. Gov't 
650 7 |a Aldehydes  |2 NLM 
650 7 |a Artemisinins  |2 NLM 
650 7 |a Lactones  |2 NLM 
650 7 |a Plant Growth Regulators  |2 NLM 
650 7 |a Alcohol Oxidoreductases  |2 NLM 
650 7 |a EC 1.1.-  |2 NLM 
650 7 |a cinnamyl alcohol dehydrogenase  |2 NLM 
650 7 |a EC 1.1.1.195  |2 NLM 
650 7 |a artemisin  |2 NLM 
650 7 |a Y1R67R7XWU  |2 NLM 
700 1 |a Ma, Dongming  |e verfasserin  |4 aut 
700 1 |a Chen, Jianlin  |e verfasserin  |4 aut 
700 1 |a Pu, Gaobin  |e verfasserin  |4 aut 
700 1 |a Ji, Yunpeng  |e verfasserin  |4 aut 
700 1 |a Lei, Caiyan  |e verfasserin  |4 aut 
700 1 |a Du, Zhigao  |e verfasserin  |4 aut 
700 1 |a Liu, Benye  |e verfasserin  |4 aut 
700 1 |a Ye, Hechun  |e verfasserin  |4 aut 
700 1 |a Wang, Hong  |e verfasserin  |4 aut 
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773 1 8 |g volume:193-194  |g year:2012  |g day:28  |g month:09  |g pages:85-95 
856 4 0 |u http://dx.doi.org/10.1016/j.plantsci.2012.05.011  |3 Volltext 
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