Literature DB >> 20483909

Molecular cloning and characterization of a broad substrate terpenoid oxidoreductase from Artemisia annua.

Anna-Margareta Rydén1, Carolien Ruyter-Spira, Ralph Litjens, Shunji Takahashi, Wim Quax, Hiroyuki Osada, Harro Bouwmeester, Oliver Kayser.   

Abstract

From Artemisia annua L., a new oxidoreductase (Red 1) was cloned, sequenced and functionally characterized. Through bioinformatics, heterologous protein expression and enzyme substrate conversion assays, the elucidation of the enzymatic capacities of Red1 was achieved. Red1 acts on monoterpenoids, and in particular functions as a menthone:neomenthol oxidoreductase. The kinetic parameter k(cat)/K(m) was determined to be 939-fold more efficient for the reduction of (-)-menthone to (+)-neomenthol than results previously reported for the menthone:neomenthol reductase from Mentha x piperita. Based on its kinetic properties, the possible use of Red1 in biological crop protection is discussed.

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Year:  2010        PMID: 20483909     DOI: 10.1093/pcp/pcq073

Source DB:  PubMed          Journal:  Plant Cell Physiol        ISSN: 0032-0781            Impact factor:   4.927


  2 in total

1.  Molecular cloning and characterization of a tropinone reductase from Dendrobium nobile Lindl.

Authors:  Wei Chen; Xiaofei Cheng; Zhenhua Zhou; Junjun Liu; Huizhong Wang
Journal:  Mol Biol Rep       Date:  2012-10-27       Impact factor: 2.316

2.  A Hedychium coronarium short chain alcohol dehydrogenase is a player in allo-ocimene biosynthesis.

Authors:  Hua Chen; Yuechong Yue; Rangcai Yu; Yanping Fan
Journal:  Plant Mol Biol       Date:  2019-07-31       Impact factor: 4.076

  2 in total

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