Molecular Cloning and Characterization of a Broad Substrate Terpenoid Oxidoreductase from Artemisia annua | Zendy

A.-M. Ryden | Zendy; Carolien RuyterSpira | Zendy; R. H. M. G. Litjens | Zendy; Shunji Takahashi | Zendy; Wim J. Quax | Zendy; Hideo Osada | Zendy; Harro J. Bouwmeester | Zendy; Oliver Kayser | Zendy

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Molecular Cloning and Characterization of a Broad Substrate Terpenoid Oxidoreductase from Artemisia annua

Author(s) -

A.-M. Ryden,

Carolien RuyterSpira,

R. H. M. G. Litjens,

Shunji Takahashi,

Wim J. Quax,

Hideo Osada,

Harro J. Bouwmeester,

Oliver Kayser

Publication year - 2010

Publication title -

plant and cell physiology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.975

H-Index - 152

eISSN - 1471-9053

pISSN - 0032-0781

DOI - 10.1093/pcp/pcq073

Subject(s) - menthone , artemisia annua , oxidoreductase , enzyme kinetics , reductase , chemistry , substrate (aquarium) , stereochemistry , enzyme , biochemistry , biology , menthol , artemisinin , active site , organic chemistry , ecology , malaria , immunology , plasmodium falciparum

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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