Molecular cloning and characterization of a broad substrate terpenoid oxidoreductase from Artemisia annua.
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.
Rydén
Anna-Margareta
AM
Department of Pharmaceutical Biology, GUIDE, University of Groningen, 9713 AV Groningen, The Netherlands.
Ruyter-Spira
Carolien
C
Litjens
Ralph
R
Takahashi
Shunji
S
Quax
Wim
W
Osada
Hiroyuki
H
Bouwmeester
Harro
H
Kayser
Oliver
O
D000595:Amino Acid Sequence; D031172:Artemisia annua / Q000201:enzymology* / Q000235:genetics; D003001:Cloning, Molecular; D019295:Computational Biology; D008401:Gas Chromatography-Mass Spectrometry; D015723:Gene Library; D008969:Molecular Sequence Data; D010088:Oxidoreductases / Q000235:genetics / Q000378:metabolism*; D016415:Sequence Alignment; D017422:Sequence Analysis, DNA; D013379:Substrate Specificity; D013729:Terpenes / Q000378:metabolism*
D013729:Terpenes; D010088:Oxidoreductases