Molecular cloning and characterization of a broad substrate terpenoid oxidoreductase from Artemisia annua.
Ryden, A.M. ; Ruyter-Spira, C.P. ; Litjens, R. ; Takahashi, S. ; Quax, W.J. ; Osada, H. ; Bouwmeester, H.J. ; Kayser, O. - \ 2010
Plant and Cell Physiology 51 (2010)7. - ISSN 0032-0781 - p. 1219 - 1228.
chain dehydrogenases/reductases sdrs - amorpha-4,11-diene synthase - functional assignments - biosynthetic-pathway - essential oil - key enzyme - expression - reductase - peppermint - acid
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 kcat/Km 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.