Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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    Natural products – learning chemistry from plants
    Staniek, A. ; Bouwmeester, H.J. ; Fraser, P.D. ; Kayser, O. ; Martens, S. ; Tissier, A. ; Krol, A.R. van der; Wessjohann, L. ; Warzecha, H. - \ 2014
    Biotechnology Journal 9 (2014)3. - ISSN 1860-6768 - p. 326 - 336.
    escherichia-coli - benzylisoquinoline alkaloids - saccharomyces-cerevisiae - vanillin production - synthetic biology - organic-synthesis - biosynthesis - biocatalysis - artemisinin - enzymes
    Plant natural products (PNPs) are unique in that they represent a vast array of different structural features, ranging from relatively simple molecules to very complex ones. Given the fact that many plant secondary metabolites exhibit profound biological activity, they are frequently used as fragrances and flavors, medicines, as well as industrial chemicals. As the intricate structures of PNPs often cannot be mimicked by chemical synthesis, the original plant providers constitute the sole source for their industrial, large-scale production. However, sufficient supply is not guaranteed for all molecules of interest, making the development of alternative production systems a priority. Modern techniques, such as genome mining and thorough biochemical analysis, have helped us gain preliminary understanding of the enzymatic formation of the valuable ingredients in planta. Herein, we review recent advances in the application of biocatalytical processes, facilitating generation of complex PNPs through utilization of plant-derived specific enzymes and combinatorial biochemistry. We further evaluate the options of employing heterologous organisms harboring PNP biosynthetic pathways for the production of secondary metabolites of interest.
    The molecular cloning of dihydroartemisinic aldehyde reductase and its implication in artemisinin biosynthesis in Artemisia annua
    Ryden, A.M. ; Ruyter-Spira, C.P. ; Quax, W.J. ; Hiroyuki, O. ; Toshiya, M. ; Kayser, O. ; Bouwmeester, H.J. - \ 2010
    Planta Medica 76 (2010). - ISSN 0032-0943 - p. 1778 - 1783.
    chain dehydrogenases/reductases sdrs - amorpha-4,11-diene synthase - key enzyme - functional assignments - expression - acid - identification - plants - dehydrogenase/reductase - terpenoids
    A key point in the biosynthesis of the antimalarial drug artemisinin is the formation of dihydroartemisinic aldehyde which represents the key difference between chemotype specific pathways. This key intermediate is the substrate for several competing enzymes, some of which increase the metabolic flux towards artemisinin, and some of which - as we show in the present study - may have a negative impact on artemisinin production. In an effort to understand the biosynthetic network of artemisinin biosynthesis, extracts of A. annua flowers were investigated and found to contain an enzyme activity competing in a negative sense with artemisinin biosynthesis. The enzyme Red1 is a broad substrate oxidoreductase belonging to the short chain dehydrogenase/reductase family with high affinity for dihydroartemisinic aldehyde and valuable monoterpenoids. Spatial and temporal analysis of cDNA revealed Red1 to be trichome specific. The relevance of Red1 to artemisinin biosynthesis is discussed.
    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.
    Cloning and characterization of glandular trichome specific cytochromes P450 from Artemisia annua
    Rydén, A.M. ; Ruyter-Spira, C.P. ; Litjens, R. ; Bertea, C.M. ; Kayser, O. ; Quax, H.J. ; Bouwmeester, H.J. - \ 2007
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