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Activation of chloroplast-localized enzymes of quinolizidine alkaloid biosynthesis by reduced thioredoxin

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Abstract

Previous studies from the laboratory of the authors have shown that the tetracyclic quinolizidine alkaloids are synthesized in leaf chloroplasts of Lupinus polyphyllus. Additionally, alkaloid formation reveals a light dependent diurnal rhythm in vivo. The present study shows that the principal biosynthetic enzymes, lysine decarboxylase and 17-oxosparteine synthase, assayed in acetone powder extracts and isolated chloroplasts of L. polyphyllus, were activated by reduced E. coli thioredoxin. Since both enzymes display optimal activity at pH 8 and were rather inactive at pH 7, both thioredoxin and the light mediated shift in the hydrogen ion concentration of the chloroplast stroma from pH 7 to pH 8 may be involved in the light controlled alkaloid formation.

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Abbreviations

DTE:

dithioerythritol

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Authors and Affiliations

  1. Institut für Pharmazeutische Biologie der Technischen Universität Braunschweig, D-3300, Braunschweig, Federal Republic of Germany

    Michael Wink & Thomas Hartmann

Authors
  1. Michael Wink
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  2. Thomas Hartmann
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Wink, M., Hartmann, T. Activation of chloroplast-localized enzymes of quinolizidine alkaloid biosynthesis by reduced thioredoxin. Plant Cell Reports 1, 6–9 (1981). https://doi.org/10.1007/BF00267646

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  • DOI: https://doi.org/10.1007/BF00267646

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