Plant Cell Reports

, Volume 12, Issue 10, pp 573–576 | Cite as

Subcellular localization of tryptophan decarboxylase, strictosidine synthase and strictosidine glucosidase in suspension cultured cells of Catharanthus roseus and Tabernaemontana divaricata

  • Lucas H. Stevens
  • Theo J. M. Blom
  • Robert Verpoorte
Article

Abstract

The subcellular localization of tryptophan decarboxylase, strictosidine synthase and strictosidine glucosidase in suspension cultured cells of Catharanthus roseus (L.) G. Don and Tabernaemontana divaricata (L.) R. Br. ex Roem. et Schult, was investigated. It was found that tryptophan decarboxylase is an extra-vacuolar enzyme, whereas strictosidine synthase is active inside the vacuole. Strong indications were obtained for the localization of strictosidine glucosidase on the outside of the tonoplast. The results suggest that tryptamine is transported into the vacuole where it is condensed with secologanin to form strictosidine, and that strictosidine passes the tonoplast and is subsequently hydrolysed outside the vacuole.

Abbreviations

AM

α-mannosidase

EDTA

ethylenediaminetetraacetic acid

Hepes

N-2-hydroxyethylpiperazine-N'-2-ethanesulfonic acid

HPLC

highperformance liquid chromatography

MDH

malate dehydrogenase

SG

strictosidine glucosidase

SSS

strictosidine synthase

TDC

tryptophan decarboxylase

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Copyright information

© Springer-Verlag 1993

Authors and Affiliations

  • Lucas H. Stevens
    • 1
  • Theo J. M. Blom
    • 1
  • Robert Verpoorte
    • 1
  1. 1.Project-group Plant Cell Biotechnology, Division of PharmacognosyCenter for Bio-Pharmaceutical Sciences, Leiden UniversityRA LeidenThe Netherlands

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