Planta

, Volume 203, Issue 2, pp 260–263

Biochemical complementation of the betalain biosynthetic pathway in Portulaca grandiflora by a fungal 3,4-dihydroxyphenylalanine dioxygenase

  • Lukas A. Mueller
  • Ursula Hinz
  • Murielle Uzé
  • Christof Sautter
  • Jean-Pierre Zryd
Rapid communication

DOI: 10.1007/s004250050190

Cite this article as:
Mueller, L., Hinz, U., Uzé, M. et al. Planta (1997) 203: 260. doi:10.1007/s004250050190

Abstract.

3,4-Dihydroxyphenylalanine (DOPA) dioxygenase from Amanitamuscaria catalyses the key reaction of betalain biosynthesis, namely the conversion of DOPA to betalamic acid by a 4,5-ring-opening reaction. In addition, it catalyses a 2,3 opening which yields the fungal pigment muscaflavin, a compound that has never been found in plants. In this work, a cDNA clone (DodA) encoding A. muscaria DOPA-dioxygenase was expressed in white Portulacagrandiflora petals, using the particle bombardment technique. Transformation resulted in the formation of yellow and violet spots that contained betalain pigments and muscaflavin, indicating that the fungal enzyme was expressed and active in plants, and could complement the plant betalain biosynthetic pathway. The presence of muscaflavin in transformed plants indicates a difference in the specificity of the plant and A.muscaria enzymes.

Key words:Amanita Betalain Dioxygenase Heterologous expression Particle gun 

Copyright information

© Springer-Verlag Berlin Heidelberg 1997

Authors and Affiliations

  • Lukas A. Mueller
    • 1
  • Ursula Hinz
    • 1
  • Murielle Uzé
    • 2
  • Christof Sautter
    • 2
  • Jean-Pierre Zryd
    • 1
  1. 1.Laboratoire de Phytogénétique Cellulaire, Université de Lausanne, Bâtiment de Biologie, CH-1015 Lausanne, SwitzerlandCH
  2. 2.Swiss Federal Institute of Technology, Institute of Plant Sciences, Universitätsstrasse 2, ETH Zentrum, CH-8092 Zürich, SwitzerlandCH