Biochemical complementation of the betalain biosynthetic pathway in Portulaca grandiflora by a fungal 3,4-dihydroxyphenylalanine dioxygenase |
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Authors: | Lukas A Mueller Ursula Hinz Murielle Uzé Christof Sautter Jean-Pierre Zryd |
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Institution: | Laboratoire de Phytogénétique Cellulaire, Université de Lausanne, Batiment de Biologie, CH-1015 Lausanne, Switzerland, CH Swiss Federal Institute of Technology, Institute of Plant Sciences, Universit?tsstrasse 2, ETH Zentrum, CH-8092 Zürich, Switzerland, CH
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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.
Received: 24 February 1997 / Accepted: 20 May 1997 |
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Keywords: | :Amanita Betalain Dioxygenase Heterologous expression Particle gun |
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