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Plant and Cell Physiology Advance Access published online on April 13, 2009
Plant and Cell Physiology, doi:10.1093/pcp/pcp053
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© The Author 2009. Published by Oxford University Press on behalf of Japanese Society of Plant Physiologists. All rights reserved. For Permissions, please e-mail: journals.permissions@oxfordjournals.org

Detection of DOPA 4,5-dioxygenase (DOD) Activity Using Recombinant Protein Prepared from Escherichia coli Cells Harboring cDNA Encoding DOD from Mirabilis jalapa

Nobuhiro Sasaki1, Yutaka Abe1, Yukihiro Goda2, Taiji Adachi3, Kichiji Kasahara4 and Yoshihiro Ozeki1

1Department of Biotechnology and Life Science, Faculty of Engineering, Tokyo University of Agriculture and Technology, 2-24-16 Naka-cho, Koganei, Tokyo 184-8588, Japan
2Division of Pharmacognosy, Phytochemistry and Narcotics, National Institute of Health Sciences, 1-18-1 Kamiyoga, Setagaya-ku, Tokyo 158-8501, Japan
3Institute for Plant Biotechnology Research & Development, Ltd. 1-46-901, Hama 5-Chome, Tsurumi-Ku, Osaka, 538-0035, Japan
41128 Moro-oka, Kohoku-ku, Yokohama, Kanagawa,222-0002 Japan

Corresponding author: Dr. Nobuhiro Sasaki, E-mail: nove{at}cc.tuat.ac.jp


  Abstract

Betalains are synthesized in flowers, fruits, and other tissues of the plant order Caryophyllales. Betalamic acid is the chromophore of betalain pigments synthesized by a ring-cleaving enzyme reaction on L-dihydroxyphenylalanine (DOPA). Although reverse genetic evidence has proven that DOPA 4,5-dioxygenase (DOD) is a key enzyme of betalain biosynthesis, all attempts to detect recombinant plant DOD activity in vitro have failed. Here, we report on the formation of betalamic acid from DOPA under a suitable assay condition using recombinant MjDOD produced by Escherichia coli. This is the first report showing biochemical evidence for DOD activity in vitro.

Keywords: Betalain - betalamic acid - DOPA dioxygenase - Mirabilis jalapa

(Received March 17, 2009; Accepted April 8, 2009)
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