Journal Article

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

Nobuhiro Sasaki, Yutaka Abe, Yukihiro Goda, Taiji Adachi, Kichiji Kasahara and Yoshihiro Ozeki

in Plant and Cell Physiology

Published on behalf of Japanese Society of Plant Physiologists

Volume 50, issue 5, pages 1012-1016
Published in print May 2009 | ISSN: 0032-0781
Published online April 2009 | e-ISSN: 1471-9053 | DOI: https://dx.doi.org/10.1093/pcp/pcp053
Detection of DOPA 4,5-Dioxygenase (DOD) Activity Using Recombinant Protein Prepared from Escherichia coli Cells Harboring cDNA Encoding DOD from Mirabilis jalapa

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  • Biochemistry
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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 suitable assay conditions 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

Journal Article.  2730 words.  Illustrated.

Subjects: Biochemistry ; Molecular and Cell Biology ; Plant Sciences and Forestry

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