Your institution may have access to this item. Find your institution then sign in to continue.

Title: Detection of DOPA 4,5-Dioxygenase (DOD) Activity Using Recombinant Protein Prepared from Escherichia coli Cells Harboring cDNA Encoding DOD from Mirabilis jalapa.
Authors: Nobuhiro Sasaki; Yutaka Abe; Yukihiro Goda; Taiji Adachi; Kichiji Kasahara; Yoshihiro Ozeki
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 suitable assay conditions using recombinant MjDOD produced by Escherichia coli. This is the first report showing biochemical evidence for DOD activity in vitro.
Subjects: DOPA; OXYGENASES; RECOMBINANT proteins; ANTISENSE DNA; ESCHERICHIA coli; MIRABILIS; GENETIC code; BIOSYNTHESIS
Publication: Plant & Cell Physiology, 2009, Vol 50, Issue 5, p1012
ISSN: 0032-0781
Publication type: Academic Journal
DOI: 10.1093/pcp/pcp053

We found a match

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