Characterization of DOPA 4,5-dioxygenase from four o'clock
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- Sasaki Nobuhiro
- Dept. of Biotechnol., TUAT
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- Yoshioka Hideaki
- Dept. of Biotechnol., TUAT
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- Koda Takatoshi
- San-Ei Gen F.F.I., Inc.
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- Wada Katsuhiro
- San-Ei Gen F.F.I., Inc.
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- Adachi Taiji
- Dept. of Plant Science, College of Agriculture, Osaka Prefecture University
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- Ozeki Yoshihiro
- Dept. of Biotechnol., TUAT
Bibliographic Information
- Other Title
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- オシロイバナにおけるベタレイン色素合成に関わる DOPA 4,5-dioxygenase の解析
Description
DOPA 4, 5-dioxygenase (DOD) is the most important enzyme involved in betalain biosynthesis. The cDNA coding DOD was isolated from common portulaca (Portulaca grandiflora) by cDNA subtraction method (Christinet, et al., Plant Physiol 134: 265-274). It was confirmed by complementation experiments using the particle bombardment that the gene was concerned with betalamic acid synthesis in vivo, but there has been no reports to detecte DOD activity in vitro. In this study, we isolated MjDOD cDNA from four o'clock (Mirabilis jalapa) by PCR method using the degenerate primer based on the conserved amino acid sequence among plant DOD genes. A MjDOD cDNA was cloned into yeast expression vector and introduced into Saccharomyces cerevisiae. A crude extract from the recombinant yeast strains was added to a reaction mixture containing L-DOPA. The color of the reaction mixture turned to yellow and a reaction product in the mixture was betalamic acid confirmed by HPLC.
Journal
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- Plant and Cell Physiology Supplement
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Plant and Cell Physiology Supplement 2005 (0), 120-120, 2005
The Japanese Society of Plant Physiologists
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Details 詳細情報について
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- CRID
- 1390001205626533120
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- NII Article ID
- 130006986604
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- Data Source
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- JaLC
- CiNii Articles
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- Abstract License Flag
- Disallowed
