Substrate-enantiomer selectivity of matairesinol <i>O</i>-methyltransferases
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- Ragamustari Safendrri Komara
- Research Institute for Sustainable Humanosphere, Kyoto University Institute of Sustainability Science, Kyoto University
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- Yamamura Masaomi
- Research Institute for Sustainable Humanosphere, Kyoto University
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- Ono Eiichiro
- Research Institute, Suntory Global Innovation Center Ltd.
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- Hattori Takefumi
- Research Institute for Sustainable Humanosphere, Kyoto University
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- Suzuki Shiro
- Kazusa DNA Research Institute
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- Suzuki Hideyuki
- Kazusa DNA Research Institute
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- Shibata Daisuke
- Kazusa DNA Research Institute
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- Umezawa Toshiaki
- Research Institute for Sustainable Humanosphere, Kyoto University Institute of Sustainability Science, Kyoto University
Bibliographic Information
- Other Title
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- Substrate-enantiomer selectivity of matairesinol O-methyltransferases
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Description
Previously we reported a cDNA encoding an O-methyltransferase (OMT) responsible for the O-methylation of matairesinol to afford arctigenin in Carthamus tinctorius. However, the regioselectivity and stereoselectivity of its reaction are not yet well understood. In this paper, we report the characterization and comparison of three matairesinol OMTs (MROMTs) encoded by cDNAs isolated from C. tinctorius (CtMROMT), Anthriscus sylvestris (AsMROMT), and Forsythia koreana (FkMROMT). Although they shared matairesinol as a substrate, each recombinant MROMT showed different catalytic behavior. AsMROMT and CtMROMT methylated matairesinol’s hydroxyl group at the C4′ position giving rise to arctigenin, while FkMROMT methylated the C4 position hydroxyl group giving rise to isoarctigenin. Analysis of the enantiomeric composition of products from racemic matairesinol showed all OMT reactions to be highly selective in terms of the substrate enantiomers and only use the (−)-enantiomer as the substrate.
Journal
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- Plant Biotechnology
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Plant Biotechnology 31 (3), 257-267, 2014
Japanese Society for Plant Biotechnology
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Details 詳細情報について
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- CRID
- 1390001204327186944
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- NII Article ID
- 130004690904
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- NII Book ID
- AA11250821
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- ISSN
- 13476114
- 13424580
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- NDL BIB ID
- 025819017
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- Text Lang
- en
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- Data Source
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- JaLC
- NDL Search
- Crossref
- CiNii Articles
- OpenAIRE
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- Abstract License Flag
- Disallowed