2021年8月23日
Monapinone Coupling Enzyme Produces Non-Natural Heterodimers
Catalysts
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- 巻
- 11
- 号
- 8
- 開始ページ
- 1015
- 終了ページ
- 1015
- 記述言語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.3390/catal11081015
- 出版者・発行元
- MDPI AG
The monapinone coupling enzyme (MCE), a fungal multicopper oxidase, catalyzes the regioselective C–C coupling between tricyclic monapinone A (the primary substrate) and other monapinones (secondary substrates) to produce atropisomeric biaryl homo- or heterodimers. In this study, mono-, bi- and tricyclic compounds were tested to determine whether they worked as secondary substrates for MCE. Among 14 cyclic compounds, MCE utilized semivioxanthin, YWA1, 1,3-naphthalenediol and flaviolin as secondary substrates to produce non-natural heterodimers. The atropisomeric biaryl heterodimers produced by MCE from monapinone A and semivioxanthin were isolated, and their structures were elucidated by NMR and MS. These findings indicate that MCE recognizes bi- and tricyclic compounds with a 1,3-dihydroxy or 1-hydroxy-3-methoxy benzene ring as a secondary substrate.
- ID情報
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- DOI : 10.3390/catal11081015
- eISSN : 2073-4344