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- Title
Monapinone Coupling Enzyme Produces Non-Natural Heterodimers.
- Authors
Ohte, Satoshi; Toyoda, Masayuki; Kobayashi, Keisuke; Fujii, Isao; Ohshiro, Taichi; Tomoda, Hiroshi
- Abstract
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.
- Subjects
HETERODIMERS; MULTICOPPER oxidase; COUPLING reactions (Chemistry); CYCLIC compounds; ENZYMES
- Publication
Catalysts (2073-4344), 2021, Vol 11, Issue 8, p1015
- ISSN
2073-4344
- Publication type
Article
- DOI
10.3390/catal11081015