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.
Highlights
Dinapinone A (DPA) (Figure 1a), a homodimer of monapinone A (MPA) with a biaryl dihydronaphthopyranone skeleton, was isolated from the culture broth of the fungusTalaromyces pinophilus FKI-3864 as an inhibitor of triacylglycerol accumulation in mammalian cells [1,2]
We showed that monapinone coupling enzyme (MCE) recognizes MPA or MPE as a high substrate specificity and regioselectivity
Recombinant MCE has been expressed in Escherichia coli and Aspergillus oryzae [16], the cell lysate prepared from MCE-expressing E. coli did not show MCE activity
Summary
Dinapinone A (DPA) (Figure 1a), a homodimer of monapinone A (MPA) with a biaryl dihydronaphthopyranone skeleton, was isolated from the culture broth of the fungusTalaromyces pinophilus FKI-3864 as an inhibitor of triacylglycerol accumulation in mammalian cells [1,2]. Organic synthesis approaches to produce carbon-carbon biaryl axes have been achieved by oxidative couplings, including Suzuki-Miyaura coupling and Negishi coupling [10,11]. These coupling reactions are very useful in both medicinal and industrial applications, the synthetic control of these divergent biaryl dimers remains a challenge. DPs of 8-80 regioselective dimers of MPs have been produced as a mixture of P- and M-form atropisomers [1]. Several oxidative enzymes, such as cytochrome P450s and laccases, which are responsible for coupling
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