Monapinone Coupling Enzyme Produces Non-Natural Heterodimers

Catalysts

卷:11

Satoshi Ohte¹  Masayuki Toyoda¹  Keisuke Kobayashi¹  Taichi Ohshiro¹  Isao Fujii²  Hiroshi Tomoda² 

[1] Department of Microbial Chemistry, Graduate School of Pharmaceutical Sciences, Kitasato University, 5-9-1 Shirokane, Minato-ku, Tokyo 108-8641, Japan;

[2] Drug Discovery Laboratory, Graduate School of Pharmaceutical Sciences, Kitasato University, 5-9-1 Shirokane, Minato-ku, Tokyo 108-8641, Japan;

关键词: multicopper oxidase;    secondary substratespecificity;    monapinone coupling enzyme;    biaryl compound;    C-C coupling;   

DOI  :  10.3390/catal11081015

来源: DOAJ

【 摘 要 】

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.

【 授权许可】

Unknown