Atropisomeric dinapinones A1 and A2 (DPA1 and DPA2) were isolated from a culture of Talaromyces pinophilus FKI‐3864. Monapinone coupling enzyme (MCE), which dimerizes naphthopyranone monapinone A (MPA), was purified from a cell‐free extract of T. pinophilus FKI‐3864. MCE regioselectively dimerizes MPA at the 8,8′‐positions to synthesize the atropisomers DPA1 and DPA2 in a ratio of approximately 1:2.5 without a cofactor. The optimal pH value and temperature for MCE were 4.0 and 50 °C, and the apparent K_m and V_max values for MPA were (72.7±23.2) μm and (1.21±0.170) μmol min⁻¹ mg⁻¹ protein. The MCE polypeptide is significantly homologous with multicopper oxidases. Heterologous expression of MCE and functional analysis confirmed that MCE catalyzes the regioselective coupling reaction of MPA to produce DPA. No fungal multicopper oxidase has previously been reported to catalyze regioselective intermolecular oxidative phenol coupling to produce naphthopyranone atropisomers.

中文翻译：

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真菌Multicopper氧化酶的发现，该酶催化三环萘并吡喃酮的区域选择性偶联以产生阻转异构体。

促阻转异构体地那平酮A1和A2（DPA1和DPA2）分离自嗜松毛球菌FKI-3864的培养物中。莫纳平酮偶联酶（MCE）使萘并吡喃酮莫纳平酮A（MPA）二聚，是从无嗜珠菌FKI-3864的无细胞提取物中纯化得到的。MCE在8,8'-位置将MPA区域选择性二聚，以合成阻转异构体DPA1和DPA2，比例约为1：2.5，而没有辅因子。MCE的最佳pH值和温度为4.0和50°C，MPA的表观K _m和V _max值为（72.7±23.2）μm和（1.21±0.170）μmolmin ^-1  mg ^-1 蛋白质。MCE多肽与多铜氧化酶显着同源。MCE的异源表达和功能分析证实，MCE催化MPA的区域选择性偶联反应以产生DPA。以前没有真菌多铜氧化酶催化区域选择性分子间氧化酚偶联反应产生萘并吡喃酮阻转异构体的报道。