Conversion of alcohols to enantiopure amines through dual-enzyme hydrogen-borrowing cascades.
Conversion of alcohols to enantiopure amines through dual-enzyme hydrogen-borrowing cascades.
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DOI：
10.1126/science.aac9283
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发表时间：
2015-09-25
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影响因子：
--
通讯作者：
Turner NJ
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文献类型：
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作者：
Mutti FG;Knaus T;Scrutton NS;Breuer M;Turner NJ
α-手性胺是工业规模合成大量化合物的关键中间体。在这里，我们提出了一个生物催化的氢借用胺化的伯和仲醇，允许高效和环境友好的生产对映体纯胺。该方法依赖于醇脱氢酶（来自芳香族的ADH，和芽孢杆菌属）与胺脱氢酶（由芽孢杆菌属改造的AmDH）串联操作的酶。胺化结构多样的芳香族和脂肪族醇（高达96%的转化率和99%的对映体过量）。此外，伯醇以高转化率（高达99%）胺化。这种氧化还原自给自足的网络具有高原子效率，从铵中获得氮，并产生水作为唯一的副产物。
α-Chiral amines are key intermediates for the synthesis of a plethora of chemical compounds on industrial scale. Here we present a biocatalytic hydrogen-borrowing amination of primary and secondary alcohols that allows for the efficient and environmentally benign production of enantiopure amines. The method relies on the combination of an alcohol dehydrogenase (ADHs from Aromatoleum sp., Lactobacillus sp. and Bacillus sp.) enzyme operating in tandem with an amine dehydrogenase (AmDHs engineered from Bacillus sp.) to aminate a structurally diverse range of aromatic and aliphatic alcohols (up to 96% conversion and 99% enantiomeric excess). Furthermore, primary alcohols are aminated with high conversion (up to 99%). This redox self-sufficient network possesses high atom efficiency, sourcing nitrogen from ammonium and generating water as the sole by-product.