A dynamic combinatorial screen for novel imine reductase activity
A dynamic combinatorial screen for novel imine reductase activity
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DOI：
10.1016/j.tet.2003.10.114
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发表时间：
2004-01-12
期刊：
影响因子：
2.1
通讯作者：
Stephens, G
中科院分区：
文献类型：
--
作者：
Li, H;Williams, P;Stephens, G
利用水-十四烷双相溶剂体系，通过对亚胺底物动态组合文库的筛选，在厌氧细菌中发现了新的亚胺还原酶活性。咖啡酸诱导的细胞将亚苄基苯胺和丁基苯胺还原为相应的胺，而未诱导的细胞仅还原亚丁基苯胺。尽管副反应消耗了一些起始材料，但还是检测到了还原。新的筛选现在可以扩展到发现合成上有用的亚胺还原酶和酶，这些酶催化尚未发现的化学反应的生物催化等价物。(C)2003爱思唯尔有限公司。保留所有权利。
New imine reductase activity has been discovered in the anaerobic bacterium Acetobacterium woodii by screening a dynamic combinatorial library of virtual imine substrates, using a biphasic water-tetradecane solvent system. Benzylidine aniline and butylidine aniline were reduced to the corresponding amines by caffeate-induced cells, whereas uninduced cells reduced butylidine aniline only. The reductions were detected despite side reactions that consumed some of the starting materials. The new screen can now be extended to discover synthetically useful imine reductases and enzymes that catalyse reactions for which biocatalytic equivalents of the chemical reactions have not yet been discovered. (C) 2003 Elsevier Ltd. All rights reserved.