首页> 外文期刊>ChemCatChem >Synthesis of Optically Active Amines Employing Recombinant ω-Transaminases in E. coli Cells
【24h】

Synthesis of Optically Active Amines Employing Recombinant ω-Transaminases in E. coli Cells

机译:在大肠杆菌细胞中利用重组ω-转氨酶合成旋光胺

获取原文
获取原文并翻译 | 示例
获取外文期刊封面目录资料

摘要

Various recombinant ω-transaminases, overexpressed in E. coli ceils and employed as whole-cell catalysts, are tested for the synthesis of enantiomerically pure amines from the corresponding prochiral ketones. Optically pure (S)-amines are obtained by formal reductive amination, consuming just ammonia and a cheap reducing agent (formate) with up to 99% ee and 97% yield. The other enantiomer was accessible by employing the same ω-transaminases in a kinetic resolution starting from racemic amines. A ω-transaminase derived from an Arthrobacter species displayed the highest stereoselectivity for all substrates tested, both for the kinetic resolution of rac-amines and for the amination of ketones.
机译:测试了在大肠杆菌细胞中过表达并用作全细胞催化剂的各种重组ω-转氨酶,用于从相应的手性酮中合成对映体纯的胺。通过正式的还原胺化获得光学纯的(S)-胺,仅消耗氨和便宜的还原剂(甲酸酯),ee高达99%,收率达97%。通过从消旋胺开始以动力学拆分方式使用相同的ω-转氨酶,可以获得其他对映体。无论是外消旋胺的动力学拆分还是酮的胺化,源自节杆菌属的ω-转氨酶对所有受试底物均显示出最高的立体选择性。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱:kefu@zhangqiaokeyan.com

京公网安备:11010802029741号 ICP备案号:京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有
  • 客服微信

  • 服务号