期刊
BIOORGANIC & MEDICINAL CHEMISTRY
卷 22, 期 20, 页码 5555-5557出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.bmc.2014.06.035
关键词
Hydroamination; Bacterial; Phenylalanine ammonia lyase; Kinetics; Biocatalysis
资金
- Centre of Excellence in Biocatalysis, Biotransformation and Biocatalytic Manufacture (CoEBio3)
- Royal Society Wolfson Research Merit Award
- Biotechnology and Biological Sciences Research Council [BB/K00199X/1] Funding Source: researchfish
- BBSRC [BB/K00199X/1] Funding Source: UKRI
Phenylalanine ammonia lyases (PALs) catalyse the regio- and stereoselective hydroamination of cinnamic acid analogues to yield optically enriched a-amino acids. Herein, we demonstrate that a liacterial PAL from Anabaena variabilis (AvPAL) displays significantly higher activity towards a series of non-natural substrates than previously described eukaryotic PALs. Biotransformations performed on a preparative scale led to the synthesis of the 2-chloro- and 4-trifluoromethyl-phenylalanine derivatives in excellent ee, highlighting the enormous potential of bacterial PALs as biocatalysts for the synthesis of high value, non-natural amino acids. (C) 2014 Elsevier Ltd. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据