文献类型：期刊文献

英文题名：Switching a nitrilase from Syechocystis sp PCC6803 to a nitrile hydratase by rationally regulating reaction pathways

作者：Jiang, Shuiqin[1];Zhang, Lujia[1];Yao, Zhiqiang[1];Gao, Bei[1];Wang, Hualei[1];Mao, Xiangzhao[2];Wei, Dongzhi[1]

机构：[1]East China Univ Sci & Technol, New World Inst Biotechnol, State Key Lab Bioreactor Engn, Shanghai 200237, Peoples R China;[2]Ocean Univ China, Coll Food Sci & Engn, Qingdao 266003, Peoples R China

年份：2017

卷号：7

期号：5

起止页码：1122

外文期刊名：CATALYSIS SCIENCE & TECHNOLOGY

收录：;EI(收录号：20173204036179);WOS:【SCI-EXPANDED(收录号:WOS:000396137800010)】；

基金：This work was supported by the National Natural Science Foundation of China (No. 31571786, No. 21676090 and No. 21406068), the Natural Science Foundation of Shanghai (No. 16ZR1449500), the National Key Research Program of China (No. 2016YFA0501701), the Special Program for Applied Research on Super Computation of the NSFC-Guangdong Joint Fund (the second phase), and the Open Funding Project of the State Key Laboratory of Bioreactor Engineering.

语种：英文

外文关键词：Amides - Biochemical engineering - Enzymes

摘要：The development of robust biocatalysts producing a large range of organic amides by hydration of nitriles is an important pursuit and challenge. A nitrilase with a broad range of nitrile substrates was switched to a nitrile hydratase by rationally regulating the reaction pathways. Five mutants improved the amide formation in the product, and four of them formed >50% amide. F193N, with the highest amide formation among the four mutants, improved its amide product up to 73%, which was 35-fold that of the wild type, while maintaining 50% activity relative to the wild type. This study would afford a new synthetic route to amides from nitriles and could be a valuable addition to the synthetic repertoire. Further protein engineering may expand the reaction range of an enzyme to afford more additional pathways to synthetic biology.