Journal
CATALYSIS SCIENCE & TECHNOLOGY
Volume 7, Issue 5, Pages 1122-1128Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c7cy00060j
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Funding
- National Natural Science Foundation of China [1571786, 21676090, 21406068]
- Natural Science Foundation of Shanghai [16ZR1449500]
- National Key Research Program of China [2016YFA0501701]
- Special Program for Applied Research on Super Computation of the NSFC-Guangdong Joint Fund
- Open Funding Project of the State Key Laboratory of Bioreactor Engineering
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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.
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