Issue 5, 2017

Switching a nitrilase from Syechocystis sp. PCC6803 to a nitrile hydratase by rationally regulating reaction pathways

Abstract

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.

Graphical abstract: Switching a nitrilase from Syechocystis sp. PCC6803 to a nitrile hydratase by rationally regulating reaction pathways

Supplementary files

Article information

Article type
Paper
Submitted
11 Jan 2017
Accepted
15 Feb 2017
First published
15 Feb 2017

Catal. Sci. Technol., 2017,7, 1122-1128

Switching a nitrilase from Syechocystis sp. PCC6803 to a nitrile hydratase by rationally regulating reaction pathways

S. Jiang, L. Zhang, Z. Yao, B. Gao, H. Wang, X. Mao and D. Wei, Catal. Sci. Technol., 2017, 7, 1122 DOI: 10.1039/C7CY00060J

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