Jump to main content
Jump to site search


Development of an engineered thermostable amine dehydrogenase for the synthesis of structurally diverse chiral amines

Author affiliations

Abstract

Amine dehydrogenases (AmDHs) are emerging as a class of attractive biocatalysts for synthesizing chiral amines via asymmetric reductive amination of ketones with inexpensive ammonia as an amino donor. However, the AmDHs developed to date exhibit limited substrate scope. Here, using directed evolution, we engineered a GkAmDH based on a thermostable phenylalanine dehydrogenase from Geobacillus kaustophilus. The newly developed AmDH is able to catalyze reductive amination of a diverse set of ketones and functionalized hydroxy ketones with ammonia or primary amines with up to >99% conversion, thus accessing structurally diverse chiral primary and secondary amines and chiral vicinal amino alcohols, with excellent enantioselectivity (up to >99% ee) and releasing water as the sole by-product.

Graphical abstract: Development of an engineered thermostable amine dehydrogenase for the synthesis of structurally diverse chiral amines

Back to tab navigation

Supplementary files

Article information


Submitted
14 Jan 2020
Accepted
11 Feb 2020
First published
12 Feb 2020

Catal. Sci. Technol., 2020, Advance Article
Article type
Paper

Development of an engineered thermostable amine dehydrogenase for the synthesis of structurally diverse chiral amines

L. Liu, D. Wang, F. Chen, Z. Zhang, Q. Chen, J. Xu, Z. Wang and G. Zheng, Catal. Sci. Technol., 2020, Advance Article , DOI: 10.1039/D0CY00071J

Social activity

Search articles by author

Spotlight

Advertisements