Redesigning alcohol dehydrogenases/reductases for more efficient biosynthesis of enantiopure isomers

Biotechnology Advances
Rongzhen ZhangRong Xiao

Abstract

Alcohol dehydrogenases/reductases predominantly catalyze the asymmetric biosynthesis of optically pure stereoisomers because of their unique chiral constitutions. The enantioselectivities of alcohol dehydrogenases/reductases are substrate- and cofactor-dependent, and therefore they usually catalyze specific reactions with high enantioselectivity under physiological conditions; this may not be suitable for asymmetric biosynthesis with non-natural substrates or non-natural cofactors, and under nonphysiological conditions. It is therefore necessary to modify alcohol dehydrogenases/reductases using various redesigning tools such as directed evolution and rational design, and their combinations, as well as engineering enzyme modules for more efficient production of "non-natural" products. In this article, progress in these aspects of alcohol dehydrogenase/reductase design is reviewed, and future challenges are discussed.

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Citations

Jan 12, 2017·Applied Microbiology and Biotechnology·Yu-Guo ZhengZhi-Qiang Liu
Oct 27, 2017·Applied Microbiology and Biotechnology·Feng-Jiao ZhaoZhong-Liu Wu
May 18, 2018·Chemical Communications : Chem Comm·Roger A Sheldon, Dean Brady
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Aug 20, 2021·Frontiers in Bioengineering and Biotechnology·Kunal DuttaIbrahim Khalifa

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