Journal
APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
Volume 104, Issue 19, Pages 8155-8170Publisher
SPRINGER
DOI: 10.1007/s00253-020-10845-z
Keywords
Biocatalysis; Old yellow enzymes; Protein engineering; Biocatalytic reduction; Stereopreference switch
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Funding
- National Natural Science Foundation of China [31971207, 81602993]
- LiaoNing Revitalization Talents Program [XLYC1907153]
- Young Elite Scientists Sponsorship Program by CAST [2016QNRC001]
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Since the first discovery of old yellow enzyme 1 (OYE1) fromSaccharomyces pastorianusin 1932, biocatalytic asymmetric reduction of activated alkenes by OYEs has become a valuable reaction in organic synthesis. To access stereocomplementary C=C-bond bioreduction, the mining of novel OYEs and especially the protein engineering of existing OYEs have been performed, which successfully achieved the stereocomplementary reduction in several cases and further raise the potential of applications. In this review, we analyzed the structures, active sites, and substrate recognition of OYEs, which are the bases for their substrate specificity and stereospecificity. Sequence similarity network of OYEs superfamily was also constructed to investigate the scope of characterized OYEs. The structure-guided engineering to switch the stereoselectivity of OYEs and thus access stereocomplementary bioreduction over the last decade (2009-2020) was then reviewed and discussed, which might give new insights into the mining and engineering of related biocatalysts.
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