期刊
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
卷 60, 期 31, 页码 16874-16879出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.202107182
关键词
biocatalysis; chalcone; chalcone isomerase; flavanone; flavonoid
资金
- European Union~s Horizon 2020 Research and Innovation Programme [814650]
The discovery of 66 novel bacterial CHIs reveals diversity in substrate specificity towards various hydroxylated and methoxylated chalcones. Mutagenesis of CHIera based on the binding models of these novel bacterial CHIs resulted in variants with significantly improved activity. Preparative scale conversion catalyzed by bacterial CHIs showed (S)-selectivity with up to 96% ee, providing an alternative biocatalytic route for the synthesis of (S)-flavanones in high yields.
Chalcone isomerase (CHI) is a key enzyme in the biosynthesis of flavonoids in plants. The first bacterial CHI (CHIera) was identified from Eubacterium ramulus, but its distribution, evolutionary source, substrate scope, and stereo-selectivity are still unclear. Here, we describe the identification of 66 novel bacterial CHIs from Genbank using a novel Sequence-Structure-Function-Evolution (SSFE) strategy. These novel bacterial CHIs show diversity in substrate specificity towards various hydroxylated and methoxylated chalcones. The mutagenesis of CHIera according to the substrate binding models of these novel bacterial CHIs resulted in several variants with greatly improved activity towards these chalcones. Furthermore, the preparative scale conversion catalyzed by bacterial CHIs has been performed for five chalcones and revealed (S)-selectivity with up to 96% ee, which provides an alternative biocatalytic route for the synthesis of (S)-flavanones in high yields.
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