期刊
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
卷 57, 期 19, 页码 5288-5291出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201712554
关键词
artificial enzymes; asymmetric catalysis; biocatalysis; carboligasse; directed evolution
资金
- Swiss National Science Foundation (SNSF)
- ETH Zurich
Enzymes are valuable biocatalysts for asymmetric synthesis due to their exacting stereocontrol. Changing the selectivity of an existing catalyst for new applications is, however, challenging. Here we show that, in contrast, the stereoselectivity of an artificial enzyme created by design and directed evolution is readily tunable. We engineered a promiscuous artificial retro-aldolase into four stereocomplementary catalysts for the Michael addition of a tertiary carbanion to an unsaturated ketone. Notably, this selectivity is also preserved with alternative Michael nucleophiles. Complete stereodiversification of other designer enzymes should similarly be possible by extension of these approaches.
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