期刊
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
卷 54, 期 19, 页码 5609-5612出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201500217
关键词
asymmetric catalysis; biocatalysis; directed evolution; enzyme design; enzyme promiscuity
资金
- Swiss National Science Foundation (SNSF)
- ETH Zurich
- Spanish Ministerio de Educacion, Cultura y Deporte
- Marie Curie Action within the FP7-PEOPLE program [IEF-2011-299400]
Recent advances in computational design have enabled the development of primitive enzymes for a range of mechanistically distinct reactions. Here we show that the rudimentary active sites of these catalysts can give rise to useful chemical promiscuity. Specifically, RA95.5-8, designed and evolved as a retro-aldolase, also promotes asymmetric Michael additions of carbanions to unsaturated ketones with high rates and selectivities. The reactions proceed by amine catalysis, as indicated by mutagenesis and X-ray data. The inherent flexibility and tunability of this catalyst should make it a versatile platform for further optimization and/or mechanistic diversification by directed evolution.
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