Structural highlights
Publication Abstract from PubMed
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.
A Promiscuous De Novo Retro-Aldolase Catalyzes Asymmetric Michael Additions via Schiff Base Intermediates.,Garrabou X, Beck T, Hilvert D Angew Chem Int Ed Engl. 2015 Mar 16. doi: 10.1002/anie.201500217. PMID:25777153[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Garrabou X, Beck T, Hilvert D. A Promiscuous De Novo Retro-Aldolase Catalyzes Asymmetric Michael Additions via Schiff Base Intermediates. Angew Chem Int Ed Engl. 2015 Mar 16. doi: 10.1002/anie.201500217. PMID:25777153 doi:http://dx.doi.org/10.1002/anie.201500217
