8xyn
From Proteopedia
Structure of the engineered retro-aldolase RA95.5-8
Structural highlights
Publication Abstract from PubMedThe introduction of an abiological catalytic group into the binding pocket of a protein host allows for the expansion of enzyme chemistries. Here, we report the generation of an artificial enzyme by genetic encoding of a non-canonical amino acid that contains a secondary amine side chain. The non-canonical amino acid and the binding pocket function synergistically to catalyze the asymmetric nitrocyclopropanation of alpha,beta-unsaturated aldehydes by the iminium activation mechanism. The designer enzyme was evolved to an optimal variant that catalyzes the reaction at high conversions with high diastereo- and enantioselectivity. This work demonstrates the application of genetic code expansion in enzyme design and expands the scope of enzyme-catalyzed abiological reactions. An Artificial Enzyme for Asymmetric Nitrocyclopropanation of alpha,beta-Unsaturated Aldehydes-Design and Evolution.,Yu MZ, Yuan Y, Li ZJ, Kunthic T, Wang HX, Xu C, Xiang Z Angew Chem Int Ed Engl. 2024 Jun 17;63(25):e202401635. doi: , 10.1002/anie.202401635. Epub 2024 May 14. PMID:38597773[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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