Structural highlights
Publication Abstract from PubMed
Cupin superfamily proteins (TM1459) work as a macromolecular ligand framework with a double-stranded beta-barrel structure ligating to a Cu ion through histidine side chains. Variegating the first coordination sphere of TM1459 revealed that H52A and H54A/H58A mutants effectively catalyzed the diastereo- and enantioselective Michael addition reaction of nitroalkanes to an alpha,beta-unsaturated ketone. Moreover, calculated substrate docking signified C106N and F104W single-point mutations, which inverted the diastereoselectivity of H52A and further improved the stereoselectivity of H54A/H58A, respectively.
Cupin Variants as a Macromolecular Ligand Library for Stereoselective Michael Addition of Nitroalkanes.,Fujieda N, Ichihashi H, Yuasa M, Nishikawa Y, Kurisu G, Itoh S Angew Chem Int Ed Engl. 2020 Feb 19. doi: 10.1002/anie.202000129. PMID:32073197[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Fujieda N, Ichihashi H, Yuasa M, Nishikawa Y, Kurisu G, Itoh S. Cupin Variants as a Macromolecular Ligand Library for Stereoselective Michael Addition of Nitroalkanes. Angew Chem Int Ed Engl. 2020 Feb 19. doi: 10.1002/anie.202000129. PMID:32073197 doi:http://dx.doi.org/10.1002/anie.202000129
