Molinari, FrancescoRabuffetti, MarcoCannazza, PietroContente, Martina LetiziaPinto, AndreaRomano, DiegoHoyos Vidal, María PilarAlcántara León, Andrés RafaelEberini, IvanoLaurenzi, TommasoGourlay, LouiseDi Pisa, FlavioMolinari, FrancescoElsevier2024-01-302024-01-302021-01-11Rabuffetti, M.; Cannazza, P.: Contente, M. L.; Pinto, A.; Romano, D.; Hoyos, P.; Alcantara, A. R.; Eberini, I.; Laurenzi, T.; Gourlay, L.; Di Pisa, F.; Molinari, F., Structural insights into the desymmetrization of bulky 1,2-dicarbonyls through enzymatic monoreduction Bioorg. Chem. 2021, 108, 1046440045-206810.1016/j.bioorg.2021.104644https://hdl.handle.net/20.500.14352/96618Benzil reductases are dehydrogenases preferentially active on aromatic 1,2-diketones, but the reasons for this peculiar substrate recognition have not yet been clarified. The benzil reductase (KRED1-Pglu) from the non conventional yeast Pichia glucozyma showed excellent activity and stereoselectivity in the monoreduction of space-demanding aromatic 1,2-dicarbonyls, making this enzyme attractive as biocatalyst in organic chemistry. Structural insights into the stereoselective monoreduction of 1,2-diketones catalyzed by KRED1-Pglu were investigated starting from its 1.77 Å resolution crystal structure, followed by QM and classical calculations; this study allowed for the identification and characterization of the KRED1-Pglu reactive site. Once identified the recognition elements involved in the stereoselective desymmetrization of bulky 1,2-dicarbonyls mediated by KRED1-Pglu, a mechanism was proposed together with an in silico prediction of substrates reactivity.engjournal articlehttps://doi.org/10.1016/j.bioorg.2021.104644restricted accessBiocatalysis, Ketoreductase, Pichia glucozyma, Enzymatic reduction, Crystal structure, In silico analysisCiencias Biomédicas23 Química