%0 Journal Article
%A Rabuffetti, Marco
%A Cannazza, Pietro
%A Contente, Martina Letizia 
%A Pinto, Andrea 
%A Romano, Diego 
%A Hoyos Vidal, María Pilar
%A Alcántara León, Andrés Rafael
%A Eberini, Ivano 
%A Laurenzi, Tommaso 
%A Gourlay, Louise 
%A Di Pisa, Flavio 
%A Molinari, Francesco 
%T Structural insights into the desymmetrization of bulky 1,2-dicarbonyls through enzymatic monoreduction
%D 2021
%@ 0045-2068
%U https://hdl.handle.net/20.500.14352/96618
%X Benzil 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.
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