RT Journal Article
T1 Structural insights into the desymmetrization of bulky 1,2-dicarbonyls through enzymatic monoreduction
A1 Rabuffetti, Marco
A1 Cannazza, Pietro
A1 Contente, Martina Letizia
A1 Pinto, Andrea
A1 Romano, Diego
A1 Hoyos Vidal, María Pilar
A1 Alcántara León, Andrés Rafael
A1 Eberini, Ivano
A1 Laurenzi, Tommaso
A1 Gourlay, Louise
A1 Di Pisa, Flavio
A1 Molinari, Francesco
A2 Elsevier, 
AB 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.
PB Elsevier
SN 0045-2068
YR 2021
FD 2021-01-11
LK https://hdl.handle.net/20.500.14352/96618
UL https://hdl.handle.net/20.500.14352/96618
LA eng
NO Rabuffetti, 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, 104644
DS Docta Complutense
RD 9 abr 2025