Structural highlights
FunctionPublication Abstract from PubMedBenzil 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 A 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. Structural insights into the desymmetrization of bulky 1,2-dicarbonyls through enzymatic monoreduction.,Rabuffetti M, Cannazza P, Contente ML, Pinto A, Romano D, Hoyos P, Alcantara AR, Eberini I, Laurenzi T, Gourlay L, Di Pisa F, Molinari F Bioorg Chem. 2021 Jan 11;108:104644. doi: 10.1016/j.bioorg.2021.104644. PMID:33486371[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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