6YC8

Crystal structure of KRED1-Pglu enzyme

Summary for 6YC8

• Entry DOI: 10.2210/pdb6yc8/pdb
• Descriptor: Ketoreductase, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ACETATE ION, ... (8 entities in total)
• Functional Keywords: ketoreductase, carbonyl reductase, pichia glucozyma, enantioselective reduction biocatalysis, oxidoreductase
• Biological source: Ogataea glucozyma
• Total number of polymer chains: 1
• Total formula weight: 31097.94

Authors

Di Pisa, F. (deposition date: 2020-03-18, release date: 2021-02-10, Last modification date: 2024-01-24)

Primary citation

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., 108:104644-104644, 2021

PubMed Abstract: 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.

PubMed: 33486371
DOI: 10.1016/j.bioorg.2021.104644

Experimental method

X-RAY DIFFRACTION (1.77 Å)