Structural insights into the desymmetrization of bulky 1,2-dicarbonyls through enzymatic monoreduction.
Biocatalysis
Crystal structure
Enzymatic reduction
In silico analysis
Ketoreductase
Pichia glucozyma
Journal
Bioorganic chemistry
ISSN: 1090-2120
Titre abrégé: Bioorg Chem
Pays: United States
ID NLM: 1303703
Informations de publication
Date de publication:
03 2021
03 2021
Historique:
received:
28
12
2020
revised:
05
01
2021
accepted:
06
01
2021
pubmed:
25
1
2021
medline:
1
10
2021
entrez:
24
1
2021
Statut:
ppublish
Résumé
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.
Identifiants
pubmed: 33486371
pii: S0045-2068(21)00020-1
doi: 10.1016/j.bioorg.2021.104644
pii:
doi:
Substances chimiques
Aldehydes
0
Alcohol Oxidoreductases
EC 1.1.-
benzil reductase
EC 1.1.1.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
104644Informations de copyright
Copyright © 2021 Elsevier Inc. All rights reserved.