Enantiocomplementary enzymes: classification, molecular basis for their enantiopreference, and prospects for mirror-image biotransformations.

Angew Chem Int Ed Engl

Department of Biochemistry, Molecular Biology & Biophysics and the Biotechnology Institute, University of Minnesota, 1479 Gortner Avenue, Saint Paul, MN 55108, USA.

Published: December 2008

One often-cited weakness of biocatalysis is the lack of mirror-image enzymes for the formation of either enantiomer of a product in asymmetric synthesis. Enantiocomplementary enzymes exist as the solution to this problem in nature. These enzyme pairs, which catalyze the same reaction but favor opposite enantiomers, are not mirror-image molecules; however, they contain active sites that are functionally mirror images of one another. To create mirror-image active sites, nature can change the location of the binding site and/or the location of key catalytic groups. In this Minireview, X-ray crystal structures of enantiocomplementary enzymes are surveyed and classified into four groups according to how the mirror-image active sites are formed.

Download full-text PDF

Source
http://dx.doi.org/10.1002/anie.200705159DOI Listing

Publication Analysis

Top Keywords

enantiocomplementary enzymes
12
active sites
12
mirror-image active
8
mirror-image
5
enzymes classification
4
classification molecular
4
molecular basis
4
basis enantiopreference
4
enantiopreference prospects
4
prospects mirror-image
4

Similar Publications

Aldolases, especially 2-deoxyribose-5-phosphate aldolase (DERA) enzymes, have been widely employed to access key chiral precursors for various active pharmaceutical ingredients (APIs). This has been enabled by expanding their substrate scope toward non-natural acceptors and donors via protein engineering. In this study, we endeavored to broaden the acceptor substrate scope of DERA from sp.

View Article and Find Full Text PDF

Taming highly enolizable aldehydes for catalytic asymmetric C-C coupling with nucleophiles remains an elusive challenge compared to widely explored simple alkyl or aryl aldehydes. Herein, we use ThDP-dependent enzymes to realize the direct C-C coupling of highly enolizable 2-phosphonate aldehydes with in situ-generated dynamically reversible nucleophiles (acyl anions). Unlike NHC-mediated reactions that yield complex mixtures of multiple adducts, our enzymatic process selectively produces biologically active β-hydroxy phosphonates with high yields (up to 95%) and excellent enantioselectivities (up to 99% ee).

View Article and Find Full Text PDF
Article Synopsis
  • The study introduces CoNSA-POase, an artificial peroxygenase made from single-atom cobalt supported on polymeric carbon nitrogen, which shows excellent performance in converting aromatic alkanes to ketones.
  • Density functional theory indicates that this artificial enzyme operates via a different catalytic mechanism compared to natural peroxygenases.
  • The integration of CoNSA-POase with other enzymes in continuous-flow systems enhances the efficient production of chiral alcohols and amines, suggesting potential advancements in enzyme-based applications.
View Article and Find Full Text PDF

Enantiopure 1,2-diols are widely used in the production of pharmaceuticals, cosmetics, and functional materials as essential building blocks or bioactive compounds. Nevertheless, developing a mild, efficient and environmentally friendly biocatalytic route for manufacturing enantiopure 1,2-diols from simple substrate remains a challenge. Here, we designed and realized a step-wise biocatalytic cascade to access chiral 1,2-diols starting from aromatic aldehyde and formaldehyde enabled by a newly mined benzaldehyde lyase from Sphingobium sp.

View Article and Find Full Text PDF

Less steric ketones exhibited low stereoselectivity toward M5 due to their difficulty in restricting the free rotation of the imine intermediate. An engineered enantio-complementary imine reductase from M5 was obtained with catalytic activity. We identified four key residues that play essential roles in controlling stereoselectivity.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!