A ThDP-Dependent Enzyme with a Broad Nucleophilic Substrate Spectrum: Stereoselective Carboligation Reactions Catalyzed by <i>Escherichia coli</i> SucA
Most bioactive molecules possess complex structures with multiple functionalities and chiral centers. Consequently, their synthesis often involves numerous steps, leading to low overall yields. An eco-friendly solution is to use the <i>Ec</i>SucA enzyme, which facilitates the highly selective formation of C-C bonds, providing access to complex multifunctional motifs. Thanks to the unusual broad substrate spectrum of this carboligase, various chiral δ-hydroxy-γ-ketoacids could be produced in a single step, demonstrating that <i>Ec</i>SucA can be efficiently integrated into total synthesis pathways.
Authors
- Marielle Lemaire (ORCID: https://orcid.org/0000-0001-5763-9209)
- Virgil Hélaine (ORCID: https://orcid.org/0000-0001-8446-7924)
- Thierry Gefflaut (ORCID: https://orcid.org/0000-0002-4411-8233)
- A. Afonso
- W. Dai
- Michel Müller
- Véronique de Bérardinis
- Christine Guérard-Hélaine
- Jean-Louis Petit
Institutions
- Centre National de la Recherche Scientifique (FR)
- University of Freiburg (DE)
- Commissariat à l'Énergie Atomique et aux Énergies Alternatives (FR)
- Université Paris-Saclay (FR)
- Génomique Métabolique du Genoscope (FR)
- Genoscope (FR)
- Sigma Clermont (FR)
- CEA Paris-Saclay (FR)
- Clermont Université (FR)
Publication Details
- Journal
- The Journal of Organic Chemistry
- Published
- 2026-01-05
- DOI
- https://doi.org/10.1021/acs.joc.5c02017
- Primary Topic
- Biochemical Acid Research Studies
- Type
- article
- Field-Weighted Citation Impact
- 0.00