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Updated: Jan 7, 2026

Overexpression and Purification of Human Cis-prenyltransferase in Escherichia coli
Published on: August 3, 2017
A ThDP-Dependent Enzyme with a Broad Nucleophilic Substrate Spectrum: Stereoselective Carboligation Reactions
Weichao Dai1, Anissa Afonso1, Virgil Hélaine1
1Institut de Chimie de Clermont-Ferrand Université Clermont Auvergne, CNRS, Clermont-Auvergne INP, 63000 Clermont-Ferrand, France.
Abstract:
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 EcSucA 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 EcSucA can be efficiently integrated into total synthesis pathways.
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