ReviewChembiochem : a European journal of chemical biology2025
Diversity of ThDP-Dependent Enzymes Forming Chiral Tertiary Alcohols.
Review in Chembiochem : a European journal of chemical biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed.
- C2α-carbanion-protonating glutamate discloses tradeoffs between substrate accommodation and reaction rate in actinobacterial 2-hydroxyacyl-CoA lyase.FEBS open bio · 2026Article
- Biocatalytic Regioselective C-Formylation of Resorcinol Derivatives.Angewandte Chemie (International ed. in English) · 2026Article
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5 authors.
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Abstract
Thiamine diphosphate (ThDP)-dependent enzymes are well known biocatalysts for CC bond-forming reactions. While this enzyme class is mainly investigated for the formation of acyloins of secondary alcohols, recent studies have expanded its scope to utilize ketones as electrophiles in asymmetric carboligation reactions for the formation of tertiary alcohols. Chiral tertiary alcohols are ubiquitous motifs in natural products and important building blocks for the synthesis of bioactive compounds. ThDP-dependent enzymes are emerging as one of the most promising classes of biocatalysts for synthesizing a wide range of products due to the variety of possible substrate combinations, accessible starting materials, high enantioselectivity, and advantageous self-regeneration of the catalytic ThDP cofactor. This review provides an overview of the ThDP-dependent enzymes (e.g., decarboxylase, DC; transketolase, TK; α-keto acid dehydrogenase 2, αKADH2) that form tertiary alcohols, focusing on the substrate scope and diversity of physiological functions. The available toolbox and the characterized reactions shall serve as a starting point for future studies. Inspired by nature, an even broader diversity of classes and substrate specificities is expected in this field.
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