ArticleOrganic & biomolecular chemistry2021
The broad amine scope of pantothenate synthetase enables the synthesis of pharmaceutically relevant amides.
Article in Organic & biomolecular chemistry, 2021. 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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2 citing papers in PubMed, 8 citations in OpenAlex.
- Amide and Thioester Synthesis Via Oxidative Coupling of Alcohols with Amines or Thiols Using Alcohol Dehydrogenases.Angewandte Chemie (International ed. in English) · 2026Article
- One-Step Biocatalytic Synthesis of Sustainable Surfactants by Selective Amide Bond Formation.Angewandte Chemie (International ed. in English) · 2022Article
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4 authors at 3 institutions in 4 countries.
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Abstract
Pantothenate synthetase from Escherichia coli (PSE. coli) catalyzes the ATP-dependent condensation of (R)-pantoic acid and β-alanine to yield (R)-pantothenic acid (vitamin B5), the biosynthetic precursor to coenzyme A. Herein we show that besides the natural amine substrate β-alanine, the enzyme accepts a wide range of structurally diverse amines including 3-amino-2-fluoropropionic acid, 4-amino-2-hydroxybutyric acid, 4-amino-3-hydroxybutyric acid, and tryptamine for coupling to the native carboxylic acid substrate (R)-pantoic acid to give amide products with up to >99% conversion. The broad amine scope of PSE. coli enabled the efficient synthesis of pharmaceutically-relevant vitamin B5 antimetabolites with excellent isolated yield (up to 89%). This biocatalytic amide synthesis strategy may prove to be useful in the quest for new antimicrobials that target coenzyme A biosynthesis and utilisation.
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