期刊
ORGANIC & BIOMOLECULAR CHEMISTRY
卷 19, 期 20, 页码 4515-4519出版社
ROYAL SOC CHEMISTRY
DOI: 10.1039/d1ob00238d
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资金
- Netherlands Organization of Scientific Research (VICI grant) [724.016.002]
- European Research Council (PoC grant) [713483]
- Indonesia Endowment Fund for Education (LPDP)
- European Research Council (ERC) [713483] Funding Source: European Research Council (ERC)
Pantothenate synthetase from Escherichia coli can efficiently synthesize pharmaceutically-relevant vitamin B-5 antimetabolites by accepting a wide range of structurally diverse amines in addition to its natural amine substrate, beta-alanine. This biocatalytic amide synthesis strategy shows promise in the search for new antimicrobials targeting coenzyme A biosynthesis and utilization.
Pantothenate synthetase from Escherichia coli (PSE. coli) catalyzes the ATP-dependent condensation of (R)-pantoic acid and beta-alanine to yield (R)-pantothenic acid (vitamin B-5), the biosynthetic precursor to coenzyme A. Herein we show that besides the natural amine substrate beta-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 B-5 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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