ArticleNature communications2017
An L-threonine transaldolase is required for L-threo-β-hydroxy-α-amino acid assembly during obafluorin biosynthesis.
Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed, 103 citations in OpenAlex.
- Retention and biosynthesis of diverse nitroarenes in Escherichia coli after combinatorial nitroreductase gene deletions.Nature chemistry · 2026Article
- Cytochrome P450- and Dehydrogenase-Mediated Regiospecific and Stereoselective Formation of β- and γ-Lactones in Drimane-Type Sesquiterpenoid Biosynthesis.Journal of the American Chemical Society · 2026Article
- A novel stress response pathway mediates biofilm architecture in Pseudomonas aeruginosa.PLoS pathogens · 2026Article
- Combined biosynthesis and site-specific incorporation of phenylalanine derivatives from aryl aldehydes or carboxylic acids.Nature communications · 2026Article
- Cyclic-di-GMP controls Type III effector export and symptom development in Pseudomonas syringae infections via the export ATPase HrcN.PLoS pathogens · 2025Article
- Enhanced Stereochemical Analysis of β‑Diastereomeric Amino Acids with Variants of Marfey's Reagent.ACS omega · 2025Article
- Chemoenzymatic Cascade Synthesis of Metal-ChelatingChemCatChem · 2025Article
- A recombinant L-threonine aldolase with high catalytic efficiency for the asymmetric synthesis of L-threo-phenylserine and L-threo-4-fluorophenylserine.Biotechnology letters · 2024Article
- Biocatalytic asymmetric aldol addition into unactivated ketones.Nature chemistry · 2024Article
- Occupational modulation in the (3+1)-dimensional incommensurate structure of (2S,3S)-2-amino-3-hydroxy-3-methyl-4-phenoxybutanoic acid dihydrate.Acta crystallographica. Section C, Structural chemistry · 2024Article
- Decarboxylation in Natural Products Biosynthesis.JACS Au · 2024Review
- Cell-Free Systems: Ideal Platforms for Accelerating the Discovery and Production of Peptide-Based Antibiotics.International journal of molecular sciences · 2024Review
- Specific glycine-dependent enzyme motion determines the potency of conformation selective inhibitors of threonyl-tRNA synthetase.Communications biology · 2024Article
- Natural Products That Contain Higher Homologated Amino Acids.Chembiochem : a European journal of chemical biology · 2024Review
- Article
- The genotype of barley cultivars influences multiple aspects of their associated microbiota via differential root exudate secretion.PLoS biology · 2024Article
- Genomic insights and biocontrol potential of ten bacterial strains from the tomato core microbiome.Frontiers in plant science · 2024Article
- The catechol moiety of obafluorin is essential for antibacterial activity.RSC chemical biology · 2023Article
- Structural advances toward understanding the catalytic activity and conformational dynamics of modular nonribosomal peptide synthetases.Natural product reports · 2023Review
- Discovery of L-threonine transaldolases for enhanced biosynthesis of beta-hydroxylated amino acids.Communications biology · 2023Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
β-Lactone natural products occur infrequently in nature but possess a variety of potent and valuable biological activities. They are commonly derived from β-hydroxy-α-amino acids, which are themselves valuable chiral building blocks for chemical synthesis and precursors to numerous important medicines. However, despite a number of excellent synthetic methods for their asymmetric synthesis, few effective enzymatic tools exist for their preparation. Here we report cloning of the biosynthetic gene cluster for the β-lactone antibiotic obafluorin and delineate its biosynthetic pathway. We identify a nonribosomal peptide synthetase with an unusual domain architecture and an L-threonine:4-nitrophenylacetaldehyde transaldolase responsible for (2S,3R)-2-amino-3-hydroxy-4-(4-nitrophenyl)butanoate biosynthesis. Phylogenetic analysis sheds light on the evolutionary origin of this rare enzyme family and identifies further gene clusters encoding L-threonine transaldolases. We also present preliminary data suggesting that L-threonine transaldolases might be useful for the preparation of L-threo-β-hydroxy-α-amino acids.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.