ArticleNature chemistry2018
Nonribosomal biosynthesis of backbone-modified peptides.
Article in Nature chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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Who cites it
50 citing papers in PubMed.
- Scaling SMILES-based chemical language models for therapeutic peptide engineering.bioRxiv : the preprint server for biology · 2026Article
- Mapping the nonribosomal specificity code through promiscuity-guided A-domain engineering.Chemical science · 2026Article
- Directed Evolution of Enzymes for Bioorthogonal Chemistry Using Acid Chloride Proximity Labeling.ACS central science · 2026Article
- Guidelines for High-Throughput Engineering of Nonribosomal Peptide Synthetase Libraries.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Computation-driven redesign of an NRPS-like carboxylic acid reductase improves activity and selectivity.Science advances · 2024Article
- Structure, Function and Engineering of the Nonribosomal Peptide Synthetase Condensation Domain.International journal of molecular sciences · 2024Review
- Spiers Memorial Lecture: Engineering biocatalysts.Faraday discussions · 2024Article
- Cell-Free Systems: Ideal Platforms for Accelerating the Discovery and Production of Peptide-Based Antibiotics.International journal of molecular sciences · 2024Review
- Structural, biochemical and bioinformatic analyses of nonribosomal peptide synthetase adenylation domains.Natural product reports · 2024Review
- High-throughput engineering of biosynthetic assembly lines.Nature chemical biology · 2024Article
- High-throughput reprogramming of an NRPS condensation domain.Nature chemical biology · 2024Article
- Incorporation of Multiple βACS central science · 2024Article
- Controlling Substrate- and Stereospecificity of Condensation Domains in Nonribosomal Peptide Synthetases.ACS chemical biology · 2024Article
- Article
- High-Throughput Engineering of Nonribosomal Extension Modules.ACS chemical biology · 2023Article
- Resurrecting ancestral antibiotics: unveiling the origins of modern lipid II targeting glycopeptides.Nature communications · 2023Article
- Repurposing conformational changes in ANL superfamily enzymes to rapidly generate biosensors for organic and amino acids.Nature communications · 2023Article
- Biosynthetic incorporation of fluorinated amino acids into the nonribosomal peptide gramicidin S.RSC chemical biology · 2023Article
- Microbial synthesis of bacitracin: Recent progress, challenges, and prospects.Synthetic and systems biotechnology · 2023Review
- Synthesis of functionalized 2,3-diaminopropionates and their potential for directed monobactam biosynthesis.Chemical science · 2023Article
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6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Biosynthetic modification of nonribosomal peptide backbones represents a potentially powerful strategy to modulate the structure and properties of an important class of therapeutics. Using a high-throughput assay for catalytic activity, we show here that an L-Phe-specific module of an archetypal nonribosomal peptide synthetase can be reprogrammed to accept and process the backbone-modified amino acid (S)-β-Phe with near-native specificity and efficiency. A co-crystal structure with a non-hydrolysable aminoacyl-AMP analogue reveals the origins of the 40,000-fold α/β-specificity switch, illuminating subtle but precise remodelling of the active site. When the engineered catalyst was paired with downstream module(s), (S)-β-Phe-containing peptides were produced at preparative scale in vitro (~1 mmol) and high titres in vivo (~100 mg l
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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.