ArticleNature chemistry2019
Modification and de novo design of non-ribosomal peptide synthetases using specific assembly points within condensation domains.
Article in Nature chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 79 papers, 2 of them syntheses that pooled it.
What it found
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Who cites it
79 citing papers in PubMed, 2 syntheses or guidelines pooled it.
- A Practical Guideline to Engineering Nonribosomal Peptide Synthetases.Methods in molecular biology (Clifton, N.J.) · 2023Guideline
- The Surfactin-Like Lipopeptides FromFrontiers in bioengineering and biotechnology · 2021Pooled it
- Reprogramming the enduracidin NRPS assembly line via thioesterase domain relocation.Synthetic and systems biotechnology · 2027Article
- Generative AI designs functional thiolation domains for reprogramming non-ribosomal peptide synthetases.Nature communications · 2026Article
- Heterologous expression of NRPS and PKS pathways in Escherichia coli: from bottlenecks to biosynthetic platforms.Essays in biochemistry · 2026Review
- Alternative enzymatic pathways to penicillin antibiotics.Nature communications · 2026Article
- Recent Advancements for Enhanced Biocatalyst and Biotransformation.Molecular biotechnology · 2026Review
- High-Throughput Engineering and Modification of Non-Ribosomal Peptide Synthetases Based on Golden Gate Assembly.Angewandte Chemie (International ed. in English) · 2025Article
- Protein Engineering of Biosynthetic Enzymes Unlocks Libraries of Bioactive Tilimycin Analogs.ACS catalysis · 2025Article
- Mixing and Matching of Hybrid Megasynthases is a Hub for the Evolution of Metabolic Diversity in Cyanobacteria.Angewandte Chemie (International ed. in English) · 2025Article
- Synthetic Biology in Natural Product Biosynthesis.Chemical reviews · 2025Review
- Engineering the future of medicine: Natural products, synthetic biology and artificial intelligence for next-generation therapeutics.Clinical and translational medicine · 2025Review
- Article
- 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
- Advances, opportunities, and challenges in methods for interrogating the structure activity relationships of natural products.Natural product reports · 2024Review
- Cryptic enzymatic assembly of peptides armed with β-lactone warheads.Nature chemical biology · 2024Article
- Natural diversifying evolution of nonribosomal peptide synthetases in a defensive symbiont reveals nonmodular functional constraints.PNAS nexus · 2024Article
- Functional Diversity and Engineering of the Adenylation Domains in Nonribosomal Peptide Synthetases.Marine drugs · 2024Review
19 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Non-ribosomal peptide synthetases (NRPSs) are giant enzyme machines that activate amino acids in an assembly line fashion. As NRPSs are not restricted to the incorporation of the 20 proteinogenic amino acids, their efficient manipulation would enable microbial production of a diverse range of peptides; however, the structural requirements for reprogramming NRPSs to facilitate the production of new peptides are not clear. Here we describe a new fusion point inside the condensation domains of NRPSs that results in the development of the exchange unit condensation domain (XUC) concept, which enables the efficient production of peptides, even containing non-natural amino acids, in yields up to 280 mg l
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Registered trials
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.