ArticleACS chemical biology2024
Controlling Substrate- and Stereospecificity of Condensation Domains in Nonribosomal Peptide Synthetases.
Article in ACS chemical biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Generative AI designs functional thiolation domains for reprogramming non-ribosomal peptide synthetases.Nature communications · 2026Article
- Structure of a stand-alone homodimeric nonribosomal peptide synthetase condensation domain reveals occlusion of the canonical carrier-protein interface.The Journal of biological chemistry · 2026Article
- Bacillus-derived antimicrobial peptides as alternatives to antibiotics in poultry: mechanisms, applications, and future prospects- a review.Archives of microbiology · 2026Review
- Structure of a Stand-Alone Homodimeric NRPS Condensation Domain Reveals Occlusion of the Canonical Carrier-Protein Interface.bioRxiv : the preprint server for biology · 2026Article
- All you need is fungi: Exploring secondary metabolites as a source of novel amoebicidal agents.Genetics and molecular biology · 2026Article
- Structural Basis for a Scaffolding Role of the COM Domain in Nonribosomal Peptide Synthetases.Angewandte Chemie (International ed. in English) · 2025Article
- Gene conversion-associated successive engineering of modular polyketide synthases.Communications chemistry · 2025Article
- Expanding the Substrate Selectivity of the Fimsbactin Biosynthetic Adenylation Domain, FbsH.ACS chemical biology · 2024Article
- Structure, Function and Engineering of the Nonribosomal Peptide Synthetase Condensation Domain.International journal of molecular sciences · 2024Review
- Expanding the substrate selectivity of the fimsbactin biosynthetic adenylation domain, FbsH.bioRxiv : the preprint server for biology · 2024Article
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Authors and funding
5 authors.
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Abstract
Nonribosomal peptide synthetases (NRPSs) are sophisticated molecular machines that biosynthesize peptide drugs. In attempts to generate new bioactive compounds, some parts of NRPSs have been successfully manipulated, but especially the influence of condensation (C-)domains on substrate specificity remains enigmatic and poorly controlled. To understand the influence of C-domains on substrate preference, we extensively evaluated the peptide formation of C-domain mutants in a bimodular NRPS system. Thus, we identified three key mutations that govern the preference for stereoconfiguration and side-chain identity. These mutations show similar effects in three different C-domains (GrsB1, TycB1, and SrfAC) when di- or pentapeptides are synthesized
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