ArticleAngewandte Chemie (International ed. in English)2020
Artificial Splitting of a Non-Ribosomal Peptide Synthetase by Inserting Natural Docking Domains.
Article in Angewandte Chemie (International ed. in English), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 35 citations in OpenAlex.
- Controlling Megasynthetase Module-Module Interactions through β-Hairpin Docking Domain Engineering.ACS chemical biology · 2025Article
- High-Throughput Engineering and Modification of Non-Ribosomal Peptide Synthetases Based on Golden Gate Assembly.Angewandte Chemie (International ed. in English) · 2025Article
- Comparative Analysis of Signature Sequences from Adenylation Domains Situated within Bacterial-Origin Nonribosomal Peptide Synthetase Modules.Journal of microbiology and biotechnology · 2025Article
- Structure, Function and Engineering of the Nonribosomal Peptide Synthetase Condensation Domain.International journal of molecular sciences · 2024Review
- ExploringMolecules (Basel, Switzerland) · 2024Review
- The specificity of intermodular recognition in a prototypical nonribosomal peptide synthetase depends on an adaptor domain.Science advances · 2024Article
- Diversity, Biosynthesis and Bioactivity of Aeruginosins, a Family of Cyanobacteria-Derived Nonribosomal Linear Tetrapeptides.Marine drugs · 2023Review
- Engineering of Specific Single-Module Nonribosomal Peptide Synthetases of the RXP Type for the Production of Defined Peptides.ACS synthetic biology · 2023Article
- Proof-Reading Thioesterase Boosts Activity of Engineered Nonribosomal Peptide Synthetase.ACS chemical biology · 2022Article
- Deletion of COM donor and acceptor domains and the interaction between modules in bacillomycin D produced bySynthetic and systems biotechnology · 2022Article
- Macrophage-targeting oligopeptides fromChemical science · 2022Article
- Recent Advances in Biocatalysis for Drug Synthesis.Biomedicines · 2022Review
- Biosynthesis of Fungal Natural Products Involving Two Separate Pathway Crosstalk.Journal of fungi (Basel, Switzerland) · 2022Review
- Complex peptide natural products: Biosynthetic principles, challenges and opportunities for pathway engineering.Synthetic and systems biotechnology · 2022Article
- Nematophilic bacteria associated with entomopathogenic nematodes and drug development of their biomolecules.Frontiers in microbiology · 2022Review
- Synthetic Zippers as an Enabling Tool for Engineering of Non-Ribosomal Peptide Synthetases*.Angewandte Chemie (International ed. in English) · 2021Article
- Cooperation between a T Domain and a Minimal C-Terminal Docking Domain to Enable Specific Assembly in a Multiprotein NRPS.Angewandte Chemie (International ed. in English) · 2021Article
- Docking domain-mediated subunit interactions in natural product megasynth(et)ases.Journal of industrial microbiology & biotechnology · 2021Review
- The inherent flexibility of type I non-ribosomal peptide synthetase multienzymes drives their catalytic activities.Open biology · 2021Review
- Exploring modular reengineering strategies to redesign the teicoplanin non-ribosomal peptide synthetase.Chemical science · 2020Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The interaction in multisubunit non-ribosomal peptide synthetases (NRPSs) is mediated by docking domains that ensure the correct subunit-to-subunit interaction. We introduced natural docking domains into the three-module xefoampeptide synthetase (XfpS) to create two to three artificial NRPS XfpS subunits. The enzymatic performance of the split biosynthesis was measured by absolute quantification of the products by HPLC-ESI-MS. The connecting role of the docking domains was probed by deleting integral parts of them. The peptide production data was compared to soluble protein amounts of the NRPS using SDS-PAGE. Reduced peptide synthesis was not a result of reduced soluble NRPS concentration but a consequence of the deletion of vital docking domain parts. Splitting the xefoampeptide biosynthesis polypeptide by introducing docking domains was feasible and resulted in higher amounts of product in one of the two tested split-module cases compared to the full-length wild-type enzyme.
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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.