ArticleApplied and environmental microbiology2014
Biosynthesis of novel Pyoverdines by domain substitution in a nonribosomal peptide synthetase of Pseudomonas aeruginosa.
Article in Applied and environmental microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 83 citations in OpenAlex.
- Generative AI designs functional thiolation domains for reprogramming non-ribosomal peptide synthetases.Nature communications · 2026Article
- High-Throughput Engineering and Modification of Non-Ribosomal Peptide Synthetases Based on Golden Gate Assembly.Angewandte Chemie (International ed. in English) · 2025Article
- Cyanobacterial Peptides in Anticancer Therapy: A Comprehensive Review of Mechanisms, Clinical Advances, and Biotechnological Innovation.Marine drugs · 2025Review
- Guidelines for High-Throughput Engineering of Nonribosomal Peptide Synthetase Libraries.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Structure, Function and Engineering of the Nonribosomal Peptide Synthetase Condensation Domain.International journal of molecular sciences · 2024Review
- Functional Diversity and Engineering of the Adenylation Domains in Nonribosomal Peptide Synthetases.Marine drugs · 2024Review
- Biosynthesis of a clickable pyoverdine via in vivo enzyme engineering of an adenylation domain.Microbial cell factories · 2024Article
- Metagenomic domain substitution for the high-throughput modification of nonribosomal peptides.Nature chemical biology · 2024Article
- Total substitution and partial modification of the set of non-ribosomal peptide synthetases clusters lead to pyoverdine diversity in theFrontiers in microbiology · 2024Article
- High-Throughput Engineering of Nonribosomal Extension Modules.ACS chemical biology · 2023Article
- Hydrocarbon degradation strategy and pyoverdine production using the salt tolerant Antarctic bacteriumRSC advances · 2023Article
- Engineering Siderophore Biosynthesis and Regulation Pathways to Increase Diversity and Availability.Biomolecules · 2023Review
- Novel Insights on Pyoverdine: From Biosynthesis to Biotechnological Application.International journal of molecular sciences · 2022Review
- Deletion of COM donor and acceptor domains and the interaction between modules in bacillomycin D produced bySynthetic and systems biotechnology · 2022Article
- Nonribosomal peptide synthetases and their biotechnological potential in Penicillium rubens.Journal of industrial microbiology & biotechnology · 2021Review
- Targeted SPION siderophore conjugate loaded with doxorubicin as a theranostic agent for imaging and treatment of colon carcinoma.Scientific reports · 2021Article
- Efficient rational modification of non-ribosomal peptides by adenylation domain substitution.Nature communications · 2020Article
- Repurposing Modular Polyketide Synthases and Non-ribosomal Peptide Synthetases for Novel Chemical Biosynthesis.Frontiers in molecular biosciences · 2020Review
- Inter-Modular Linkers play a crucial role in governing the biosynthesis of non-ribosomal peptides.Bioinformatics (Oxford, England) · 2019Article
- Modification and de novo design of non-ribosomal peptide synthetases using specific assembly points within condensation domains.Nature chemistry · 2019Article
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Pyoverdine is a fluorescent nonribosomal peptide siderophore made by fluorescent pseudomonads. The Pseudomonas aeruginosa nonribosomal peptide synthetase (NRPS) PvdD contains two modules that each incorporate an l-threonine residue at the C-terminal end of pyoverdine. In an attempt to generate modified pyoverdine peptides, we substituted alternative-substrate-specifying adenylation (A) and peptide bond-catalyzing condensation (C) domains into the second module of PvdD. When just the A domain was substituted, the resulting strains produced only wild-type pyoverdine-at high levels if the introduced A domain specified threonine or at trace levels otherwise. The high levels of pyoverdine synthesis observed whenever the introduced A domain specified threonine indicated that these nonnative A domains were able to communicate effectively with the PvdD C domain. Moreover, the unexpected observation that non-threonine-specifying A domains nevertheless incorporated threonine into pyoverdine suggests that the native PvdD C domain exhibited stronger selectivity than these A domains for the incorporated amino acid substrate (i.e., misactivation of a threonine residue by the introduced A domains was more frequent than misincorporation of a nonthreonine residue by the PvdD C domain). In contrast, substitution of both the C and A domains of PvdD generated high yields of rationally modified pyoverdines in two instances, these pyoverdines having either a lysine or a serine residue in place of the terminal threonine. However, C-A domain substitution more commonly yielded a truncated peptide product, likely due to stalling of synthesis on a nonfunctional recombinant NRPS template.
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