ArticleNature communications2023
Elucidating the molecular programming of a nonlinear non-ribosomal peptide synthetase responsible for fungal siderophore biosynthesis.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Siderophore production by the lichen fungus Xanthoria parietina supports its algal symbiont.Nature communications · 2026Article
- Fusaric Acid Analogs and Dimers from Marine-DerivedJournal of natural products · 2026Article
- PARAS: High-Accuracy Machine Learning of Substrate Specificities in Nonribosomal Peptide Synthetases.JACS Au · 2026Article
- A biosynthetic survey of hypocrealean biocontrol fungi.Nature chemical biology · 2026Article
- Bacterial Siderophore Production in Metal-Rich Environments: Underexplored Sources of Siderophores and Insights into Bioremediation.Journal of natural products · 2026Review
- Expression of a strain-specific non-ribosomal peptide synthetase from Aspergillus lentulus lead to the discovery of a new fungal alkaloid lentoquinazoline.The Journal of antibiotics · 2026Article
- Ferrichrome: bacterial function, synthetic mimics, and biomedical applications.Frontiers in microbiology · 2026Review
- Siderophores and secondary metabolites produced byMicrobiology (Reading, England) · 2025Article
- Article
- The Intricate Nonribosomal Assembly of a Potent Antifungal Lipopeptide from theJournal of the American Chemical Society · 2025Article
- Review
- Article
- Controlling Substrate- and Stereospecificity of Condensation Domains in Nonribosomal Peptide Synthetases.ACS chemical biology · 2024Article
Corrections and comments
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Authors and funding
10 authors.
Funding
Abstract
Siderophores belonging to the ferrichrome family are essential for the viability of fungal species and play a key role for virulence of numerous pathogenic fungi. Despite their biological significance, our understanding of how these iron-chelating cyclic hexapeptides are assembled by non-ribosomal peptide synthetase (NRPS) enzymes remains poorly understood, primarily due to the nonlinearity exhibited by the domain architecture. Herein, we report the biochemical characterization of the SidC NRPS, responsible for construction of the intracellular siderophore ferricrocin. In vitro reconstitution of purified SidC reveals its ability to produce ferricrocin and its structural variant, ferrichrome. Application of intact protein mass spectrometry uncovers several non-canonical events during peptidyl siderophore biosynthesis, including inter-modular loading of amino acid substrates and an adenylation domain capable of poly-amide bond formation. This work expands the scope of NRPS programming, allows biosynthetic assignment of ferrichrome NRPSs, and sets the stage for reprogramming towards novel hydroxamate scaffolds.
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