Siderophores play a pivotal role in the viability of fungi and are essential for the virulence of many pathogenic fungal species. Despite their importance in fungal physiology and pathogenesis, the programming rules of siderophore assembly by fungal nonribosomal peptide synthetases (NRPSs) remain unresolved. This seminar will explore the unusual enzymology and biosynthetic logic employed during the construction of two structurally distinct siderophores. The use of intact protein mass spectrometry, together with in vitro biochemical assays of native and dissected enzymes, provides unique snapshots of individual biosynthetic steps during NPRS catalysis, and sets the stage for bioengineering efforts to diversify these complex chemical scaffolds.

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