Nonribosomal peptides (NRPs) constitute a class of peptide secondary metabolites distinguished by their biosynthetic origin outside the ribosomal machinery, being assembled by dedicated multimodular enzyme systems rather than translated from a messenger RNA template. This nonribosomal origin confers upon NRPs a defining structural freedom: their monomeric building blocks are not restricted to the 21 proteinogenic amino acids but extend to a vast repertoire of nonproteinogenic residues, including D-amino acids, hydroxy acids, aryl acids, and other non-canonical units ^[1][2]. The structural consequences of this freedom are substantial. NRPs frequently adopt cyclic or branched architectures, contain non-standard peptide bonds and modified side chains, and exhibit a degree of structural complexity—encompassing macrocyclic rings, heterocyclic elements, and diverse tailoring modifications—that far exceeds the range accessible to ribosomal peptides ^[2][3]. The term encompasses a pharmacologically significant array of compounds, including glycopeptide antibiotics such as vancomycin, lipopeptides such as daptomycin, immunosuppressants such as cyclosporine, antitumor agents such as bleomycin, and siderophores such as enterobactin ^[4][5]. Within the taxonomy of microbial natural products and biosynthesis, NRPs are defined as ribosome-independent peptide natural products whose structural diversity and biological activity derive from the incorporation of nonproteinogenic building blocks and from extensive post-assembly modification, rather than from direct gene-encoded translation ^[1][2].