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The two precursors and the growing depsipeptide chain are tethered to the T domains through phosphopantetheinyl prosthetic groups.

In the linear model, T have the same function of holding the growing depsipeptide chain.

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Adenylation (A), thiolation (T) and condensation (C) are essential domains for the formation and elongation of the peptide chain. Both modular enzymes have the same architecture of C.

Other tailoring domains, such as methyltransferase (MT), oxidation (Ox) and epimerization (E), contribute to the large structural diversity in natural NRPs, such as bacterial metabolites enterobactin, echinomycin and gramicidin, as well as fungal natural products beauvericin (1), beauvericins A–C (2–4), bassianolide (5), enniatins A–C (6–8) and verticilide (9) (Fig. These molecules possess a wide range of biological activities, including antimicrobial, insecticidal, anthelmintic, herbicidal, anti-haptotactic, anti-cholesterol and anticancer activities(a) Representative NRPs (1–9) synthesized by fungal iterative NRPSs. The beauvericin and bassianolide synthetases (Bb BEAS and Bb BSLS) share significant sequence homology (66% identity and 79% similarity) and the same domain organization (Fig. In spite of the high sequence similarity, Bb BEAS catalyses recursive head-to-tail condensation of three dipeptidol monomers, while Bb BSLS condenses four monomers.

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Nonribosomal peptide synthetases (NRPSs) assemble a large group of structurally and functionally diverse natural products.

The common architecture of these NRPSs suggests that they share a general assembly rule.