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Nonribosomal Peptide Synthesis—Principles and Prospects

2017; Wiley; Volume: 56; Issue: 14 Linguagem: Inglês

10.1002/anie.201609079

1521-3773

Roderich D. Süßmuth, Andi Mainz,

Chemical Synthesis and Analysis

Abstract Nonribosomal peptide synthetases (NRPSs) are large multienzyme machineries that assemble numerous peptides with large structural and functional diversity. These peptides include more than 20 marketed drugs, such as antibacterials (penicillin, vancomycin), antitumor compounds (bleomycin), and immunosuppressants (cyclosporine). Over the past few decades biochemical and structural biology studies have gained mechanistic insights into the highly complex assembly line of nonribosomal peptides. This Review provides state‐of‐the‐art knowledge on the underlying mechanisms of NRPSs and the variety of their products along with detailed analysis of the challenges for future reprogrammed biosynthesis. Such a reprogramming of NRPSs would immediately spur chances to generate analogues of existing drugs or new compound libraries of otherwise nearly inaccessible compound structures.