Nonribosomal peptides display a broad range of biological activities,
including antimicrobial, antitumor and immunosuppressive agents, as well as signaling
molecules and virulence factors. Many of these nonribosomal peptides are biosynthesized
by large, highly versatile multifunctional proteins known as nonribosomal
peptide synthetases (NRPSs). The results of genetic, biochemical, and bioinformatic
investigations over the past three decades have offered a profound understanding of the
functional characteristics and molecular basis underpinning the enzymology of
nonribosomal peptide biosynthesis; however, studies at the proteomic level are limited.
This chapter will focus on tools recently developed not only for studies aimed at
visualizing, monitoring and tracking NRPS proteins but also for rapid labeling,
isolation, identification and enzymatic characterization of NRPS family members as
required for proteomics in natural product biosynthesis.
Keywords: Activity-based protein profiling (ABPP), Adenylation domains,
Chemical proteomic probes, Chemoproteomics, Competitive ABPP, Nonribosomal
peptide synthetases, 5′-O-(N-aminoacyl)-sulfamoyladenosine.
