ABSTRACT
Non-ribosomal peptide synthetases (NRPSs) are enzymatic complexes which act as catalyzers for the synthesis of biologically important microbial peptides. One of these microbial peptides of commercial importance is cyclic lipopeptides. Cyclic lipopeptides are structurally and functionally diverse molecules, which are produced by large, complex and multifunctional NRPSs using the thioesterase mechanism. Ligand identification of plipastatin is done on the basis of its mechanism of action and its structure prediction through homology modeling on the NRPS template. Antimicrobial lipopeptides are a cluster of small peptides linked with fatty acids which are secreted by various microorganisms. Lipopeptide synthases play an important role in the synthesis of lipopeptides. They are multienzyme complexes which have various modules for peptide biosynthesis. Once the structures of the synthases were obtained, they were docked with the various ligands to obtain the ligand and their pharmacokinetic properties after uptake of drug.
