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Nonribosomal peptides (NRP) are a class of peptide secondary metabolites, usually produced by microorganisms like bacteria and fungi. Nonribosomal peptides are also found in higher organisms, such as nudibranchs , but are thought to be made by bacteria inside these organisms. [ 1 ]
The three main classes of fungal secondary metabolites are: polyketides, nonribosomal peptides and terpenes. Although fungal secondary metabolites are not required for growth they play an essential role in survival of fungi in their ecological niche. [33] The most known fungal secondary metabolite is penicillin discovered by Alexander Fleming ...
Some proteins are synthesized by nonribosomal peptide synthetases, which can be big protein complexes, each specializing in synthesizing only one type of peptide. Nonribosomal peptides often have cyclic and/or branched structures and can contain non- proteinogenic amino acids - both of these factors differentiate them from ribosome synthesized ...
The nonribosomal peptide synthetase (NRPS), a multi-modular enzyme complex, minimally contains repeating, tri-domains (adenylation (A), peptidyl carrier protein (PCP) and lastly condensation(C)). The adenylation domain (A) is the focus for substrate specificity since it is the initiating and substrate recognition domain.
Glycopeptide antibiotics are a class of drugs of microbial origin that are composed of glycosylated cyclic or polycyclic nonribosomal peptides.Significant glycopeptide antibiotics include the anti-infective antibiotics vancomycin, teicoplanin, telavancin, ramoplanin, avoparcin and decaplanin, corbomycin, complestatin and the antitumor antibiotic bleomycin.
Many siderophores are nonribosomal peptides, [3] [8] although several are biosynthesised independently. [9] Siderophores are also important for some pathogenic bacteria for their acquisition of iron. [3] [4] [10] In mammalian hosts, iron is tightly bound to proteins such as hemoglobin, transferrin, lactoferrin and ferritin.
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Since nonribosomal peptide assembly lines use carrier proteins similar to those use in polyketide synthases, convergence of the two systems evolved to form hybrids, resulting in polypeptides with nitrogen in the skeletal structure and complex function groups similar to those found in amino acids.