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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 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.
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RiPPs consist of any peptides (i.e. molecular weight below 10 kDa) that are ribosomally-produced and undergo some degree of enzymatic post-translational modification.This combination of peptide translation and modification is referred to as "post-ribosomal peptide synthesis" (PRPS) in analogy with nonribosomal peptide synthesis (NRPS).
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Peptide bond formation via dehydration reaction. When two amino acids form a dipeptide through a peptide bond, [1] it is a type of condensation reaction. [2] In this kind of condensation, two amino acids approach each other, with the non-side chain (C1) carboxylic acid moiety of one coming near the non-side chain (N2) amino moiety of the other.