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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 ...
Analogous to the nonribosomal code is prediction of peptide composition by DNA/RNA codon reading, which is well supported by the central dogma of molecular biology and accomplished using the genetic code simply by following the DNA codon table or RNA codon table. However, prediction of natural product/secondary metabolites by the nonribosomal ...
Creatine peptides promote the release of hormones that influence one's exercise performance, muscle recovery and body composition, which is why some athletes are drawn to the amino acids.
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.
In addition to these subclasses, there also exist polyketides that are hybridized with nonribosomal peptides (Hybrid NRP-PK and PK-NRP). 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 ...
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).