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The biosynthesis of nonribosomal peptides shares characteristics with the polyketide and fatty acid biosynthesis. Due to these structural and mechanistic similarities, some nonribosomal peptide synthetases contain polyketide synthase modules for the insertion of acetate or propionate -derived subunits into the peptide chain.
Insulin biosynthesis is regulated by transcriptional and translational levels. The β-cells promote their protein transcription in response to nutrients. The exposure of rat Langerhans islets to glucose for 1 hour is able to remarkably induce the intracellular proinsulin levels. It was noted that the proinsulin mRNA remained stable.
In molecular biology, post-translational modification (PTM) is the covalent process of changing proteins following protein biosynthesis. PTMs may involve enzymes or occur spontaneously. Proteins are created by ribosomes , which translate mRNA into polypeptide chains , which may then change to form the mature protein product.
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.
Photosynthetic carbohydrate synthesis in plants and certain bacteria is an anabolic process that produces glucose, cellulose, starch, lipids, and proteins from CO 2. [6] It uses the energy produced from the light-driven reactions of photosynthesis, and creates the precursors to these large molecules via carbon assimilation in the photosynthetic ...
Insulin is a peptide hormone containing two chains cross-linked by disulfide bridges. Insulin (/ ˈ ɪ n. sj ʊ. l ɪ n /, [5] [6] from Latin insula, 'island') is a peptide hormone produced by beta cells of the pancreatic islets encoded in humans by the insulin (INS) gene. It is the main anabolic hormone of the body. [7]
Protein primary structure is the linear sequence of amino acids in a peptide or protein. [1] By convention, the primary structure of a protein is reported starting from the amino-terminal (N) end to the carboxyl-terminal (C) end. Protein biosynthesis is most commonly performed by ribosomes in cells. Peptides can also be synthesized in the ...
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).