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Enteropeptidase (also called enterokinase) is an enzyme produced by cells of the duodenum and is involved in digestion in humans and other animals. Enteropeptidase converts trypsinogen (a zymogen) into its active form trypsin, resulting in the subsequent activation of pancreatic digestive enzymes.
Pepsin / ˈ p ɛ p s ɪ n / is an endopeptidase that breaks down proteins into smaller peptides and amino acids. It is one of the main digestive enzymes in the digestive systems of humans and many other animals, where it helps digest the proteins in food. Pepsin is an aspartic protease, using a catalytic aspartate in its active site. [2]
The enzymes exist as homodimers. In eukaryotes, each monomer consisting of two major regions: an N-terminal oxygenase domain, which belongs to the class of heme-thiolate proteins, and a multi-domain C-terminal reductase, which is homologous to NADPH:cytochrome P450 reductase (EC 1.6.2.4) and other flavoproteins. The FMN binding domain is ...
Post-translational modifications can occur before protein folding or after. Common biological methods of modifying peptide chains after translation include methylation, phosphorylation, and disulfide bond formation. Methylation often occurs to arginine or lysine and involves adding a methyl group to a nitrogen (replacing a hydrogen).
Aminopeptidases are a diverse group of enzymes that play crucial roles in various biological processes, including protein digestion, cell growth, and immune response.They are classified based on their substrate specificity (strength of binding) and catalytic mechanism (means of catalyzing their reaction) into two main categories: metalloaminopeptidases and cysteine aminopeptidases.
Proteolysis in organisms serves many purposes; for example, digestive enzymes break down proteins in food to provide amino acids for the organism, while proteolytic processing of a polypeptide chain after its synthesis may be necessary for the production of an active protein.