Trypsin
Definition:
EC Tree > 3 Hydrolases > 3.4 Acting on peptide bonds (peptidases) > 3.4.21 Serine endopeptidases > 3.4.21.4 trypsin
Trypsin is the archetypal serine endopeptidase in family S1; cattle beta-trypsin is a single polypeptide chain formed from trypsinogen by cleavage of one peptide bond, with further cleavages producing alpha and other isoforms, and multiple cationic and anionic trypsins have been isolated from vertebrate pancreas and lower species including crayfish, insects (cocoonase) and microorganisms such as Streptomyces griseus; it preferentially cleaves Arg and Lys bonds. By activating pancreatic zymogens and digesting dietary proteins it drives intestinal proteolysis. It is distributed across Eukaryota and Bacteria.
Trypsin is the archetypal serine endopeptidase in family S1; cattle beta-trypsin is a single polypeptide chain formed from trypsinogen by cleavage of one peptide bond, with further cleavages producing alpha and other isoforms, and multiple cationic and anionic trypsins have been isolated from vertebrate pancreas and lower species including crayfish, insects (cocoonase) and microorganisms such as Streptomyces griseus; it preferentially cleaves Arg and Lys bonds. By activating pancreatic zymogens and digesting dietary proteins it drives intestinal proteolysis. It is distributed across Eukaryota and Bacteria.
References:
Biomedical Dictionary
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