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Trypsin is an enzyme in the first section of the small intestine that starts the digestion of protein molecules by cutting long chains of amino acids into smaller pieces. It is a serine protease from the PA clan superfamily, found in the digestive system of many vertebrates, where it hydrolyzes proteins.
Crystal structure of Trypsin, a typical serine protease.. Serine proteases (or serine endopeptidases) are enzymes that cleave peptide bonds in proteins. Serine serves as the nucleophilic amino acid at the (enzyme's) active site. [1]
The early crystal structures included chymotrypsin (PDB file 2CHA), [17] chymotrypsinogen (PDB file 1CHG), [18] trypsin (PDB file 1PTN), [19] and elastase (PDB file 1EST). [20] They also were the first protein structures that showed two near-identical domains, presumably related by gene duplication. One reason for their wide use as textbook and ...
Proteolysis of the zymogen yields an active protein; for example, when trypsinogen is cleaved to form trypsin, a slight rearrangement of the protein structure that completes the active site of the protease occurs, thereby activating the protein.
Enteropeptidase exhibits trypsin-like activity, cleaving proteins following a lysine at a specific cleavage site (Asp-Asp-Asp-Asp-Lys). [19] This cleavage results in trypsindependent activation of other pancreatic zymogens, such as chymotrypsinogen, proelastase, procarboxypeptidase and prolipase in the lumen of the gut. [ 20 ]
436522 Ensembl ENSG00000274247 ENSG00000204983 ENSMUSG00000071521 UniProt P07477 Q792Z1 RefSeq (mRNA) NM_002769 NM_001038996 RefSeq (protein) NP_002760 NP_001034085 Location (UCSC) Chr 7: 142.75 – 142.75 Mb Chr 6: 41.33 – 41.33 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Trypsin-1, also known as cationic trypsinogen, is a protein that in humans is encoded by the PRSS1 gene ...
Trypsinogen (/ ˌ t r ɪ p ˈ s ɪ n ə dʒ ə n,-ˌ dʒ ɛ n / [1] [2]) is the precursor form (or zymogen) of trypsin, a digestive enzyme.It is produced by the pancreas and found in pancreatic juice, along with amylase, lipase, and chymotrypsinogen.
They appear to have independently and convergently evolved an Asp/Ser/His catalytic triad, like in the trypsin serine proteases. The structure of proteins in this family shows that they have an alpha/beta fold containing a 7-stranded parallel beta sheet. The subtilisin family is the second largest serine protease family characterised to date.