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is a serine protease, found in the digestive system of many vertebrates, where it hydrolyses proteins[1].
Trypsin is produced in the pancreas as the inactive protease trypsinogen.
Trypsin Break peptide chains mainly at the carboxyl side of the amino acids lysine or arginine,
except when either is followed by proline. It is used for numerous biotechnological processes.
The process is commonly referred to as trypsin proteolysis or trypsinisation,
and proteins that have been digested/treated with trypsin are said to have been trypsinized.
Function
In the duodenum, trypsin catalyzes the hydrolysis of peptide bonds, breaking down proteins into smaller peptides.
The enzymatic mechanism is similar to that of other serine proteases. These enzymes contain a catalytic triad consisting of . These three residues form a charge relay that serves to make the active site serine nucleophilic.
Trypsin contains an "oxyanion hole" formed by the backbone amide hydrogen atoms of , which serves to stabilize the developing negative charge on the carbonyl oxygen atom of the cleaved amides.
The located in the catalytic pocket (S1) of trypsin is responsible for attracting and stabilizing positively charged lysine and/or arginine, and is, thus, responsible for the specificity of the enzyme.
Disease
Relevance
Structural highlights
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