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Trypsin
- Molecular classification
- Enzyme, Serine protease, Protease
01
Overview
Trypsin is a serine protease enzyme crucial for protein digestion in the small intestine. It is produced by the pancreas as an inactive precursor, trypsinogen, which is then activated in the duodenum by enterokinase. Once active, trypsin cleaves peptide bonds at the carboxyl side of lysine and arginine residues within proteins. It works synergistically with other digestive enzymes to ensure complete protein digestion.
- Other names
- Trypsin 1Cationic trypsinAnionic trypsin
02
Mechanism of action
Catalyzes hydrolysis of peptide bonds at lysine and arginine residues.
03
Biological functions
Protein digestionHydrolysis of peptide bonds
04
Disease associations
MalabsorptionCystic fibrosisPancreatic insufficiency
05
Safety considerations
Potential for autodigestion if not properly regulatedImpaired protein digestion in cases of deficiency
06
Biomarkers
Elevated serum trypsin levels in cystic fibrosis
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