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Chymotrypsinogen B1 is a serine protease precursor produced by pancreatic acinar cells. After secretion into the small intestine, it is activated to chymotrypsin B1, a proteolytic enzyme involved in dietary protein digestion and regulation of trypsin activity. CTRB1 is closely related to other chymotrypsinogen genes (especially CTRB2) and can exist in different isoforms due to gene variation. Functional studies have shown that CTRB1 helps protect the pancreas from autodigestive injury by promoting degradation of trypsinogen, thus moderating trypsin-mediated damage. Mutations or genetic rearrangements near this locus can affect susceptibility to pancreatitis. As an archetype of the serine protease PA clan, its enzyme mechanism involves a catalytic triad (serine, histidine, aspartate) that hydrolyzes peptide bonds after aromatic amino acids in proteins. It is not currently the primary target of marketed drugs but is implicated in pancreatic disease risk and may be explored for therapeutic enzyme modulation.
Catalytic hydrolysis of peptide bonds, especially after aromatic amino acids. Degradation of trypsinogen, reducing pathological trypsin activation.
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