CTRC hydrolyses PRSS1

Stable Identifier
Reaction [transition]
Homo sapiens
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Digestive proteases are synthesised and secreted by the pancreas as inactive zymogens whose activation occur in the duodenum. Activation of trypsin (PRSS1) within the pancreas before secretion is thought to be a major initiating factor in chronic pancreatitis. Chymotrypsin-C (CTRC) is a pancreatic serine protease that regulates activation and degradation of trypsinogens and procarboxypeptidases by targeting specific cleavage sites within their zymogen precursors. CTRC regulates trypsinogen activation and stability by two opposing cleavage sites: it can cleave cationic trypsinogen either at Phe18-Asp19 in the activation peptide, leading to enhanced autoactivation or at Leu81-Glu82 within the Ca2+-binding loop, resulting in degradation (the latter not shown here) (Batra et al. 2013).

Literature References
PubMed ID Title Journal Year
23430245 Long-range electrostatic complementarity governs substrate recognition by human chymotrypsin C, a key regulator of digestive enzyme activation

Batra, J, Szabo, A, Caulfield, TR, Soares, AS, Sahin-Tóth, M, Radisky, ES

J. Biol. Chem. 2013
Catalyst Activity

peptidase activity of CTRC [extracellular region]

Orthologous Events
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