Chymotrypsin B (CTRB1)

Chymotrypsin B is a major serine protease produced by the pancreas as an inactive zymogen, chymotrypsinogen, which is subsequently activated by trypsin in the small intestine. Its primary biological function is the digestion of dietary proteins, where it selectively cleaves peptide bonds on the carboxyl side of aromatic or large hydrophobic amino acids such as phenylalanine, tyrosine, and tryptophan [1, 2]. Beyond digestion, the chymotrypsin-like activity of the 20S proteasome is a critical target in the treatment of hematological malignancies like multiple myeloma, where inhibitors like bortezomib disrupt protein degradation pathways [3, 4]. Genetic mutations or imbalances in chymotrypsin levels are clinically significant, with variants in the CTRB1 and CTRB2 genes being strongly associated with the risk of chronic pancreatitis and type 2 diabetes [5]. Therapeutically, chymotrypsin itself has been used as an anti-inflammatory agent to reduce edema and as a debriding agent for wounds, while its inhibitors are studied for managing inflammatory conditions [6]. Monitoring fecal chymotrypsin levels remains a standard diagnostic tool for evaluating pancreatic exocrine insufficiency [7].

Other names

Chymotrypsinogen BCTRB1CTRB2ChymotrypsinAlpha-chymotrypsinSerine protease

Chymotrypsin is a serine protease that catalyzes the hydrolysis of peptide bonds at the carboxyl side of aromatic amino acids. Therapeutic agents either inhibit this activity to prevent tissue damage (e.g., in pancreatitis) or utilize the enzyme's proteolytic properties for therapeutic debridement or anti-inflammatory effects.