Description
Chymotrypsin is a digestive enzyme component of pancreatic juice acting in the duodenum where it performs proteolysis, the breakdown of proteins and polypeptides. Chymotrypsin preferentially cleaves peptide amide bonds where the carboxyl side of the amide bond (the P1 position) is a large hydrophobic amino acid (tyrosine, tryptophan, and phenylalanine). These amino acids contain an aromatic ring in their sidechain that fits into a 'hydrophobic pocket' (the S1 position) of the enzyme. It is activated in the presence of trypsin.
Abbr
α-Chymotrypsin, Native (Human)
Alias
avazyme; chymar; α-Chymotrypsin
Applications
Human α-chymotrypsin has been used in a study to assess the quantitative structure-activity relationships for organophosphates binding to trypsin and chymotrypsin. Human α-chymotrypsin has also been used in a study to investigate the direct detection of native proteins in biological matrices using extractive electrospray ionization mass spectrometry.
Enzyme Commission Number
EC 3.4.21.1
Molecular Weight
mol wt 25 kDa
Unit Definition
One unit will hydrolyze 1.0 μmole of BTEE per min at pH 7.8 at 25°C.
Pathway
Activation of Matrix Metalloproteinases, organism-specific biosystem; Degradation of the extracellular matrix, organism-specific biosystem; Extracellular matrix organization, organism-specific biosystem; Pancreatic secretion, organism-specific biosystem; Pancreatic secretion, conserved biosystem; Protein digestion and absorption, organism-specific biosystem; Protein digestion and absorption, conserved biosystem
Function
peptidase activity; serine-type endopeptidase activity
Synonyms
EC 3.4.21.1; α-Chymotrypsin; chymotrypsins A and B; alpha-chymar ophth; avazyme; chymar; chymotest; enzeon; quimar; quimotrase; alpha-chymar; alpha-chymotrypsin A; alpha-chymotrypsin; Chymotrypsin