Explore: Chymotrypsin

Chymotrypsin (EC 3.4.21.1, chymotrypsins A and B, alpha-chymar ophth, avazyme, chymar, chymotest, enzeon, quimar, quimotrase, alpha-chymar, alpha-chymotrypsin

Serine proteases fall into two broad categories based on their structure: chymotrypsin-like (trypsin-like) or subtilisin-like. The MEROPS protease classification

elastases", chymotrypsin, and neutrophil elastase are serine proteases. The "macrophage elastase" is a matrix metallopeptidase. Chymotrypsin is weaker at

Chymotrypsinogen is an inactive precursor (zymogen) of chymotrypsin, a digestive enzyme which breaks proteins down into smaller peptides. Chymotrypsinogen

Chymotrypsin C, also known as caldecrin or elastase 4, is an enzyme that in humans is encoded by the CTRC gene. Chymotrypsin C is a member of the peptidase

Chymotrypsin-like elastase family member 3B also known as elastase-3B, protease E, or fecal elastase is an enzyme that in humans is encoded by the CELA3B

1-chloro-3-tosylamido-4-phenyl-2-butanone. TPCK is an irreversible inhibitor of chymotrypsin. Also inhibits some cysteine proteases such as caspase, papain, bromelain

the interaction between the enzyme and the substrate, for instance, chymotrypsin activation (as it can be seen in the images). Many different types of

k cat / K m {\displaystyle k_{\text{cat}}/K_{\mathrm {m} }} (M−1s−1) Chymotrypsin 1.5 × 10−2 0.14 9.3 Pepsin 3.0 × 10−4 0.50 1.7 × 103 tRNA synthetase

makes up the catalytic site. In chymotrypsin, these residues are Ser-195, His-57 and Asp-102. The mechanism of chymotrypsin can be divided into two phases