is a protease, which is an enzyme that catalyzes the cleavage of amino acids at the carboxyl side. This study utilized a bovine pancreatic trypsin inhibitor (BTPI) in order to study the structure of bovine α-chymotrypsin homodimer.[1]
Function
The active site of chymotrypsin consists of a (Ser 195, His 57, Asp 102), which are highlighted in blue.
The S1 binding pocket is responsible for stabilization of the substrate in the active site prior to cleavage. The S1 pocket is mainly hydrophobic and preferentially binds to large, nonpolar amino acids, which includes tyrosine, tryptophan, and phenylalanine. The of the bovine α-chymotrypsin is highlighted in yellow.
Chymotrypsin and other serine protease enzymes catalyzes the cleavage of amino acids, and the S1 binding pocket helps stabilize the intermediate before completely cleaving the amino acid. Both the active site and S1 pocket can be seen . The catalytic triad is highlighted in blue and the S1 pocket is highlighted in yellow.
Disease
Relevance
Structural highlights
Chymotrypsin is composed of (residues 1-13 shown in maroon, 16-146 shown in blue, and 149-245 shown in gold).
