Trypsin is serine protease which catalyzes the hydrolysis of peptide bonds of a substrate via an acylation reaction and a deacylation reaction. In the first (acylation) reaction, the nucleophilic serine attacks the substrate scissile bond, forming a tetrahedral intermediate and then a covalent acyl-enzyme with the release of the C-terminal fragment. In the second (deacylation) reaction, a water molecule attacks the acyl-enzyme, leading to a second tetrahedral intermediate followed by release of the N-terminal fragment. The specificity of substrates is determined by the structure of its active site, which contains Ser-195, , and Asp-189. (Asp189 Sandbox Wabash3. Click above on edit this page to modify. Be careful with the < and > signs.
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