Sandbox Wabash3

Kenton Hicks, Kyle Stucker, Allen Betts

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 specificity pocket, which contains Ser 195, His 57, and Asp 102. These three residues make up the

^[1]

Disease

Relevance

Structural highlights

This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.