Trypsin is a serine protease that contains serine, histidine, and aspartic acid residues. Trypsin catalyzes peptide bond hydrolysis through acid catalysis, base catalysis, and covalent catalysis. In the first step serine acts as a nucleophile to attack the substrate peptide bond, which forms a tetrahedral intermediate via covalent catalysis. Then a acyl-enzyme intermediate is formed and the C-terminal fragment is released. A water molecule attacks the acyl enzyme leading to the creation of a second tetrahedral intermediate. This is followed by the release of the N-terminal fragment, which results in the creation of the active enzyme.
Scene 1:catalytic triad
Scene 2:acyl intermediate
Scene 3: oxyanion hole
Scene 4: specificity pocket
BY: MICHAEL GREEN AND AARON BECKER AND BEIDOU CHENG
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Function
Disease
Relevance
Structural highlights
This is a sample scene created with SAT to by Group.
One key features of the mechanism of trypsin hydrolysis is Ser-195
Another
