Trypsin is a serine protease that catalyzes acyl peptide bonds. It is specific for positively charged residues. The His 57 and Ser 195 are located in the active site of the trypsin. The trypsin mechanism is defined by 2 separate reactions. The mechanism begins by the breaking of the scissile bond in the substrate polypeptide. A tetrahedral intermediate forms followed by an acyl-enzyme intermediate. The C terminus then departs followed by the creation of an additional tetrahedral intermediate. Finally the N terminus of the substrate polypeptide exits, leaving the active enzyme.
Function
Disease
Relevance
Structural highlights
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