Trypsin is a serine protease that catalyzes acyl peptide bonds. It is specific for positively charged residues. The and 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. Trypsin also contains a catalytic triad to either split a substrate or transfer a substrate. The triad in trypsin consists of histidine, aspartate, and serine. In addition to this triad Trypsin also contains an oxyanion hole consisting of glycine and serine to stabilize the charge. Finally in the creation of trypsin the specificity pocket leads to a binding preference for lysine or arginine. [1]
Labels showing the sulfate, carbonyl, and Calcium ligands
Location of His 57 residue which shows the alpha helix regular secondary structure.
Location of Asp 102 residue which shows the beta sheet regular secondary structure.
Function
Disease
Relevance
Structural highlights
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