Kyle Schroering Sandbox 1
The Mechanism of TrypsinThe Mechanism of Trypsin
Trypsin structure contains an aspartate residue (189) in its catalytic pocket that is used to attract and stabilize the positively charged lysine and/or arginine. Therefore, the aspartate residue is responsible for the specificity of the enzyme. Trypsin cleaves protein on the carboxyl end of lysine and arginine except when they are bound to proline. Once in the small intestine, the enzyme enteropeptidase activates it into trypsin by proteolytic cleavage. The cleavage occurs within the polypeptide chain rather than at the terminal amino acids located at the ends of polypeptides.
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| 2age, resolution 1.15Å () | |||||||||
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| Ligands: | |||||||||
| Non-Standard Residues: | |||||||||
| Activity: | Trypsin, with EC number 3.4.21.4 | ||||||||
| Related: | 2agg, 2agi, 2ah4
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
