Ann Taylor sandbox 20
From Proteopedia
Trypsin Mechanism
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Trypsin is an enzyme that is part of a group of digestive enzymes that are classifies as serine proteases. Trypsin is responsible for the breakdown of the polypeptide backbone of positively charged proteins like Arg and Lys. This is accomplished by its structure. The active site of trypsin has an anionic Asp residual that can form ionic bonds with charged Arg and Lys . The active site also contains His, which is responsible for proton movement and polarization of hydrogens creating an environment conducive to catalysis. The Final key feature of the trypsin active site is called a oxyanion hole. This is a spot that, once the substrate is in its tetrahedral form, can form hydrogen bonds to stabilize the intermediate but when it is not the substrate is not in the correct orientation to form these stabilizing bonds. This is important because it increases the enzymes affinity for the transition state.
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| 2agg, resolution 1.28Å () | |||||||||
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| Ligands: | , | ||||||||
| Non-Standard Residues: | |||||||||
| Activity: | Trypsin, with EC number 3.4.21.4 | ||||||||
| Related: | 2age, 2agi, 2ah4 | ||||||||
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| Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
