This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
User:Ann Taylor/Sandbox Trypsin
From Proteopedia
(Difference between revisions)
(New page: ==The Mechanism of Trypsin== <StructureSection load='1agg' size='340' side='right' caption='Acyl intermediate of trypsin catalyzed hydrolysis' scene=''> One of the ways we know about the ...) |
|||
| Line 4: | Line 4: | ||
One of the ways we know about the mechanism of enzymes is through the use of xray crystallography structures of trapped intermediates or inhibitors bound to enzymes. In a paper by Radisky and Koshland<ref>PMID: 16636277</ref>, an acyl intermediate of trypsin (PDB code [[2AGG]] was characterized. | One of the ways we know about the mechanism of enzymes is through the use of xray crystallography structures of trapped intermediates or inhibitors bound to enzymes. In a paper by Radisky and Koshland<ref>PMID: 16636277</ref>, an acyl intermediate of trypsin (PDB code [[2AGG]] was characterized. | ||
| + | Serine proteases use a covalent mechanism to catalyze the hydrolysis of a peptide bond. A covalent bond is formed between <scene name='72/725330/Ser195/1'>Ser195</scene> and a substrate <scene name='72/725330/Substrate_and_ser/1'>peptide</scene>. | ||
| + | Specificity of the proteases is determined by a binding pocket. | ||
Revision as of 15:49, 12 February 2016
The Mechanism of Trypsin
| |||||||||||
