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 ...) |
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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
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