User:Ann Taylor/Sandbox Trypsin: Difference between revisions
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The Mechanism of Trypsin
References
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==The Mechanism of Trypsin== | ==The Mechanism of Trypsin== | ||
<StructureSection load=' | <StructureSection load='2agg' size='340' side='right' caption='Acyl intermediate of trypsin catalyzed hydrolysis' scene=''> | ||
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. | ||
Revision as of 18:50, 12 February 2016
The Mechanism of TrypsinThe Mechanism of Trypsin
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[1], 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 and a substrate . Specificity of the proteases is determined by a binding pocket.
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