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Sandbox wabash15
From Proteopedia
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(→"Structure of Trypsin") |
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<StructureSection load='2agg' size='340' side='right' caption='Acyl intermediate of trypsin catalyzed hydrolysis=''> | <StructureSection load='2agg' size='340' side='right' caption='Acyl intermediate of trypsin catalyzed hydrolysis=''> | ||
| - | *'''Trypsin''' is a serine protease formed in the small intestine and catalyzes the hydrolysis of smaller peptides. As with other members of its family, it possesses a catalytic triad (His-57, Asp-102, and Ser-195). This active site produces a nucleophilicity that enables its reaction with the serine groups on its substrate, i.e. smaller peptides. Within the catalytic triad-active site, an oxyanion hole exists that essentially stabilizes the acyl-intermediate states of the reaction, creating a binding pocket for the reaction to take place. These acyl-intermediates are key in protease reactions, as they are very susceptible to hydrolysis reactions, providing an opportunity for the second substrate of trypsin (water) to hydrolyze the interaction between His-57 and the attached C-terminus end of the protein substrate.. To stabilize this process, Asp-189 stabilizes the reaction by mediating an interaction with Lys or other positively-charged residues on the smaller protein. | + | *'''Trypsin''' is a serine protease formed in the small intestine and catalyzes the hydrolysis of smaller peptides. As with other members of its family, it possesses a <scene name='Sandbox_45/Ctriadd102h57s195/4'>catalytic triad</scene> (His-57, Asp-102, and Ser-195). This active site produces a nucleophilicity that enables its reaction with the serine groups on its substrate, i.e. smaller peptides. Within the catalytic triad-active site, an oxyanion hole exists that essentially stabilizes the acyl-intermediate states of the reaction, creating a binding pocket for the reaction to take place. These acyl-intermediates are key in protease reactions, as they are very susceptible to hydrolysis reactions, providing an opportunity for the second substrate of trypsin (water) to hydrolyze the interaction between His-57 and the attached C-terminus end of the protein substrate.. To stabilize this process, Asp-189 stabilizes the reaction by mediating an interaction with Lys or other positively-charged residues on the smaller protein. |
== Function == | == Function == | ||
Current revision
"Structure of Trypsin"
By: Luke Knutson and Graham Redweik This is a sub structure of trypsin Sandbox wabash15. Click above on edit this page to modify. Be careful with the < and > signs. You may include any references to papers as in: the use of JSmol in Proteopedia [1] or to the article describing Jmol [2] to the rescue.
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