Sandbox Wabash24
From Proteopedia
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==Trypsin Mechanism (By: Andrew Powell, Bilal Jawed, Mazin Hakim) == | ==Trypsin Mechanism (By: Andrew Powell, Bilal Jawed, Mazin Hakim) == | ||
<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 that catalyzes acyl peptide bonds. It is specific for positively charged residues. The <scene name='72/725353/His_57/6'>His 57</scene> and <scene name='72/725353/Ser_195/2'>Ser 195</scene> are located in the active site of the trypsin | + | Trypsin is a serine protease that catalyzes acyl peptide bonds. It is specific for positively charged residues. The <scene name='72/725353/His_57/6'>His 57</scene> and <scene name='72/725353/Ser_195/2'>Ser 195</scene> are located in the active site of the trypsin. The trypsin mechanism is defined by 2 separate reactions. The mechanism begins by the breaking of the scissile bond in the substrate polypeptide. A tetrahedral intermediate forms followed by an acyl-enzyme intermediate. The C terminus then departs followed by the creation of an additional tetrahedral intermediate. Finally the N terminus of the substrate polypeptide exits, leaving the active enzyme. Trypsin also contains a catalytic triad to either split a substrate or transfer a substrate. The triad in trypsin consists of histidine, aspartate, and serine. In addition to this triad Trypsin also contains an oxyanion hole consisting of glycine and serine to stabilize the charge. Finally in the creation of trypsin the specificity pocket leads to a binding preference for lysine or arginine. <ref>PMID:16636277</ref> |
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| + | Structure also includes sulfate, carbonyl, and Calcium <scene name='72/725353/Labels_of_heme_groups/3'>ligands</scene> | ||
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| + | The role of asp 102 and his 57 during Trypsin catalysis is to effectively function as a proton shuttle. | ||
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| + | <scene name='72/725353/Asp_102/2'>Asp 102 Location Highlighted in Magenta</scene> | ||
| + | Location of Asp 102 residue which shows the beta sheet regular secondary structure. | ||
Revision as of 05:16, 19 February 2016
Trypsin Mechanism (By: Andrew Powell, Bilal Jawed, Mazin Hakim)
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