Sandbox Wabash13
From Proteopedia
(Difference between revisions)
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| - | Trypsin Structure - Chase Francoeur, Elias Arellano | + | Trypsin Mechanism & Structure - Chase Francoeur, Elias Arellano |
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> | <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> | ||
== Function == | == Function == | ||
| - | Trypsin is a serine protease released by the pancreas and secreted into the duodenum that acts as a digestive enzyme that catalyzes the hydrolysis of peptide bonds, specifically for positively charged residues (K, R, H). The mechanism in which the enzyme acts as a protease is as follows: | + | Trypsin is a serine protease released by the pancreas and secreted into the duodenum that acts as a digestive enzyme that catalyzes the hydrolysis of peptide bonds, specifically for positively charged residues (K, R, H). The catalytic mechanism in which the enzyme acts as a protease is as follows: |
1. Nucleophillic and base catalysis by enzyme to substrate to form tetrahedral intermediate at carbonyl group of scissile peptide. | 1. Nucleophillic and base catalysis by enzyme to substrate to form tetrahedral intermediate at carbonyl group of scissile peptide. | ||
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2. Acid catalysis breaks the tetrahedral intermediate through cleaving of the scissile peptide bond to form an acyl-enzyme intermediate. | 2. Acid catalysis breaks the tetrahedral intermediate through cleaving of the scissile peptide bond to form an acyl-enzyme intermediate. | ||
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3. The amine product is replaced by H2O and subsequently released from the enzyme/substrate complex. | 3. The amine product is replaced by H2O and subsequently released from the enzyme/substrate complex. | ||
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4. Base catalysis by enzyme; H2O forms a covalent bond with the carbonyl group of the N-terminal peptide, leading to another tetrahedral intermediate | 4. Base catalysis by enzyme; H2O forms a covalent bond with the carbonyl group of the N-terminal peptide, leading to another tetrahedral intermediate | ||
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5. Acid catalysis by the breaking of the C-O covalent bond of the tetrahedral intermediate, releasing the peptide from the enzyme substrate complex. Once the peptide is released, the enzyme once again becomes active. <ref>PMID:16636277</ref>. | 5. Acid catalysis by the breaking of the C-O covalent bond of the tetrahedral intermediate, releasing the peptide from the enzyme substrate complex. Once the peptide is released, the enzyme once again becomes active. <ref>PMID:16636277</ref>. | ||
| - | + | Below is a Diagram of the Catalytic Mechanism: | |
== Disease == | == Disease == | ||
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<scene name='72/725338/Ribbon_diagram_n_c_rainbow/1'>Ribbon Diagram of Trypsin (N-->C Rainbow)</scene> | <scene name='72/725338/Ribbon_diagram_n_c_rainbow/1'>Ribbon Diagram of Trypsin (N-->C Rainbow)</scene> | ||
| - | <scene name='Sandbox_45/Ctriadd102h57s195/4'> | + | <scene name='Sandbox_45/Ctriadd102h57s195/4'>Catalytic Triad</scene> |
<scene name='72/725338/Serine__195/1'>Serine 195 - Base Catalysis Residue</scene> | <scene name='72/725338/Serine__195/1'>Serine 195 - Base Catalysis Residue</scene> | ||
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<scene name='72/725338/Aspartic_acid_102/1'>Aspartic Acid 102 - Important Residue in Stabilization of Catalytic Mechanism</scene> | <scene name='72/725338/Aspartic_acid_102/1'>Aspartic Acid 102 - Important Residue in Stabilization of Catalytic Mechanism</scene> | ||
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</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 23:18, 18 February 2016
Trypsin Mechanism & Structure - Chase Francoeur, Elias Arellano
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