Sandbox Wabash13

From Proteopedia

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'''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:
'''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:
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1. Nucleophillic and base catalysis by enzyme to substrate to form tetrahedral intermediate at carbonyl group of scissile peptide.
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1. Nucleophillic and base catalysis by enzyme to substrate to form tetrahedral intermediate at carbonyl group of scissile peptide. The nucleophilic attack is carried out by Ser 195, by attacking the
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scissile peptide's carbonyl group to form the tetrahedral intermediate.
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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<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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Ser 195 nucleophilically attacks the scissile's peptide's carbonyl group
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'''Ser 195 nucleophilically attacks the scissile's peptide's carbonyl group'''
<scene name='72/725338/Histidine_57/1'>Histidine 57 - Acid Catalysis Residue</scene>
<scene name='72/725338/Histidine_57/1'>Histidine 57 - Acid Catalysis Residue</scene>
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'''The N3 of His 57 donates a proton (General Acid Catalysis)'''
<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>

Revision as of 01:24, 19 February 2016

Trypsin Mechanism & Structure - Chase Francoeur, Elias Arellano

Trypsin

Drag the structure with the mouse to rotate

References

  1. ↑ Radisky ES, Lee JM, Lu CJ, Koshland DE Jr. Insights into the serine protease mechanism from atomic resolution structures of trypsin reaction intermediates. Proc Natl Acad Sci U S A. 2006 May 2;103(18):6835-40. Epub 2006 Apr 24. PMID:16636277
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