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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=''>
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Trypsin is a serine protease that catalyzes acyl peptide bonds. It is specific for positively charged residues. The <scene name='72/725353/His_57/5'>His 57</scene> and <scene name='72/725353/Ser_195/1'>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.<ref>PMID:16636277</ref>
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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_195/1'>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.<ref>PMID:16636277</ref>

Revision as of 03:39, 19 February 2016

Trypsin Mechanism (By: Andrew Powell, Bilal Jawed, Mazin Hakim)

PDB ID 2agg

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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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