User:Ann Taylor/Sandbox Trypsin

The Mechanism of TrypsinThe Mechanism of Trypsin


One of the ways we know about the mechanism of enzymes is through the use of xray crystallography structures of trapped intermediates or inhibitors bound to enzymes. In a paper by Radisky and Koshland[1], an acyl intermediate of trypsin (PDB code 2AGG was characterized.

Serine proteases use a covalent mechanism to catalyze the hydrolysis of a peptide bond. A covalent bond is formed between and a substrate .

Specificity of the proteases is determined by a binding pocket.



Acyl intermediate of trypsin catalyzed hydrolysis

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ReferencesReferences

  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