Template:Sandbox Reserved Taylor 1

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==Trypsin: an example of a serine protease==
 
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Trypsin is a serine protease. It works with a catalytic triad of aspartic acid, histidine and serine to catalyze the formation of a covalent intermediate with the substrate. This structure shows the binding of trypsin to a competitive inhibitor, leupeptin. There is a hydrophobic binding pocket to help align the substrate protein with the enzyme, and an oxyanion hole to stabilize the intermediate. Radisky ES, Lee JM, Lu CJ, Koshland DE Jr, Proc Natl Acad Sci U S A. 2006 May 2;103(18):6835-40. Epub 2006 Apr 24. PMID:16636277
 
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{{STRUCTURE_2agi | PDB=2agi | SCENE= }}
 

Revision as of 06:41, 9 February 2014

This Sandbox is Reserved from Jan 1, through May 1, 2014 for use in a Biochemistry course taught by Ann Taylor at the University of Tennessee, Knoxville, USA. -->
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