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==Trypsin: an example of a serine protease== | ==Trypsin: an example of a serine protease== | ||
Trypsin is a serine protease that hydrolyzes on the carboxyl side of hydrophobic residues. 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 | Trypsin is a serine protease that hydrolyzes peptides on the carboxyl side of hydrophobic residues. 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 | ||
{{STRUCTURE_2agi | PDB=2agi | SCENE= }} | {{STRUCTURE_2agi | PDB=2agi | SCENE= }} | ||