Kyle Schroering Sandbox 1 - Revision history

Kyle Schroering at 14:54, 19 February 2010

Kyle Schroering — Fri, 19 Feb 2010 14:54:18 GMT

←Older revision		Revision as of 14:54, 19 February 2010
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	Trypsin structure contains an aspartate residue (189) in its catalytic pocket that is used to attract and stabilize the positively charged lysine and/or arginine. Therefore, the aspartate residue is responsible for the specificity of the enzyme. Trypsin cleaves protein on the carboxyl end of lysine and arginine except when they are bound to proline. Once in the small intestine, the enzyme enteropeptidase activates it into trypsin by proteolytic cleavage. The cleavage occurs within the polypeptide chain rather than at the terminal amino acids located at the ends of polypeptides.		Trypsin structure contains an aspartate residue (189) in its catalytic pocket that is used to attract and stabilize the positively charged lysine and/or arginine. Therefore, the aspartate residue is responsible for the specificity of the enzyme. Trypsin cleaves protein on the carboxyl end of lysine and arginine except when they are bound to proline. Once in the small intestine, the enzyme enteropeptidase activates it into trypsin by proteolytic cleavage. The cleavage occurs within the polypeptide chain rather than at the terminal amino acids located at the ends of polypeptides.

-	[[2age]]	+	[[2age]]<ref>PMID:16636277</ref>.
		+


	{{STRUCTURE_2age \| PDB=2age \| SCENE= }}		{{STRUCTURE_2age \| PDB=2age \| SCENE= }}
		+
		+	<references/>

Kyle Schroering — Fri, 19 Feb 2010 14:51:37 GMT

←Older revision		Revision as of 14:51, 19 February 2010
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	Trypsin structure contains an aspartate residue (189) in its catalytic pocket that is used to attract and stabilize the positively charged lysine and/or arginine. Therefore, the aspartate residue is responsible for the specificity of the enzyme. Trypsin cleaves protein on the carboxyl end of lysine and arginine except when they are bound to proline. Once in the small intestine, the enzyme enteropeptidase activates it into trypsin by proteolytic cleavage. The cleavage occurs within the polypeptide chain rather than at the terminal amino acids located at the ends of polypeptides.		Trypsin structure contains an aspartate residue (189) in its catalytic pocket that is used to attract and stabilize the positively charged lysine and/or arginine. Therefore, the aspartate residue is responsible for the specificity of the enzyme. Trypsin cleaves protein on the carboxyl end of lysine and arginine except when they are bound to proline. Once in the small intestine, the enzyme enteropeptidase activates it into trypsin by proteolytic cleavage. The cleavage occurs within the polypeptide chain rather than at the terminal amino acids located at the ends of polypeptides.
		+
		+	[[2age]]


	{{STRUCTURE_2age \| PDB=2age \| SCENE= }}		{{STRUCTURE_2age \| PDB=2age \| SCENE= }}

Kyle Schroering — Fri, 19 Feb 2010 14:48:38 GMT

←Older revision		Revision as of 14:48, 19 February 2010
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	==The Mechanism of Trypsin==		==The Mechanism of Trypsin==

-		+	Trypsin structure contains an aspartate residue (189) in its catalytic pocket that is used to attract and stabilize the positively charged lysine and/or arginine. Therefore, the aspartate residue is responsible for the specificity of the enzyme. Trypsin cleaves protein on the carboxyl end of lysine and arginine except when they are bound to proline. Once in the small intestine, the enzyme enteropeptidase activates it into trypsin by proteolytic cleavage. The cleavage occurs within the polypeptide chain rather than at the terminal amino acids located at the ends of polypeptides.


	{{STRUCTURE_2age \| PDB=2age \| SCENE= }}		{{STRUCTURE_2age \| PDB=2age \| SCENE= }}

Kyle Schroering — Fri, 19 Feb 2010 14:46:23 GMT

New page: ==The Mechanism of Trypsin== {{STRUCTURE_2age | PDB=2age | SCENE= }}

New page

==The Mechanism of Trypsin==

{{STRUCTURE_2age | PDB=2age | SCENE= }}