Jasper Sandbox 10 - Revision history

Jasper Small at 14:54, 19 February 2010

Jasper Small — Fri, 19 Feb 2010 14:54:14 GMT

←Older revision		Revision as of 14:54, 19 February 2010
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	{{STRUCTURE_2age\| PDB=2age \| SCENE= }}		{{STRUCTURE_2age\| PDB=2age \| SCENE= }}

-	Tryspin is a serine protease, whose function in the body is to hydrolyze peptide bonds of the foodstuffs we eat. Tryspin targets positively charged residues, much like chymotrypsin targets bulky hydrophobic residues and elastase targets small neutral residues. It has three important sites: histidine-57, aspartate-102, and serine-195. The mechanism for the reaction begins with a nucleophilic attack by SER-195. A tetrahedral intermediate forms, which is then decomposed into the acyl-enzyme intermediate. Water then replaces the RNH2 group, eventually binding to the C-terminus and regenerates the enzyme. Hey look at [[2age]].	+	Tryspin is a serine protease, whose function in the body is to hydrolyze peptide bonds of the foodstuffs we eat. Tryspin targets positively charged residues, much like chymotrypsin targets bulky hydrophobic residues and elastase targets small neutral residues. It has three important sites: histidine-57, aspartate-102, and serine-195. The mechanism for the reaction begins with a nucleophilic attack by SER-195. A tetrahedral intermediate forms, which is then decomposed into the acyl-enzyme intermediate. Water then replaces the RNH2 group, eventually binding to the C-terminus and regenerates the enzyme. Hey look at [[2age]]<ref>PMID:166636277</ref>.

Jasper Small at 14:51, 19 February 2010

Jasper Small — Fri, 19 Feb 2010 14:51:40 GMT

←Older revision		Revision as of 14:51, 19 February 2010
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	{{STRUCTURE_2age\| PDB=2age \| SCENE= }}		{{STRUCTURE_2age\| PDB=2age \| SCENE= }}

-	Tryspin is a serine protease, whose function in the body is to hydrolyze peptide bonds of the foodstuffs we eat. Tryspin targets positively charged residues, much like chymotrypsin targets bulky hydrophobic residues and elastase targets small neutral residues. It has three important sites: histidine-57, aspartate-102, and serine-195. The mechanism for the reaction begins with a nucleophilic attack by SER-195. A tetrahedral intermediate forms, which is then decomposed into the acyl-enzyme intermediate. Water then replaces the RNH2 group, eventually binding to the C-terminus and regenerates the enzyme.	+	Tryspin is a serine protease, whose function in the body is to hydrolyze peptide bonds of the foodstuffs we eat. Tryspin targets positively charged residues, much like chymotrypsin targets bulky hydrophobic residues and elastase targets small neutral residues. It has three important sites: histidine-57, aspartate-102, and serine-195. The mechanism for the reaction begins with a nucleophilic attack by SER-195. A tetrahedral intermediate forms, which is then decomposed into the acyl-enzyme intermediate. Water then replaces the RNH2 group, eventually binding to the C-terminus and regenerates the enzyme. Hey look at [[2age]].

Jasper Small at 14:47, 19 February 2010

Jasper Small — Fri, 19 Feb 2010 14:47:07 GMT

←Older revision		Revision as of 14:47, 19 February 2010
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	==The Mechanism of Trypsin==		==The Mechanism of Trypsin==
		+	{{STRUCTURE_2age\| PDB=2age \| SCENE= }}
		+
	Tryspin is a serine protease, whose function in the body is to hydrolyze peptide bonds of the foodstuffs we eat. Tryspin targets positively charged residues, much like chymotrypsin targets bulky hydrophobic residues and elastase targets small neutral residues. It has three important sites: histidine-57, aspartate-102, and serine-195. The mechanism for the reaction begins with a nucleophilic attack by SER-195. A tetrahedral intermediate forms, which is then decomposed into the acyl-enzyme intermediate. Water then replaces the RNH2 group, eventually binding to the C-terminus and regenerates the enzyme.		Tryspin is a serine protease, whose function in the body is to hydrolyze peptide bonds of the foodstuffs we eat. Tryspin targets positively charged residues, much like chymotrypsin targets bulky hydrophobic residues and elastase targets small neutral residues. It has three important sites: histidine-57, aspartate-102, and serine-195. The mechanism for the reaction begins with a nucleophilic attack by SER-195. A tetrahedral intermediate forms, which is then decomposed into the acyl-enzyme intermediate. Water then replaces the RNH2 group, eventually binding to the C-terminus and regenerates the enzyme.
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-	{{STRUCTURE_2age\| PDB=2age \| SCENE= }}

Jasper Small: New page: ==The Mechanism of Trypsin== Tryspin is a serine protease, whose function in the body is to hydrolyze peptide bonds of the foodstuffs we eat. Tryspin targets positively charged residues, m...

Jasper Small — Fri, 19 Feb 2010 14:46:00 GMT

New page: ==The Mechanism of Trypsin== Tryspin is a serine protease, whose function in the body is to hydrolyze peptide bonds of the foodstuffs we eat. Tryspin targets positively charged residues, m...

New page

==The Mechanism of Trypsin==
Tryspin is a serine protease, whose function in the body is to hydrolyze peptide bonds of the foodstuffs we eat. Tryspin targets positively charged residues, much like chymotrypsin targets bulky hydrophobic residues and elastase targets small neutral residues. It has three important sites: histidine-57, aspartate-102, and serine-195. The mechanism for the reaction begins with a nucleophilic attack by SER-195. A tetrahedral intermediate forms, which is then decomposed into the acyl-enzyme intermediate. Water then replaces the RNH2 group, eventually binding to the C-terminus and regenerates the enzyme.

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