Sandbox 32: Difference between revisions
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Trypsin is a medium size globular protein that functions as a pancreatic serine protease. This enzyme hydrolyzes bonds by cleaving peptides on the C-terminal side of the amino acid residues lysine and arginine. It has also been shown that cleavage will not occur if there is a proline residue on the carboxyl side of the cleavage site. Trypsin was first discovered in 1876 by Kuhne, who investigated the proteolytic activity of the enzyme. In 1931 the enzyme was purified by crystallization by Norothrop and Kunitz and later in 1974 the three dimensional structure of trypsin was determined. Throughout the 1990's the role of trypsin in hereditary pancreatitis and the mutation that causes it was discovered. Today trypsin is used in the development of cell and tissue protocols, as well as in the medical field to determine the role of trypsin in pancreatic diseases<ref>Trypsin. 2010. 30 October 2010 <http://www.worthington-biochem.com/tyr/default.html></ref>. | Trypsin is a medium size globular protein that functions as a pancreatic serine protease. This enzyme hydrolyzes bonds by cleaving peptides on the C-terminal side of the amino acid residues lysine and arginine. It has also been shown that cleavage will not occur if there is a proline residue on the carboxyl side of the cleavage site. Trypsin was first discovered in 1876 by Kuhne, who investigated the proteolytic activity of the enzyme. In 1931 the enzyme was purified by crystallization by Norothrop and Kunitz and later in 1974 the three dimensional structure of trypsin was determined. Throughout the 1990's the role of trypsin in hereditary pancreatitis and the mutation that causes it was discovered. Today trypsin is used in the development of cell and tissue protocols, as well as in the medical field to determine the role of trypsin in pancreatic diseases<ref>Trypsin. 2010. 30 October 2010 <http://www.worthington-biochem.com/tyr/default.html></ref>. | ||
[[Image:Tryogen.gif |thumb]] | |||
Trypsinogen is the precursor form or zymogen of Trypsin. Zymogens are enzyme precursors that are made and secreted in the lysosome of the cell. Zymogens are not active until they go through a chemical process such as hydrolysis, cleavage, or other cleavages that reveal the active site. The zymogen precursor is necessary in order to prevent the destruction of cellular proteins and to allow the enzyme to be in it's active state only when in appropriate conditions. Trypsinogen is specifically produced in the exocrine cells of the pancreas. There are three isoforms of Trypsinogen that are secreted by the pancreas. The precursor is only activated when it reaches the lumen of the small intestine. This activation occurs through the help of an enteropeptidase and once activated trypsin stimulates the formation of more trypsinogen<ref>Trypsin. 30 October 2010 <http://www.sigmaaldrich.com/life-science/metabolomics/enzyme-explorer/analytical-enzyme/trypsin.html>.</ref>. The structure of Bovine Trypsinogen is shown in the figure to the right <ref> Image From: http://chemistry.umeche.maine.edu/MAT500/Peptidase1.html</ref>. | |||
==Structure== | ==Structure== | ||
The <scene name='Sandbox_32/N-c_rainbow/2'>pathway</scene> of the protein can be followed from N-terminus of the protein (blue) to the C-terminus of the protein (red). | The <scene name='Sandbox_32/N-c_rainbow/2'>pathway</scene> of the protein can be followed from N-terminus of the protein (blue) to the C-terminus of the protein (red). | ||
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===Oxyanion Hole=== | ===Oxyanion Hole=== | ||
An important motif that is formed in this reaction is an oxyanion hole. This is also shown in the figure to the right <ref> Williams, Loren. Georgia Tech. http://www2.chemistry.gatech.edu/~1W26/bcourse_information/6521/protein/serine_protease/triad_1/html.</ref>. This oxyanion hole is specifically formed between the amide hydrogen atoms of Serine 195 and Glycine 193. This oxyanion hole stabilizes the tetrahedral intermediate through the distribution of negative charge to the cleaved amide <ref>Structural Biochemistry. 10 June 2010. 30 October 2010.<http://en.wikibooks.org/wiki/Structural_Biochemistry/Enzyme/Catalytic_Triad>.</ref>. | An important motif that is formed in this reaction is an oxyanion hole. This is also shown in the figure to the right <ref> Williams, Loren. Georgia Tech. http://www2.chemistry.gatech.edu/~1W26/bcourse_information/6521/protein/serine_protease/triad_1/html.</ref>. This oxyanion hole is specifically formed between the amide hydrogen atoms of Serine 195 and Glycine 193. This oxyanion hole stabilizes the tetrahedral intermediate through the distribution of negative charge to the cleaved amide <ref>Structural Biochemistry. 10 June 2010. 30 October 2010.<http://en.wikibooks.org/wiki/Structural_Biochemistry/Enzyme/Catalytic_Triad>.</ref>. | ||
==Comparison to Chymotrypsin and Elastase== | ==Comparison to Chymotrypsin and Elastase== | ||
<applet scene='Sandbox_32/Chymotrypsin/1' size='275' frame='true' align='true' align='left' caption='Structure of Chymotrypsin and Elastase.'/> | <applet scene='Sandbox_32/Chymotrypsin/1' size='275' frame='true' align='true' align='left' caption='Structure of Chymotrypsin and Elastase.'/> | ||
