Sandbox 46: Difference between revisions

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Enteropeptidase cleaves after Lysine if it is preceded by 4 Aspartic Acid residues and not followed by a Proline residue. This particular cleavage converts trypsinogen (zymogen) into trypsin.

Once activated, trypsin catalyzes the hydrolysis of peptides into amino acids which the body can absorb during digestion. Trypsin's active site normally contains a triad of residues: Histidine, Serine, and Apartic Acid. The particular mutant form discussed here does not contain this particular active site, but rather 4 different active sites. Click on any of the following links to view a specific active site: <scene name='Sandbox_46/Ac1/1'>Active Site 1</scene> (light blue); <scene name='Sandbox_46/Ac2/1'>Active Site 2</scene> (pink); <scene name='Sandbox_46/Ac3/1'>Active Site 3</scene>(yellow); <scene name='Sandbox_46/Ac4/1'>Active Site 4</scene> (dark blue). This <scene name='Sandbox_46/Ac_all/1'>model</scene> compares the orientation of all four active sites. Site 1 and 3 share a small portion (Arginine residue 42) which is shown in maroon.

Once activated, trypsin catalyzes the hydrolysis of peptides into amino acids which the body can absorb during digestion. Trypsin has an affinity for positively charged molecules; thus, it specifically cleaves on the carboxyl end (after) of Lysine and Arginine, unless Proline follows the residue. Trypsin's active site normally contains a triad of residues: Histidine, Serine, and Apartic Acid. The particular mutant form discussed here does not contain this particular active site, but rather 4 different active sites. Click on any of the following links to view a specific active site: <scene name='Sandbox_46/Ac1/1'>Active Site 1</scene> (light blue); <scene name='Sandbox_46/Ac2/1'>Active Site 2</scene> (pink); <scene name='Sandbox_46/Ac3/1'>Active Site 3</scene>(yellow); <scene name='Sandbox_46/Ac4/1'>Active Site 4</scene> (dark blue). This <scene name='Sandbox_46/Ac_all/1'>model</scene> compares the orientation of all four active sites. Site 1 and 3 share a small portion (Arginine residue 42) which is shown in maroon. Active site three most closely resembles the traditional composition of trypsin's active site.

Sandbox 46: Difference between revisions

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Revision as of 21:38, 29 October 2010 view source Student (talk \| contribs) students 33,923 edits No edit summary ← Older edit		Revision as of 21:52, 29 October 2010 view source Student (talk \| contribs) students 33,923 edits No edit summary Newer edit →
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	Enteropeptidase cleaves after Lysine if it is preceded by 4 Aspartic Acid residues and not followed by a Proline residue. This particular cleavage converts trypsinogen (zymogen) into trypsin.		Enteropeptidase cleaves after Lysine if it is preceded by 4 Aspartic Acid residues and not followed by a Proline residue. This particular cleavage converts trypsinogen (zymogen) into trypsin.
	Once activated, trypsin catalyzes the hydrolysis of peptides into amino acids which the body can absorb during digestion. Trypsin's active site normally contains a triad of residues: Histidine, Serine, and Apartic Acid. The particular mutant form discussed here does not contain this particular active site, but rather 4 different active sites. Click on any of the following links to view a specific active site: <scene name='Sandbox_46/Ac1/1'>Active Site 1</scene> (light blue); <scene name='Sandbox_46/Ac2/1'>Active Site 2</scene> (pink); <scene name='Sandbox_46/Ac3/1'>Active Site 3</scene>(yellow); <scene name='Sandbox_46/Ac4/1'>Active Site 4</scene> (dark blue). This <scene name='Sandbox_46/Ac_all/1'>model</scene> compares the orientation of all four active sites. Site 1 and 3 share a small portion (Arginine residue 42) which is shown in maroon.		Once activated, trypsin catalyzes the hydrolysis of peptides into amino acids which the body can absorb during digestion. Trypsin has an affinity for positively charged molecules; thus, it specifically cleaves on the carboxyl end (after) of Lysine and Arginine, unless Proline follows the residue. Trypsin's active site normally contains a triad of residues: Histidine, Serine, and Apartic Acid. The particular mutant form discussed here does not contain this particular active site, but rather 4 different active sites. Click on any of the following links to view a specific active site: <scene name='Sandbox_46/Ac1/1'>Active Site 1</scene> (light blue); <scene name='Sandbox_46/Ac2/1'>Active Site 2</scene> (pink); <scene name='Sandbox_46/Ac3/1'>Active Site 3</scene>(yellow); <scene name='Sandbox_46/Ac4/1'>Active Site 4</scene> (dark blue). This <scene name='Sandbox_46/Ac_all/1'>model</scene> compares the orientation of all four active sites. Site 1 and 3 share a small portion (Arginine residue 42) which is shown in maroon. Active site three most closely resembles the traditional composition of trypsin's active site.