Sandbox 46: Difference between revisions

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).