Sandbox Wabash24

==Trypsin Mechanism (By: Andrew Powell, Bilal Jawed, Mazin Hakim) ==

Trypsin is a serine protease that catalyzes acyl peptide bonds. It is specific for positively charged residues. The <scene name='72/725353/His_57/6'>His 57</scene> and <scene name='72/725353/Ser_195/2'>Ser 195</scene> are located in the active site of the trypsin. The role of asp 102 and his 57 during Trypsin catalysis is to effectively function as a proton shuttle. Location of <scene name='72/725353/Asp_102/4'>Asp 102</scene> residue which shows the beta sheet regular secondary structure. The trypsin mechanism is defined by 2 separate reactions. The mechanism begins by the breaking of the scissile bond in the substrate polypeptide. A tetrahedral intermediate forms followed by an acyl-enzyme intermediate. The C terminus then departs followed by the creation of an additional tetrahedral intermediate. Finally the N terminus of the substrate polypeptide exits, leaving the active enzyme. Trypsin also contains a <scene name='72/725353/Catalytic_triad/1'>catalytic triad</scene> to either split a substrate or transfer a substrate. The triad in trypsin consists of histidine, aspartate, and serine. In addition to this triad Trypsin also contains an <scene name='72/725353/Oxyanion_hole/2'>oxyanion hole</scene> consisting of glycine and serine to stabilize the charge. Finally in the creation of trypsin the specificity pocket leads to a binding preference for lysine or arginine. <ref>PMID:16636277</ref>

Structure also includes sulfate, carbonyl, and Calcium <scene name='72/725353/Labels_of_heme_groups/3'>ligands</scene>

<scene name='72/725353/Labels_of_heme_groups/1'>Heme Groups</scene>