Sandbox Wabash24
From Proteopedia
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| - | ==Trypsin Mechanism | + | ==Trypsin Mechanism by Andrew Powell, Bilal Jawed, Mazin Hakim == |
<StructureSection load='2agg' size='340' side='right' caption='Acyl intermediate of trypsin catalyzed hydrolysis=''> | <StructureSection load='2agg' size='340' side='right' caption='Acyl intermediate of trypsin catalyzed hydrolysis=''> | ||
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> to stabilize charge in between glycine and serine when the anionic carbonyl oxygen of the scissile peptide approaches. Finally in the creation of trypsin the specificity pocket leads to a binding preference for lysine or arginine. <ref>PMID:16636277</ref> | 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> to stabilize charge in between glycine and serine when the anionic carbonyl oxygen of the scissile peptide approaches. Finally in the creation of trypsin the specificity pocket leads to a binding preference for lysine or arginine. <ref>PMID:16636277</ref> | ||
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== Structural highlights == | == Structural highlights == | ||
| - | Structure also includes sulfate, carbonyl, and Calcium <scene name='72/725353/Labels_of_heme_groups/3'>ligands</scene> | + | Structure also includes sulfate, carbonyl, and Calcium <scene name='72/725353/Labels_of_heme_groups/3'>ligands</scene>. |
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</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
Current revision
Trypsin Mechanism by Andrew Powell, Bilal Jawed, Mazin Hakim
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