Sandbox 46: Difference between revisions
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==Structure== | ==Structure== | ||
To follow the primary structure (amino acid sequence) of Trypsin, click <scene name='Sandbox_46/Secondary_structure_tryp/2'>here.</scene> | The trypsin structure displayed is a mutant form isolated from a bovine pancreas. It contains 58 amino acid residues as well as an altered binding loop. To follow the primary structure (amino acid sequence) of Trypsin, click <scene name='Sandbox_46/Secondary_structure_tryp/2'>here.</scene> Begin at the N-terminus (blue) and move toward the C-terminus (red). | ||
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<scene name='Sandbox_46/Polar_vs_nonpolar_wire/1'>Wire</scene> | <scene name='Sandbox_46/Polar_vs_nonpolar_wire/1'>Wire</scene> | ||
==Stability== | ===Stability=== | ||
<scene name='Sandbox_46/Disulfide_bonds/3'>Disulfide</scene> | <scene name='Sandbox_46/Disulfide_bonds/3'>Disulfide</scene> | ||
Revision as of 19:31, 29 October 2010
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Trypsin
Trypsin, a member of the serine protease family, is produced in the pancreas and found in the digestive tracks of vertebrates. To avoid pancreatic self-degradation, trypsin is synthesized as trypsinogen, a zymogen. Cleavage by enteropeptidase allows tryspin to enter its active form. As a serine protease, trypsin contains a serine residue in its active site.
Structure
The trypsin structure displayed is a mutant form isolated from a bovine pancreas. It contains 58 amino acid residues as well as an altered binding loop. To follow the primary structure (amino acid sequence) of Trypsin, click here. Begin at the N-terminus (blue) and move toward the C-terminus (red).
The secondary structure of Trypsin consists of two alpha helices (light green) and two beta sheets (peach). The yellow and red molecules are not part of the Trypsin structure; they were added during crystallization to freeze Trypsin in a specific conformation. Fix THIS. they bind at active site
Stability
Function
The reaction catalysed by Enteropeptidase:
trypsinogen → trypsin + hexapeptide
Val--(Asp)4--Lys--Ile--Val~ (trypsinogen) → Val--(Asp)4--Lys (hexapeptide) + Ile--Val~ (trypsin)
Enteropeptidase cleaves after Lysine if the Lys is preceded by four Asp and not followed by a Pro. Source ^ "Enterokinase, light chain (P8070), Proteases, NEB". https://www.neb.com/nebecomm/products/productP8070.asp. Retrieved 2007-10-04.
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