Sandbox 46
From Proteopedia
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==Function== | ==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". http://www.neb.com/nebecomm/products/productP8070.asp. | ||
| + | Retrieved 2007-10-04. | ||
<scene name='Sandbox_46/Ac1/1'>Active Site 1</scene> | <scene name='Sandbox_46/Ac1/1'>Active Site 1</scene> | ||
Revision as of 01:56, 29 October 2010
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Contents |
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
To follow the primary structure (amino acid sequence) of Trypsin, click The N-terminus is blue and the C-terminus is red.
The 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". http://www.neb.com/nebecomm/products/productP8070.asp. Retrieved 2007-10-04.
Shared active site
