Sandbox 46
From Proteopedia
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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. such, it contains a serine residue in the 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
Shared active site
