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spinqualitylabelsall models Trypsin Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D

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 here. The N-terminus is blue and the C-terminus is 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

polar vs. nonpolar

Wire

Stability

Disulfide

DS bonds labeled

H bonds backbone

H bonds r groups

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.

Active Site 1

Active Site 2

Active Site 3

Active Site 4

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