User:Karsten Theis/Trypsin

This is a lesson on Trypsin, a serine protease. It assumes you already know how chymotrypsin, another serine protease, works. It explores substrate specificity, activation and degradation, and relationship to thrombin.

By the end of this brief session, students will be able to:

• Explain how substrate specificity in trypsin is achieved, emphasizing the role of Asp189 in recognizing and binding positively charged residues like Arg and Lys.

• Compare the substrate-binding pockets of trypsin and chymotrypsin, noting how differences in residue composition drive specificity.

• Describe the biological importance of regulating trypsin activation and degradation, considering the fact that a significant portion of amino acids in the gut come from digestive enzymes themselves.

• Recognize the historical and structural relevance of trypsin as a model for thrombin, and appreciate how this influenced early biochemical and structural studies.

Center on:

Figures

spinqualitylabelsall models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Figure 1: overall view Transition: overall view in 1oph Figure 2: P1 pocket with mesh Figure 3: with mesh Figure 4: Trypsinogen superposition Figure 5: inhibitor complex Further reading https://www.worthington-biochem.com/products/trypsin/manual (alpha trypsin, beta, anionic, cationic...) anhydro: treated to convert serines to anhydroalanines https://www.elegantexperiments.net/en/post/length-digestive-system/ digestive tract length https://derangedphysiology.com/main/cicm-primary-exam/gastrointestinal-system/Chapter-110/composition-volumes-and-regulation-gastrointestinal-secretions volume of secretions https://pubmed.ncbi.nlm.nih.gov/24694282/ Surface area (tennis court or badminton court?)

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Karsten Theis