49. Proteolytic Catalytic Mechanism. (7 points, 5 parts) Below is a schematic of

Question

49. Proteolytic Catalytic Mechanism. (7 points, 5 parts) Below is a schematic of a serine protease active site & a potential substrate. Use the schematic & the numbered atoms as references if necessary in your responses to answer the following questions. AA-EC 1CH3 20 Draw the H-bonds that would be present in the empty active site. (1 point) B. Chymotrypsin & sin cleave with different specificities. What feature gives n its substrate specificity? (1 point) (Write a full sentence!) C. Fill in the blanks. (2 points) Upon binding to the substrate, atom acts as a(n) & then attacks atom as a (n) This leads to formation which acts of the tetrahedral intermediate D. Fill in the blanks (1 point) Overall, chymotrypsin the bond of the substrate to produce 2 products E. Draw & number the products of the reaction catalyzed by chymotrypsin in the order that they are released from the active site for the substrate depicted in the diagram above. (2 points) Number at least a few of the atoms! Mark clearly all derived from water. Product 1 Product 2: 15

Explanation / Answer

The substrate specificity of Chymotrypsin is due to the complementarity between binding cavity of Chymotrypsin and peptide of substrate.

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