2. Metal ion catalysis in a protease (30 points). Some proteases contain a metal

Question

2. Metal ion catalysis in a protease (30 points). Some proteases contain a metal ion in their active site that participates in peptide bond hydrolysis. The reaction in the active site of one such protease is depicted below: Substrate Products R2 NH O NH3 H N His T His Asp His Asp IS IS His His c. The following compound is a transition state analog that was developed as a selective inhibitor for this enzyme: Redraw this compound and circle the functional group(s) designed to mimic the transition state. Which chemical features of the transition state does this functional group successfully mimic? d. This transition state analog is a selective inhibitor of this particular enzyme. Why would we expect a transition state analog to be an effective enzyme inhibitor? (2- 3 sentences) e. Based on the structure of this compound, which amino acid side chain would you expect to find at the P1' position of the enzyme's preferred substrate (see the substrate side chain nomenclature for chymotrypsin)? Why? (1-3 sentences)

Explanation / Answer

amino side chain would i expect to do something at p1 position is not possible for anything to regenrate.

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