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Chymotrypsin serves as a catalyst in the "Hydrolysis" of pepdite bonds - found in carboxylic groups of amino acids, which consist of aromatic pedand groups and large hydrophobic groups. Chymotrypsin is also known to serve as a catalyst in the Hydrolysis of "ester - and amide bonds" , found in hydrophobic groups. 1. Would you expect the KM of the reactions of Chymotrypsin with the different substrates to have the same value ? explain. 2. Would you expect the Vmax of the reactions of Chymotrypsin with the different substrates to have the same value ? explain. 3. Would you expect the " pH-dependence " of the "hydrolysis - reactions" of the different substrates to be the same for all substrates ? explain your reasoning.

  • 3 weeks later...
Posted

This is a fairly complex question; therefore, a small amount of guidance is not entirely without justification.  The answer to at least one of these questions depends upon whether the substrate is an ester or an amide.

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