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8. Aminopeptidase is an enzyme that removes an amino acid from the N-terminus of a polypeptide chain by cleaving the peptide bond that connects it to the rest of the chain. This process can be inhibited by the molecule shown below. a. What similarities and differences do you observe when you compare the structure of the inhibitor to the structure of the enzyme's natural substrate? b. Shown below is the arrow pushing mechanism for the first step of the reaction catalyzed by this aminopeptidase. Draw the transition state for this reaction. In your transition state, show bonds that are breaking and forming using dashed lines. Be sure to show partial charges whenever a formal charge is developing or dissipating. c. Based on the structure of the inhibitor and the arrow pushing mechanism from part b, propose an explanation for why this inhibitor binds more strongly to the enzyme than the natural substrate does. Your answer should discuss both molecular geometry as well as charges