1. Figure Number: 24-01b
Title: Figure 24.1(b)
Caption: Reaction coordinate diagrams for catalyzed vs. uncatalyzed reaction.
Notes: This figure shows the case where catalysis occurs because the catalyst lowers the energy of the transition state without changing the reaction mechanism.

2. Figure Number: 24-02
Title: Figure 24.2
Caption: Reaction coordinate diagrams for catalyzed vs. uncatalyzed reaction involving change of mechanism.
Notes: This figure shows the case where catalysis occurs because the catalyst lowers the energy of the activated complex by changing the reaction mechanism.

3. Figure Number: 24-03a,b
Title: Figure 24.3
Caption: Reaction coordinate diagrams for specific-acid-catalyzed and general-acid-catalyzed reactions.
Notes: In specific-acid catalysis proton transfer leads to an intermediate preceding the rate-determining step. In general-acid catalysis proton transfer occurs during the rate-determining step

4. Figure Number: UNa,b
Title: Lock-and-Key vs. Induced-Fit Models
Caption: Schematic diagram illustrating the difference between the lock-and-key and induced-fit models of enzyme catalysis.
Notes: In the lock-and-key model the enzyme active site does not change its shape to accommodate the substrate, whereas in the induced-fit model this does occur.

5. Figure Number: 24-06
Title: Top Half of Figure 24.6
Caption: Schematic diagram illustrating shapes and polarities of the binding pockets of trypsin, chymotrypsin, and elastase.
Notes: Shapes and charge distributions in binding pockets explain why trypsin binds long basic (cationic) amino acids, chymotrypsin binds flat, nonpolar amino acids, and elastase binds only small amino acids.

6. Figure Number: 24-10
Title: Figure 24.10
Caption: pH-Rate Profile for Lysozyme.
Notes: The optimum pH for enzyme activity is the pH midway between the pKa of a basic group which needs to be in its basic form to be active and an acidic group which needs to be in its acid form to be active.

7. Figure Number: 24-11
Title: Figure 24.11
Caption: Proposed mehanism of isomerization of d-glucose-6-phosphate to d-fructose-6-phosphate.
Notes: This mechanism involves ring opening, three tautomerization steps which shift the carbonyl by one carbon, and ring closure.

8. Figure Number:
Title: Table The pKa of Metal-Bound Water
Caption:
Notes:

9. Figure Number:
Title: Table Relative Rates of an Intermolecular Reaction and Five Intramolecular Reactions
Caption:
Notes: