Which of the following is incorrect? a. The ratio "catalyzed rate/uncatalyzed rate" is known as catalytic power Ob. Most enzymes exhibit a higher degree of specificity than non-biologic catalysts Most enzymes are proteins; but a few are RNA molecules Od. Most enzymes exhibit a higher catalytic power than non-biologic catalysts O c.

Which of the following does NOT describe enzyme-catalyzed rate acceleration derived from the binding of substrate to enzyme a. repulsion between like charges b. substrate proximity and orientation c. reduction of entropy (increased order) d. desolvation of the substrate by the enzyme active site e. introduction of strain in bonds that need to break

8.Choose the False statement about enzyme binding sites Binding at an allosteric site ca affect binding and catalysis at the Ortho steric site. In addition to ortho steric sites , some enzymes have other sites where catalysis can be conducted. They are called , allosteric sites, from “allo,” the other. In principle, allosteric ligands can have structures that do not resemble those of substrates. Ligand binding at an allosteric site can cause a conformational change of an enzyme. Enzyme can be inhibited by an allosteric ligand that does not complete with substrate.

What kind of catalysis is cysteine driving in this picture? S Los i fy R……—NHR N-H---S O. N-H H-N H-N. O Metal catalysis Covalent catalysis Base catalysis O Acid catalysis NHR²

Which of the following is incorrect about an enzyme-catalyzed reaction? a. Its progress can be monitored as the disappearance of substrate Ob. Its progress can be monitored as the formation of product OC. The reaction rate can be expressed as the change in [enzyme] with time d. None; all the other choices are correct

Consider the following free energy diagram for an uncatalyzed and enzyme-catalyzed reaction. Select all the statements that are true. Without enzyme With enzyme A+B Time AB Oa. The reaction is now spontaneous due to the addition of enzyme b. The rate of the enzyme catalyzed reaction is faster than the uncatalyzed reaction O C. The reaction is exergonic O d. The change in free energy for the reaction is greater in the catalyzed reaction, compared to the uncatalyzed reaction e. The enzyme stabilizes the transition state for the reaction Released Energy pes

4. Using a fluorescent model substrate, you study the kinetics of an enzyme-catalyzed reaction. You observe the below data. Write an equation describing reaction velocity (v) versus [S]. Define and provide a numerical value for any constants that you include in your equation. 16 14 12 4 2 0.0 0.5 1.0 1.5 2.0 2.5 3.0 3.5 [S] / mM `N' at 50 mM and observe the following In pilot experiments, you add the putative inhibitor imidazole Doesn't affect anything 1 reaction velocities: [S] = 1 mM5 µM min-1 [S] = 2 mM9 9 µM min-1 [S] = 4 mM 911 µM min-1 Is imidazole a competitive or non-competitive inhibitor? Provide a brief explanation. > 9 00 v/ µM min-