bioanalytical chemistry

PS #4 CHM 3450 Name: Note: Review appropriate topics and provide detailed answers wherever appropriate. 1. Describe the term ‘apoenzyme’. 3.Explain the term ‘initial velocity’ used in enzyme kinetics. 4. Give the mathematical and qualitative definition of Km 5 Calculate the substrate concentration, if an enzyme-catalyzed reaction has a Km of 5 mM and a Vmax of 60 nM/sec, at velocity of 30 nM/sec. 6 Using biochemical terms describe the effect of temperature and pH on an enzyme catalyzed reaction. 7. Provide the equation for turnover number and explain all the terms. 8. In noncompetitive inhibition, the inhibitor can bind to: a) enzyme (E) d) a and b b) the enzyme-substrate complex (ES) e) b and c c) the product (P) 9. What characteristics are typically found at the active site an enzyme? 10. All of the following are correct statements about enzyme regulation EXCEPT: a. Enzymes can be inhibited by the products they produce. b. Enzymes can be inactivated by the addition of a functional group. c. Coenzyme and substrate availability can regulate enzyme reaction rate. d. The reaction rate slows as equilibrium is approached. e. The activity of an enzyme is covalently affected by allosteric regulators. 11. Why is histidine a particular versatile amino acid residue in its involvement in enzymatic reaction mechanisms? 12. Using Cartoons, show the following (a) Uncompetitive inhibition (b) Induced fit model of substrate binding.