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problem_set_5 - Problem Set#5 BMB 401 Spring 2004 Problems...

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Problem Set #5 BMB 401 Spring 2004 Problems from Lehninger: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 12, Problem 1 – The k cat for alkaline phosphatase-catalyzed hydrolysis of methylphosphate is approximately 14 sec -1 at pH 8 and 25°C. The rate constant for the uncatalyzed hydrolysis of methylphosphate under the same conditions is approximately 1 x 10 -15 sec. What is the difference in the free energies of activation of these two reactions? Problem 2 – For a Michaelis–Menten reaction (shown below), k 1 = 7 x 10 7 M -1 sec -1 , k -1 = 1 x 10 3 sec -1 , and k 2 = 2 x 10 4 sec -1 . What are the values of K s and K M ? Does substrate binding approach equilibrium or does it behave more like a steady-state system? Problem 3 – The following kinetic data were obtained for an enzyme in the absence of any inhibitor ( 1 ), and in the presence of two different inhibitors ( 2 ) and ( 3 ) at 5 mM concentration. Assume [E T ] is the same in each experiment. [S] (mM) ( 1 ) ν (μmol mL -1 sec -1 ) ( 2 ) ν (μmol mL -1 sec -1 ) ( 3 ) ν (μmol mL -1 sec -1 ) 1 12 4.3 5.5 2 20 8 9 4 29 14 13 8 35 21 16 12 40 26 18 a. Determine V max and K M for the enzyme.
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