Enzyme Kinetics_PS8_F10

Enzyme Kinetics_PS8_F10 - CHEM 4511/6501 Problem Set 8 1...

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CHEM 4511/6501 Problem Set 8 1. Consider the nonenzymatic elementary reaction A B. When the concentration of A is 20 mM, the reaction velocity is measured as 5 μ M B produced per minute. Calculate the rate constant for this reaction. 2. Explain why each of the following data sets from a Lineweaver-Burk plot are not individually ideal for determining the K M for an enzyme-catalyzed reaction that follows Michaelis-Menten kinetics. Set A 1/[S] (mM -1 ) 1/v ( μ M -1 ·s) 0.5 2.4 1.0 2.6 1.5 2.9 2.0 3.1 Set B 1/[S] (mM -1 ) 1/v ( μ M -1 ·s) 8 5.9 10 6.8 12 7.8 14 8.7 3. Calculate K M and V max from the following data: [S] ( μ M) V (mM·s -1 ) 0.1 0.34 0.2 0.53 0.4 0.74 0.8 0.91 1.6 1.04 4. You are attempting to determine K M by measuring the reaction velocity at different substrate concentrations, but you do not realize that the substrate tends to precipitate under the experimental conditions you have chosen. How would this affect your measurement of K M ? 5. The K M for the reaction of chymotrypsin with N -acetylvaline ethyl ester is 8.8 x 10 -2 M, and the K M for the reaction of chymotrypsin with
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This note was uploaded on 11/04/2010 for the course CHEM 6501 taught by Professor Wendyl.kelly during the Fall '10 term at Georgia Tech.

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Enzyme Kinetics_PS8_F10 - CHEM 4511/6501 Problem Set 8 1...

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