Exam 1 Review - Enzyme Kinetics & Hemoglobin and Myoglobin Binding

Exam 1 Review - Enzyme Kinetics & Hemoglobin and Myoglobin Binding

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Kaiser Imam September 23, 2007 BIOL 215 Exam 1 Review Enzyme Kinetics 1. Why does v max but not K m depend on the amount of enzyme used in an enzyme reaction? 2. Write out the direct kinetic function. 3. The following data were obtained by measuring the change in reaction rate in an enzyme- catalyzed reaction over time. The k cat for the enzyme is known to be 1500 min -1 . Find the K m and the total enzyme concentration value from the data below: [S] (mM) v o (μmol/min) 1.00 49 2.00 96 8.00 349 50.00 621 100.00 676 1000.00 698 5000.00 699 4. What is the equation for the Lineweaver-Burk plot and what does it tell you? 1
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For a one-substrate, enzyme-catalyzed reaction Lineweaver-Burk plots were determined for three different enzyme concentrations . Which of the following three sets of plots would best describe this situation? 6. What is the equation for the Eadie-Hofstee plot? 7. What are the three types of inhibition? 1) 2) 3) 8. Modify the Michaelis-Menten mechanism to explain the various types of reversible inhibition and describe which type of inhibition is occurring in each. 2
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Exam 1 Review - Enzyme Kinetics & Hemoglobin and Myoglobin Binding

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