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Calculate the V max and K M for this enzyme

You perform enzyme assays with 0.005 uM enzyme with the given substrate concentrations, and measured the corresponding initial velocities. Graph a Lineweaver -Burk plot of the following data:. Calculate the V max and K M for this enzyme. What is the K cat for this enzyme?.

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Calculate the V max and K M for this enzyme

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  1. You perform enzyme assays with 0.005 uM enzyme with the given substrate concentrations, and measured the corresponding initial velocities. Graph a Lineweaver-Burk plot of the following data: Calculate the Vmax and KM for this enzyme

  2. What is the Kcat for this enzyme? What is the catalytic efficiency? Is this an efficient enzyme? Draw the Michaelis-Menton curve for this enzyme

  3. You perform the same assay, this time in the presence of 4 mM Inhibitor A, and measure the following initial velocities. Plot the data on the same Lineweaver-Burk plot as the uninhibited data. What type of inhibitor is this?

  4. What is the KI for this inhibitor? Plot the data on the previous Michaelis-Menton curve

  5. You assay 0.00004 uM enzyme A at two different substrate concentrations in the presence and absence of an inhibitor with the following results: • Construct a Lineweaver-Burk plot of the data

  6. You assay 0.00004 uM enzyme A at two different substrate concentrations in the presence and absence of an inhibitor with the following results: • Determine the following for the enzyme in the absence of inhibitor: • Vmax; KM; and Kcat • Determine the following in the presence of inhibitor: • Vmax; apparent KM

  7. Do you expect the inhibitor to bind to: • The enzyme’s substrate binding site? • A separate regulatory site? • Free enzyme? • E-S complex?

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