The steady-state kinetics of an enzyme are studied in the absence and presence of inhibitor A with different concentrati
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The steady-state kinetics of an enzyme are studied in the absence and presence of inhibitor A with different concentrati
The steady-state kinetics of an enzyme are studied in the absence and presence of inhibitor A with different concentration. The reaction rate is given as a function of substrate concentration in the following table: a) Using graph on the last page, create a Lineweaver-Burk plot using a ruler. Be sure to label the axes and the lines. (13 points) b) Use the graph that you made in (a), determine the Vmax and the Km in the absence and presence of inhibitor. (18 points) c) What kind of inhibitor is A? Explain how you reach this conclusion. (4 points) d) This enzyme is a homodimer and each subunit has an active site. If the enzyme concentration is 0.2mM, what is the kcat and the enzyme efficiency? (6 points)
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