The kinetics of an enzyme (E)-catalyzed reaction are measured over a range of substrate (S) concentrations in the presence or absence of a reversible inhibitor (I). The total enzyme concentration is 10 uM, and the inhibitor concentration used is 50 uM. Analysis of the data indicates that the enzyme operates with typical Michaelis-Menton kinetics. A double-reciprocal (Lineweaver-Burke) plot provides the following information:
y-intercept (absence of I) = 0.75 sec/uM
y-intercept (presence of I) = 2.5 sec/uM
slope (absence of I) = 3.5 sec
slope (presence of I) = 7.0 sec
Calculate the Vmax for this reaction in the absence of inhibitor. Show all work & indicate proper units.
Calculate the Vmax for this reaction in the presence of inhibitor. Show all work & indicate proper units.
Calculate the Km for this reaction in the absence of inhibitor. Show all work & indicate proper units.
Calculate the Km for this reaction in the presence of inhibitor. Show all work & indicate proper units.
The kinetics of an enzyme (E)-catalyzed reaction are measured over a range of substrate (S) concentrations in the presence or absence of a reversible inhibitor (I). The total enzyme concentration is 10 uM, and the inhibitor concentration used is 50 uM. Analysis of the data indicates that the enzyme operates with typical Michaelis-Menton kinetics. A double-reciprocal (Lineweaver-Burke) plot provides the following information:
y-intercept (absence of I) = 0.75 sec/uM
y-intercept (presence of I) = 2.5 sec/uM
slope (absence of I) = 3.5 sec
slope (presence of I) = 7.0 sec
Calculate the Vmax for this reaction in the absence of inhibitor. Show all work & indicate proper units.
Calculate the Vmax for this reaction in the presence of inhibitor. Show all work & indicate proper units.
Calculate the Km for this reaction in the absence of inhibitor. Show all work & indicate proper units.
Calculate the Km for this reaction in the presence of inhibitor. Show all work & indicate proper units.
