a) The Km of an enzyme of an enzyme-catalyzed reaction is 7.5 ïM. What substrate concentration will be required to obtain 65% of Vmax for this enzyme? (same enzyme was used in part a and b) (6 points)

b) Calculate the Ki for a competitive inhibitor whose concentration is 7 x10-6 M. The Km in the presence of inhibitor was found to be 1.2x10-5 M. (6 points)

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Deanna HettingerLv2

28 Sep 2019

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a) The Km of an enzyme of an enzyme-catalyzed reaction is 7.5 ïM. What substrate concentration will be required to obtain 75% of Vmax for this enzyme? (same enzyme was used in part a and b) (6 points) b) Calculate the Ki for a competitive inhibitor whose concentration is 7.5 x10-6 M. The Km in the presence of inhibitor was found to be 1.25x10-5 M. (6 points)

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violetrabbit340

This is all the information given. I am having an issue posting the photo of the plot, but I'm pretty sure all you need are the trendline equations for the inhibitor and without the inhibitor, which I have provided.

The Lineweaver-Burk plot (1/v vs 1/[S]) for an enzyme-catalyzed reaction in the presence and absence of an inhibitor provides the lines y = 0.663x + 0.0222 (no inhibitor) and y = 0.224x + 0.0224 (inhibitor). (The units for 1/v are mmol/min and the units for 1/[S] are mM.)

A) What type of inhibitor was used to obtain this data?

B) What are the KM and Vmax values for the non-inhibited enzyme?

C) What are the apparent KM of the inhibited enzyme?

D) What is the alpha value?

E) What is the KI of the inhibitor if 1 mM of inhibitor was used

Enzyme kinetics for biochemistry.

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 V_max for this reaction in the absence of inhibitor. Show all work & indicate proper units.

Calculate the V_max for this reaction in the presence of inhibitor. Show all work & indicate proper units.

Calculate the K_m for this reaction in the absence of inhibitor. Show all work & indicate proper units.

Calculate the K_m for this reaction in the presence of inhibitor. Show all work & indicate proper units.