How is this NONcompetitive inhibition ? How do I find the Vmax ?
How is this NONcompetitive inhibition ?
How do I find the Vmax ?
Homework Answers
Vmax = k2 [Eo] = 900 s-1 x 0.1nM = 90 nM/s
After the addition of the inhibitor, the effective enzyme concentration is lower and also Vmax is lower (50 nM/s).
The evidence that the inhibition is non competitive is the experimental fact that:
apparent Km = initial Km
and only Vmax is reduced.
b. Uncompetitive inhibition. c. Mixed inhibition. d. Pure noncompetitive inhibition. 22. What type of inhibition is...
b. Uncompetitive inhibition. c. Mixed inhibition. d. Pure noncompetitive inhibition. 22. What type of inhibition is the Lineweaver-Burk plot? 1/yo a. Competitive inhibition. b. Uncompetitive inhibition. c. Mixed inhibition. d. Pure noncompetitive inhibition. 23. In the Question 22, how do the values of [I] change in the 1/[S] arrow's direction? a. Increasing. b. Decreasing c. Increasing or decreasing. d. Do not change 24. Which of the following inhibition types cause ESI? n Competitiye, uncompetitive, and mixed inhibition
biochemistry: how do noncompetitive, mixed, and uncompetitive inhibitors affect Km and Vmax?
biochemistry: how do noncompetitive, mixed, and uncompetitive inhibitors affect Km and Vmax?
A simple noncompetitive inhibitor of acetylcholinesterase binds to the enzyme to affect Vmax only; it does...
A simple noncompetitive inhibitor of acetylcholinesterase binds to the enzyme to affect Vmax only; it does not affect KM. Part A For an inhibition constant of KI=2.9×10?4M, what concentration of inhibitor is needed to give a 90% inhibition of the enzyme? Express your answer using two significant figures and include the appropriate units. [I] =
Which general mechanisms could be responsible for the initial inhibition of glycolysis during oxidative stress? Choose all that apply. Competitive Inhibition Noncompetitive Inhibition O Uncompetitive...
Which general mechanisms could be responsible for the initial
inhibition of glycolysis during oxidative stress? Choose all that
apply.
Competitive Inhibition Noncompetitive Inhibition O Uncompetitive Inhibitionn Transcriptional Modification
Competitive Inhibition Noncompetitive Inhibition O Uncompetitive Inhibitionn Transcriptional Modification
Please show the rate law. (See p. 413 and Fig. 7-11) ki E+ SHE-S Noncompetitive inhibition:...
Please show the rate law.
(See p. 413 and Fig. 7-11) ki E+ SHE-S Noncompetitive inhibition: the inhibitor attaches k2 kz to only one type of site and the substrate only to the E+I+E: 1 other site on the enzyme. E-S+1 HS.E:1 Please show the rate law (Homework): Vmax [S] L ([S]+KD)(1+ E:I+S4SE1 E-Sky >E+P
1. Explain the difference between competitive and noncompetitive inhibition. I am having a hard time understanding...
1. Explain the difference between competitive and noncompetitive inhibition. I am having a hard time understanding the difference between the two. Could someone please explain the difference between the two? 2. Could someone also give an example of one drug that acts as an enzyme inhibitor and explain its mechanism of action.
Compare competitive and noncompetitive inhibition Question An enzyme is placed in the presence of an unknown...
Compare competitive and noncompetitive inhibition Question An enzyme is placed in the presence of an unknown substance to determine whether the substance is an inhibitor. As the substrate concentration is increased, the rate of reaction is compared to the normal rate of reaction. Initially, the rate is equal to normal, and as the substrate concentration is increased more and more, the rate of reaction remains the same as the normal rate. What can be concluded about the unknown substance? Select...
Compare competitive and noncompetitive inhibition Question An enzyme is placed in the presence of an unknown...
Compare competitive and noncompetitive inhibition Question An enzyme is placed in the presence of an unknown substance to determine whether the substance is an inhibitor. As the substrate concentration is increased, the rate of reaction is compared to the normal rate of reaction. Initially, the rate is slower than normal, but as the substrate concentration is increased more and more, the rate of reaction approaches normal. What can be concluded about the unknown substance? Select the correct answer below: O...
Based on the graph of the "Determination of Km and Vmax" and "inhibition Studies" tube data,...
Based on the graph of the "Determination of Km and Vmax"
and "inhibition Studies" tube data, what do you believe to be the
mode of inhibition by PTU? Why?
LINEWEAVER-BURKE PLOT FOR UNINHIBITED AND INHIBITED ENZYME United: 51. 81611.8755 ntion of and me Bed on the graph of the e w by Prut Why?
Which is the most inappropriate description of enzyme inhibition? Select one: a. A competitive inhibitor increases...
Which is the most inappropriate description of enzyme inhibition? Select one: a. A competitive inhibitor increases Km only. b. A noncompetitive inhibitor decreases Vmax only. c. An uncompetitive inhibitor decreases both Km and Vmax. d. All of the above e. None of the above
b. Uncompetitive inhibition. c. Mixed inhibition. d. Pure noncompetitive inhibition. 22. What type of inhibition is the Lineweaver-Burk plot? 1/yo a. Competitive inhibition. b. Uncompetitive inhibition. c. Mixed inhibition. d. Pure noncompetitive inhibition. 23. In the Question 22, how do the values of [I] change in the 1/[S] arrow's direction? a. Increasing. b. Decreasing c. Increasing or decreasing. d. Do not change 24. Which of the following inhibition types cause ESI? n Competitiye, uncompetitive, and mixed inhibition
Which general mechanisms could be responsible for the initial
inhibition of glycolysis during oxidative stress? Choose all that
apply.
Competitive Inhibition Noncompetitive Inhibition O Uncompetitive Inhibitionn Transcriptional Modification
Competitive Inhibition Noncompetitive Inhibition O Uncompetitive Inhibitionn Transcriptional Modification
Please show the rate law.
(See p. 413 and Fig. 7-11) ki E+ SHE-S Noncompetitive inhibition: the inhibitor attaches k2 kz to only one type of site and the substrate only to the E+I+E: 1 other site on the enzyme. E-S+1 HS.E:1 Please show the rate law (Homework): Vmax [S] L ([S]+KD)(1+ E:I+S4SE1 E-Sky >E+P
Compare competitive and noncompetitive inhibition Question An enzyme is placed in the presence of an unknown substance to determine whether the substance is an inhibitor. As the substrate concentration is increased, the rate of reaction is compared to the normal rate of reaction. Initially, the rate is equal to normal, and as the substrate concentration is increased more and more, the rate of reaction remains the same as the normal rate. What can be concluded about the unknown substance? Select...
Compare competitive and noncompetitive inhibition Question An enzyme is placed in the presence of an unknown substance to determine whether the substance is an inhibitor. As the substrate concentration is increased, the rate of reaction is compared to the normal rate of reaction. Initially, the rate is slower than normal, but as the substrate concentration is increased more and more, the rate of reaction approaches normal. What can be concluded about the unknown substance? Select the correct answer below: O...
Based on the graph of the "Determination of Km and Vmax"
and "inhibition Studies" tube data, what do you believe to be the
mode of inhibition by PTU? Why?
LINEWEAVER-BURKE PLOT FOR UNINHIBITED AND INHIBITED ENZYME United: 51. 81611.8755 ntion of and me Bed on the graph of the e w by Prut Why?
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