(b) You are investigating the effects of several agents on the activity of alcoholdehydrogenase. The enzyme activity data are shown in the table below. Construct a[substrate] vs. activity plot and a double-reciprocal plot for this enzyme. Be sure tolabel all axes. Determine the Vmax and KM for AD from the graphs in each type ofplot.AD activity(nM/min)AD activity + agent A(nM/min)AD activity + agent B(nM/min)[Alcohol] (nM)0.11420.55078.1.06510302.07212454.08014628.085157532.0901690

Km and Vmax can be calculated from the graphs that are plotted between substrate concentration and…

Answered: (b) You are investigating the effects…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Given the following information, calculate the catalytic efficiency of the enzyme. Step by step please [S] = 100 mM k1 = 10 sec-1 k2 = 3000 sec-1 k-1 = 20 sec-1 [E]T = 1 \muμM
Please label (a) from (b)
What is the impact of the lower value Vmax on the affinity for enzyme for substrate? And what is impact of the lower V max on the amount of product formed ? If the lower value of black resulting in the new plot (red curve) is due to presence of enzyme inhibitor is the inhibitor reversible or irreversible ? And why?
KM is determined by measuring the reaction velocity of two enzymes (X and Y) at different concentrations. The curves for X and Y were sigmoid and hyperbolic, respectively. How are these graphs different, and why?
Enzyme X can be inhibited by two distinct inhibitors, only one of which is acting as a competitive inhibitor, while the other one is non-competitive. The three plots below (designated A, B, and Cy show Michaelis-Menten kinetics for the reactions carried out with the same concentr ation of the enzyme and either in the absence of any inhibitors or in the presence of one of the two inhibitors. Match the type of reaction (uninhibited, competitive inhibition, non-competitive inhibition) with the corresponding plot? Plot A Plot B Plot C Substrate concentration 1.Plot A v LUninhibited roaction 2. Plot C v Inhibition by a competitive inhibitor 3Plot B v Inhibition by a non-competitive inhibitor A Moving to another question will save this response. lup
Use the plot provided to estimate Km and Vmax values for both with and without inhibitor of the enzyme catalyzed reactions.
Please see the attached image.
During a test of kinetics of an enzyme-catalyzed reaction, the following data were recorded: E, () T(C) I (mmol/ml) S (mmol/ml) V (mmol/ml-min) 1.6 1.6 30 0.1 2.63 1.92 147 30 0.033 1.6 30 0.02 0.01 0.005 16 30 0.96 0.56 5.13 1.6 30 1.6 49.6 0.1 1.6 49.6 0.033 3.70 1.89 1.6 1.6 1,6 49.6 0.01 0.0067 49.6 1.43 49.6 0.005 LII 0.92 30 0.1 1.64 0.02 0.01 0.1 0.90 0.92 0.92 30 30 0. 0.58 0.92 30 0.6 0.92 0.92 30 30 0.6 0.6 0.033 0.02 1.33 0.80 0.57 a. Determine the Michaelis-Mentcn constant for the reaction with no inhibitor present at 30°C and at 49.6°C. b. Determine the maximum velocity of the uninhibited reaction at 30°C and an enzyme concentration of 1.6 g/l. c. Determine the KI for the inhibitor at 30*C and decide what type of inhibitor is being used.
Use the relationships revealed by a Lineweaver–Burk plot and the table of enzyme performance to calculate the ?max and ?M of the enzyme with no inhibitor, with inhibitor A, and with inhibitor B. Substrate concentration, [S], has units of micromolar, μM. Enzyme velocity, ?0, has units of micromole per minute, (μmol/min). Using data from only the extremes of the [S] range is unreliable. Select the type of inhibition displayed by inhibitor A. competitive noncompetitive uncompetitive Select the type of inhibition displayed by inhibitor B. competitive noncompetitive uncompetitive
Draw a hypothetical Michaelis-Menten plot for an enzyme reaction (i) without and (ii) with a pure noncompetitive inhibitor. Label Vax and Km on plot
The following question focuses on how the parameters regulating enzyme function might change, and how these might appear graphically on a Michaelis-Menten plot and a Lineweaver-Burke plot. Carbonic anhydrase is an enzyme that will convert CO2 and water into HCO3. CO2 + H20 > H+ + HCO3 There are many different isoforms of this enzyme. Morphine is a non-competitive inhibitor of carbonic anhydrase. Draw on the same Lineweaver-Burke plot as above a graph showing the effect of a concentration of morphine that inhibits the first enzyme such that it reduces the Vmax to ½ its maximal value. Make sure to put in sample data points. Imidazol is a competitive inhibitor of carbonic anhydrase. It is effective at an alkaline (high) pH; in lower (more acidic) pH, it no longer inhibits the enzyme. Draw on a separate graph a Lineweaver-Burke plot for the effects of this compound at high pH and low pH. Be sure to label the axes and put in sample data points.
What type of inhibition is being shown in the following graphs?

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