The Lineweaver - Burk plot (Figure 1) shows an enzyme-catalyzed reaction in the absence andpresence of 0.1µM inhibitor (ketoconazole).O Estimate Vmax and Km in the absence and presence of the inhibito..(ii) Determine the type of inhibition shown by the inhibitor. Explain.0.1-0.080.06 -With inhibitor0.040.02Without inhibitor0.4 -0.2-0.020.2 0.4 0.6 0.8 1.01/{S\(&M-1)1/vo (pmol-11 min)

In a lineweaver burk plot, x intercept represents the negative reciprocal of Km and y axis…

Answered: The Lineweaver - Burk plot (Figure 1)…

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter25: Nitrogen Acquisition And Amino Acid Metabolism

Section: Chapter Questions

Problem 22P

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An enzyme-catalyzed reaction has a KM of 20.0 mmol L-1 and Vmax of 17.0 pmol s-1. When a mixed inhibitor is added, the apparent KM is 50.0 mmol L-1 and the apparent Vmax is 5.20 pmol s-1. Calculate α.
A particular enzyme-catalyzed reaction has an apparent Vmax = 9.00 nmol s-1 and α' = 3.00 when 2.00 µmol L-1 inhibitor X is present and uncompetitively inhibiting the reaction. Calculate Vmax for the uninhibited reaction in nmol s-1.
The accompanying figure shows three Lineweaver–Burk plots for enzymereactions that have been carried out in the presence, or absence, of aninhibitor. Indicate what type of inhibition is predicted based on eachLineweaver–Burk plot. For each plot indicate which line corresponds to thereaction without inhibitor and which line corresponds to the reaction withinhibitor present.
In an enzyme kinetics study, three inhibitors resulted to the following results: Inhibitor ABC Inhibitor XYZ Inhibitor PQR Without Inhibitor Vmax 40.2 mM/ sec 40.3 mM/ sec 12.32 mM/ sec 65.43 mM/ sec Km 24.3 mM 28.5 mM 24.3 mM 15.7 mM d. Draw the estimated Michaelis Menten Curve of Inhibitor ABC and the curve without the inhibitor.
(b) You are investigating the effects of several agents on the activity of alcohol dehydrogenase. 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 to label all axes. Determine the Vmax and KM for AD from the graphs in each type of plot. AD activity (nM/min) AD activity + agent A (nM/min) AD activity + agent B (nM/min) [Alcohol] (nM) 0.1 14 2 0.5 50 7 8. 1.0 65 10 30 2.0 72 12 45 4.0 80 14 62 8.0 85 15 75 32.0 90 16 90
Shown below are Km, and Vmax values obtained for an enzyme A which catalyze the transformation of the following substrates. Enzyme concentration used was 0.01 M. Km, mM 0.02 Vmax, mM/min 5.3 Substrate 1 2 1.5 13.7 3 2.6 100 4 0.1 25 0.05 62 1. Which substrate have the highest affinity for the enzyme? Explain. 2. Which will show higher efficiency of converting the substrate to the product? Show solutions and еxplain.
1.1)the following data duscribe an enzyme-catalyzed reaction(hydrolysis of cabobenzoxyglycyl-L-tryptophan) Plot these results using a lineweaver-Burk method, and determine values for Km and Vmax. substrate concenrate(mM) Velocity(mM.sec-1) 2,5 0.024 5 0.036 10 0.053 15 0.060 20 0.061 25 0.062 1.2) If the Km of an enzyme for it's substrate remains constant as the concentration of the inhibitor icreaces, what can be said about the mode of inhibition and why? 1.3) calculate the turnover number for an enzyme, assuming Vmax is 0.5M.sec-1 and the concentration of the enzyme used is 0.002M . why is it usefull to know this? 1.4) discuss the mechanism of the bohr effect that occurs during the interactions of Hb with oxygen under physiological conditions in the lungs and tissues. make use of relavant graphs and diagrams to explain your answer.
For the following aspartase reaction in the presence of the inhibitor hydroxymethylaspartate, determine Km and whether the inhibition is competitive or noncompetitive. You have to plot thegraph on the graph paper and also by using excel.[S] V, No Inhibitor V, Inhibitor Present(molarity) (arbitrary units) (same arbitrary units) 1 x 10-4 0.026 0.0105 x 10-4 0.092 0.0401.5 x 10-3 0.136 0.0862.5 x 10-3 0.150 0.1205 x 10-3 0.165 0.142
In an enzyme kinetics study, three inhibitors resulted to the following results: Inhibitor ABC Inhibitor XYz Inhibitor PQR Without Inhibitor V 40.2 mM/sec 40.3 mM/sec 12.32 mM/sec 65.43 mM/sec max K 24.3 mM 28.5 mM 24.3 mM 15.7 mM b. What type of inhibitor is inhibitor PQR? Why do you say so?
You will perform the protocol below for the calf intestinal alkaline phosphatase (CIP) provided. For each reaction, your final enzyme concentration should be 10 nM CIP. Note: Enzymes purchased are typically labelled with their “units of activity” (U), as this relates to how much enzyme is needed to catalyze a reaction. The 100 nM CIP provided has approximately 3 U/mL and was diluted 1 in 1,000 from a 500 U/mL purchased enzyme. 1) Create a table (similar to the one below) to help you determine and keep track of what to add to each of the cuvettes in which your reactions will be measured. The five different concentrations of PNPP should be: 25, 50, 100, 200, 300 μM. Each reaction will be in a final volume of 1 mL and contain 10 nM alkaline phosphatase. Concentrations of stock solutions: 1.0 mM PNPP, 100 nM calf intestinal phosphatase
The enzyme β-methylaspartase catalyzes the deamination of β-methylaspartate. For this aspartate reaction in the presence of the inhibitor hydroxymethylaspartate (3.8 M), determine KM and whether the inhibition is competitive or noncompetitive (KI = 1.0 M). In the ABSENCE of inhibitor: The Lineweaver-Burke equation is 1V=1V= __________ (1[S])(1[S]) + __________, and the KM is __________ M. In the PRESENCE of inhibitor: The Lineweaver-Burke equation is 1V=1V= ____________ (1[S])(1[S]) + ___________, and the KM is ___________ M. The type of inhibition is ____________. Round-off all answers to two (2) significant figures.
Give an example of a noncompetitive inhibitor and its target enzyme. Draw a hypothetical Michaelis-Menten curves in the presence and absence of the noncompetitive inhibitor. Discuss the effects of noncompetitive inhibition and the reasons for these effects on the values of Km and Vmax.

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The Lineweaver - Burk plot (Figure 1) shows an enzyme-catalyzed reaction in the absence and presence of 0.1µM inhibitor (ketoconazole). O Estimate Vmax and Km in the absence and presence of the inhibito.. (i) Determine the type of inhibition shown by the inhibitor. Explain. 0.1