In an enzyme kinetics study, three inhibitors resulted to the following results:Inhibitor ABCInhibitor XYZInhibitor PQRWithout InhibitorVmax40.2 mM/ sec40.3 mM/ sec12.32 mM/ sec65.43 mM/ secKm24.3 mM28.5 mM24.3 mM15.7 mMd.Draw the estimated Michaelis Menten Curve of Inhibitor ABC and the curve without the inhibitor.

Vmax km Competitive remains same increases Non Competitive Decreases remains same…

Answered: In an enzyme kinetics study, three…

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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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?
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.. (ii) Determine the type of inhibition shown by the inhibitor. Explain. 0.1- 0.08 0.06 - With inhibitor 0.04 0.02 Without inhibitor 0.4 -0.2 -0.02 0.2 0.4 0.6 0.8 1.0 1/{S\(&M-1) 1/vo (pmol-11 min)
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.
a. Calculate both Vmax and KM for the control using Lineweaver-Burk curve. b. Provide the type of inhibition for both? Find, KI, for the inhibitor binding to the enzyme, for experiments (2) and (3). d. Calculate the reaction Kcat for the Control in experiment (1). e. Draw a velocity versus [S] showing Michaelis-Menten curve for the Control. Clearly show Vmax and Ky for the enzyme. c. (1) V. [(umol/(ml.s)] 7.6 (2) V- Τ (μmol/ (ml.s)] [S] (mM) (3) V. [(umol/(ml.s)] 6.6 2 4 14.6 26.6 45.8 4.4 8.6 16.4 29.8 11.4 17.8 24.6 28.2 16 24 60 40.8
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.
Note the Michaelis Menton kinetics results of inhibition by inhibitor A and by B, separately. Normal enzyme Inhibitor A Convert these to lineweaver burke in graphs below. -5+ -4 Inhibitor B -3+ -2 Effect of Inhibitor A. Draw uninhibited first and then draw the result- ing inhibition for comparison. What kind of an inhibitor is A? How can you tell? Effect of Inhibitor B. Draw uninhibited first and then draw the result- ing inhibition for comparison. What kind of an inhibitor is B? How can you tell?
8) plot of enzyme activity with and without an inhibitor present gave the following plot. What type of inhibitor is present? How does this inhibitor function? What changes are seen in Vmax and KM? Draw a line that approximates the result from addition of twice as much inhibitor to the reaction. 1/v (v in mM/min) 0.8 0.6 0.4 0.2 0 0.2 0.4 06 1/[s] ([S] in mM) 0.8
For an enzyme that displays Michaelis-Menton kinetics, what is thereaction velocity, V (as a percentage of V max , observed at the followingvalues?[S] = K M[S] = 0.5K M[S] = 0.1K M[S] = 2K M[S] = 10K M
From your Lineweaver-Burk plot,the vlaues are: Km Vmax Uninhibited 0.09 mmol/L 3.02 min/mmol Inhibited 6.22 mmol/L 9.98 min/mmol By describing the potential changes in the kinetic parameters, identify and justify the type of inhibitor that was inhibiting the acid phosphatase activity.
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.
Calculate the slope on a Lineweaver-Burk plot (Km / Vmax) for the lactase reaction with inhibitor X. (inhibitor X changes lactase activity to a Vo of 0.10 mM per minute when [S] = 1.0 mM, and a Vo of 0.133333333333 mM per minute when [S] = 2.0 mM) 0.20 per minute 0.50 per minute 1.0 per minute 2.0 per minute 5.0 per minute

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