Answer the table below and show complete handwritten solution Consider the given data for an enzyme-catalyzed reaction. Determine the Vm, Km andthe type of inhibition based on the given data below.Substrate concentration,mmol/LExperiment A(Initial velocity withoutinhibitor, mmol/L-min)Experiment B(Initial velocity with inhibitor,mmol/L-min)0.7100.2000.1800.4000.1800.1500.3100.1600.1100.0980.1200.0700.0660.1000.0500.0400.0700.040Complete the table below (include correct units).Experiment AExperiment Bslopey-interceptVmKmType of Inhibition:

Enzyme kinetics are explained by Michaelis Menten equation which is as below: V=Vmax[S]Km+[S] Here,…

Answered: Experiment A (Initial velocity without…

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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Similar questions

You were asked to determine the mode of inhibition exerted by Inhibitor DEDS to a newly discovered enzyme known as BILISTASE. The kinetics data are shown below: [Substrate, uM) Vo with DEDS (uM/min) Vo without DEDS (uM/min) 1.667 1.600 3.544 2.500 1.923 4.259 3.333 2.139 4.737 14.000 2.268 5.019 5.000 2.410 5.336 Using linear regression analysis, determine the values of Vmax and KM of the enzyme in the ABSENCE of inhibitor: (Express your answer in 3 decimal places, do NOT include the units) Vmax KM
The table below contains experimental data for the enzyme A; substrate concentration (mM) and initial velocity (mM/min). Plot a suitable graph and calculate the Km and Vmax for this enzyme. In 2. your answer, insert an image of the graph and show your calculations. Substrate concentration; [S] (mM) Initial Velocity; Vo (mM/min) 10.00 33.33 5.00 20.00 3.33 14.29 2.50 11.11
The change in the amount of product B in a reaction which is catalyzed by Enzyme A is given in the table below. Determine the Vmax and Km of the enzyme in the absence and presence of C. Is C an inhibitor or an activator of enzyme A? Determine the type of inhibition or activation. Rate of formation of Product B in the presence of 25 mg/mL C (mM/min) Substrate Rate of formation of (mM) Product B (mM/min) 0.5 21.5 14.1 1 30.2 22.2 1.5 34.9 27.0 2.5 39.8 33.1 3.5 42.0 36.3
Compound A is the substrate for two enzymes, El and E2, their reaction rates, r1 and r2,Determine the Km and rmax for both enzymes, with respect to the concentration of A. Which set of data is more likely to be for El and which for E2, and why? Concentration of 0.2 0.6 1.2 3 4 5 6 8 12 15 A (mM) Reaction rate (r.) (mmol/L'min) 3.33 4.29 4.62 4.76 4.84 4.88 4.9 4.92 4.94 4.95 4.96 4.97 Reaction rate (r,) (mmol/L*min) 0.09 0.23 0.38 0.5 0.6 0.67 0.71 0.75 0.8 0.82 0.86 0.80
Vo 60 50 40 30 20 mm/sec 0100 0 O 0 0 50 100 150 200 250 300 Substrate (mM) Use the Michaelis-Menten plot to answer this question. What is the estimated value of Vmax of the enzyme catalyzed reaction (square data points)? (choose the one best answer) 10
From the following data of an enzymatic reaction, determine the type of inhibition, the KM for the substrate and Ki for the enzyme-inhibitor complex. [S] mM 2.0 3.0 4.0 10.0 15.0 [P] mM/h (without inhibitor) 139 179 213 313 370 [P] mM/h ([I]=6mM) 88 121 149 257 313
An experiment on enzyme-catalyzed reaction was conducted in the laboratory by a student. Results obtained are summarized in the table below. In all the experiments, the concentration of the enzyme is the same. Substrate Concentration Velocity (pmol/min) (pmol) 1.5 0.21 3 0.28 4 0.32 0.36 8 0.4 15 0.45 18 0.47 1. Plot or graph these results using the Lineweaver-Burk method. 2. Determine the KM and Vmax values. Show all equations and calculations.
A researcher has measured the initial rate of an enzyme-catalyzed reaction as a function of substrate concentration in the presence and absence of 0.001μM inhibitor. She obtains the following data. What is the Vmax and Km for the "no inhibitor" and "+ inhibitor" experiments. Ans, What would be value of V0 for the "+inhibitor" at [S] = 0.4μM and the inhibitor is most likely a competitive, uncompetitive or mixed inhibitor.
Below is the set of kinetics data of a velocity of an enzymatic reaction without inhibitor (Vo) and with an inhibitor (Voi): Which one is correct about the inhibition? Vo Voi 1 0.286 0.133 0.5 0.22 0.08 0.33 0.18 0.057 0.25 0.15 0.044 0.2 0.13 0.036 O Inhibitor decreases Vmax of the enzyme O Inhibitor is most likely structurally similar to a substrate O Inhibition of the enzyme is irreversible O Inhibitor can only bind to ES complex You are studying the kinetics of an unknown enzyme. Concentration of the enzyme is 5 micromolar. You obtained the following kinetic data: IS[ (mM) Vo, mM/s 10.83 18.57 0.02 0.04 0.07 26.76 0.1 0.15 32.50 39.00 0.2 43.33 0.3 48.75 0.5 54.17 0.7 56.88 What is the Km of the enzyme? O 0.1 mM 10 mM 65 mM 60 mM Which statement about the enzyme from previous question is correct? (Kinetic data are provided again just in case) IS] (mM) 0.02 Vo, mM/s 10.83 0.04 18.57 0.07 26.76 0.1 32.50 0.15 39.00 0.2 43.33 48.75 54.17 0.3 0.5 0.7 56.88 O Enzyme functions near…
The above graphs (Lineweaver-Burk) were plotted using data from an experiment that investigated changes in initial velocity, V0, (in mmol/min) as a function of substrate concentration, [S], (in mmol/L) for an enzyme-catalysed reaction. The initial velocity was measured at a fixed concentration of enzyme at different concentrations of substrate in the absence of any inhibitor and was then repeated in the presence of a competitive inhibitor at two different concentrations. Use the graph to determine the maximal velocity of the reaction the Km value of the uninhibited reaction the Km value of the reaction with (i) the lower level of inhibitor and (ii) the higher level of the inhibitor. TEMPLATE FOR ANSWERS Vmax of uninhibited reaction Intercept on y-axis = = __________________ Vmax = __________________ Km value of the uninhibited reaction Intercept on x-axis = =…
The following data were collected for an enzyme that can be described by Michaelis Menton kinetics. Use graphical analysis to determine the Km and Vmax for this exzyme / substrate combination. [S] mM Product formed (umol/min) 0.21 1.5 2.0 0.24 3.0 0.28 4.0 0.33 8.0 0.40 16.0 0.45
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.

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