Homework Answers
Answer.
An uncompetitive inhibitor will lower the KM and create a better enzyme-substrate binding because it only binds to ES complex, not to free enzyme E.
For noncompetitive inhibition, Vmax decreases because there are ESI complexes being formed and they inhibit formation of product.
1. Inhibitor (Trial 2)
2. Non-competitive Inhibitor
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You are running an enzyme assay to determine its activity in the presence and absence of...
The kinetic data given below are for an enzyme in the absence and presence of a...
The kinetic data given below are for an enzyme in the absence and presence of a reversible inhibitor. From the data, generate both a Michaelis-Menten and Linweaver-Burk Plot for both that uninbibited and inhibited reactions. Graph both the uninhibited and inhibited data on the same plot. From these data calculate the Vmax and Km for the enzyme in absence and presence of the inhibitor. Is the inhibitor working cometitively or noncompetitively? Explain. [S], mM Vo, mM/min Vo, mM, min with...
Given the kinetics data for each enzyme in the presence and absence of its inhibitor, determine...
Given the kinetics data for each enzyme in the presence and absence of its inhibitor, determine the type of inhibition. EnzymeK_(M)(mM)V_(max)(mmol//s)carbonic anhydrase8,000600,000+ inhibitor A12,000600,000chymotrypsin5,000100+ inhibitor B5,00075penicillinase502,000+ inhibitor C301,500lysozyme60.5+ inhibitor D150.5carboxypeptisase A31,000+ inhibitor E3800
The following data was obtained for an enzyme in the absence of an inhibitor, and in...
The following data was obtained for an enzyme in the absence of an inhibitor, and in the presence of two different inhibitors. The concentration of each inhibitor was 10 mM. The total concentration of enzyme was the same for each experiment. [S] {mM} without inhibitor v, {umol/(ml*s)} with inhibitor A v, {umol/(ml*s)} With inhibitor B v, {umol/(ml*s)} 0.0 0.0 0.0 0.0 1.0 3.6 3.2 2.6 2.0 6.3 5.3 4.5 4.0 10.0 7.8 7.1 8.0 14.3 10.1 10.2 12.0 16.7 11.3...
1. The kinetics of an enzyme was examined at various substrate concentrations in both the presence...
1. The kinetics of an enzyme was examined at various substrate concentrations in both the presence and absence of 3 mM inhibitor Z. The initial velocity data obtained are shown below: [S] (mmoles liter) v (mmoles"litermin) no inhibitor inhibitor Z 1.25 1.67 2.50 5.00 10.0 1.72 2.04 2.63 3.33 4.17 0.98 1.17 1.47 1.96 2.38 (4 pts) Estimat e Vmax and Kw in the presence and absence of inhibitor using the Michaelis Menton curve-fitting program on Kaleidagraph (see lab manual)....
Q1: A marine microorganism contains an enzyme that hydrolyzes glucose-6- sulfate (S). The assay is based...
Q1: A marine microorganism contains an enzyme that hydrolyzes glucose-6- sulfate (S). The assay is based on the rate of glucose formation. The enzyme in a cell-free extract has kinetic constants of km = 6.7 x 10-4, Vmax = 300 nm/L/min in presence of 10-5M competitive inhibitor (Galactose-6-sulfate) and 2 x 10-5M substrate (Glucose-6-sulfate), velocity was 1.5 nmoles /L/min. a) Calculate Ki for Galactose-6-sulfate b) Calculate velocity in absence of the inhibitor
CHEM3250 Assignment-Enzyme Inhibition Consider the data below for an enzyme catalyzed reaction. T...
CHEM3250 Assignment-Enzyme Inhibition Consider the data below for an enzyme catalyzed reaction. The rate of the reaction has been determined with and without an inhibitor. A total concentration of enzyme of 20 uM was used in the experiment. SHOW WORK AND UNITS!!! Without Inhibitor With Inhibitor [substrate] (mM)Rate of formation of te of formation of product product (mM/min) mM/min) 6.67 5.25 0.49 7.04 38.91 1.0 2.2 6.9 41.8 44.0 1.5 3.5 1 a) On the same graph, plot the data...
i need help with part two PART TWO 1) The steady-state kinetics of an enzyme is studied in the absence and presence...
i
need help with part two
PART TWO 1) The steady-state kinetics of an enzyme is studied in the absence and presence of inhibitor A. The initial rate is given as a function of substrate concentration in the following table. [S] (MM) * Velocity in substrate only y (mM/min) .25 1.72 58 ,598 r.60 2.04 .44 50 A 2.63 238 5.00 .2 3.33 10.00 4.17 4 Velocity in substrate + S inhibitor A (MM/min) 0.98 1.02 | 1.17 . 5...
5) (14 marks) The following kinetic data were obtained for an enzyme in the absence of...
5) (14 marks) The following kinetic data were obtained for an enzyme in the absence of inhibitor (1), and in the presence of an inhibitor at 5 mM concentration (2). Assume[ET] is the same in each experiment. [S] (MM) (1) v(umol/mL sec) 12 (2) v(umol/mL sec) 4.3 1 8 2 4 20 29 14 21 8 35 12 40 26 a. Using a graphing program (excel or sigmaplot) construct a lineweaver burke plot representing the uninhibited reaction and the inhibited...
2. The table shows the kinetic data for a reaction catalyzed by an enzyme under the...
2. The table shows the kinetic data for a reaction catalyzed by an enzyme under the following conditions: in the absence of an inhibitor, and in the presence of two different inhibitors, (1) and (2) each at a concentration of 10 mM. Assume the total enzyme concentration, [Elo, is the same for all reactions and the enzyme obeys the Michaelis-Menten mechanism In the presence of presence of 10 mM inhibitor 1 inhibitor2 In the 10 mM No inhibitor mM 2.5...
Q2) Using the data in the below table, which were obtained for enzyme activity without presence...
Q2) Using the data in the below table, which were obtained for enzyme activity without presence of inhibitors. [15 points) IS (MM) 1.3 2.6 6.5 13.0 26.0 VomM/s) 2.50 4.00 6.30 7.60 9.00 A) Draw Lineweaver-Burk plot and determine the K. and Vmax for this uninhibited enzyme. (You may use hand, excel or other program to draw the graph and find the equation. Then copy and paste the graph here, you need to show axis labels) [6 points) B) From...
1. The kinetics of an enzyme was examined at various substrate concentrations in both the presence and absence of 3 mM inhibitor Z. The initial velocity data obtained are shown below: [S] (mmoles liter) v (mmoles"litermin) no inhibitor inhibitor Z 1.25 1.67 2.50 5.00 10.0 1.72 2.04 2.63 3.33 4.17 0.98 1.17 1.47 1.96 2.38 (4 pts) Estimat e Vmax and Kw in the presence and absence of inhibitor using the Michaelis Menton curve-fitting program on Kaleidagraph (see lab manual)....
Q1: A marine microorganism contains an enzyme that hydrolyzes glucose-6- sulfate (S). The assay is based on the rate of glucose formation. The enzyme in a cell-free extract has kinetic constants of km = 6.7 x 10-4, Vmax = 300 nm/L/min in presence of 10-5M competitive inhibitor (Galactose-6-sulfate) and 2 x 10-5M substrate (Glucose-6-sulfate), velocity was 1.5 nmoles /L/min. a) Calculate Ki for Galactose-6-sulfate b) Calculate velocity in absence of the inhibitor
CHEM3250 Assignment-Enzyme Inhibition Consider the data below for an enzyme catalyzed reaction. The rate of the reaction has been determined with and without an inhibitor. A total concentration of enzyme of 20 uM was used in the experiment. SHOW WORK AND UNITS!!! Without Inhibitor With Inhibitor [substrate] (mM)Rate of formation of te of formation of product product (mM/min) mM/min) 6.67 5.25 0.49 7.04 38.91 1.0 2.2 6.9 41.8 44.0 1.5 3.5 1 a) On the same graph, plot the data...
i
need help with part two
PART TWO 1) The steady-state kinetics of an enzyme is studied in the absence and presence of inhibitor A. The initial rate is given as a function of substrate concentration in the following table. [S] (MM) * Velocity in substrate only y (mM/min) .25 1.72 58 ,598 r.60 2.04 .44 50 A 2.63 238 5.00 .2 3.33 10.00 4.17 4 Velocity in substrate + S inhibitor A (MM/min) 0.98 1.02 | 1.17 . 5...
5) (14 marks) The following kinetic data were obtained for an enzyme in the absence of inhibitor (1), and in the presence of an inhibitor at 5 mM concentration (2). Assume[ET] is the same in each experiment. [S] (MM) (1) v(umol/mL sec) 12 (2) v(umol/mL sec) 4.3 1 8 2 4 20 29 14 21 8 35 12 40 26 a. Using a graphing program (excel or sigmaplot) construct a lineweaver burke plot representing the uninhibited reaction and the inhibited...
2. The table shows the kinetic data for a reaction catalyzed by an enzyme under the following conditions: in the absence of an inhibitor, and in the presence of two different inhibitors, (1) and (2) each at a concentration of 10 mM. Assume the total enzyme concentration, [Elo, is the same for all reactions and the enzyme obeys the Michaelis-Menten mechanism In the presence of presence of 10 mM inhibitor 1 inhibitor2 In the 10 mM No inhibitor mM 2.5...
Q2) Using the data in the below table, which were obtained for enzyme activity without presence of inhibitors. [15 points) IS (MM) 1.3 2.6 6.5 13.0 26.0 VomM/s) 2.50 4.00 6.30 7.60 9.00 A) Draw Lineweaver-Burk plot and determine the K. and Vmax for this uninhibited enzyme. (You may use hand, excel or other program to draw the graph and find the equation. Then copy and paste the graph here, you need to show axis labels) [6 points) B) From...
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