2. The table shows the kinetic data for a reaction catalyzed by an enzyme under the...
Pysical Chemistry! Please show all work thank you. 8. A chemist obtains the following Lineweaver-Burk plots for an enzyme catalyzed reaction in the absence and presence of two different inhibitors, A and B. The linear fit for no inhibition is 302.61.96 x 105 .0 x 10 2.5 x 10 2.0 x 10 1.5x 10 1.0 x10 The linear fit for inhibitor A is: 757.82.03 x 105 No inhibitor And the linear fit for inhibitor B is 50 к 10°- 1015.35.95...
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...
8. A chemist obtains the following Lineweaver-Burk plots for an enzyme catalyzed reaction in the absence and presence of two different inhibitors, A and B. The linear fit for no inhibition is: 1 ?0 = 302.6 1 [?] + 1.96 × 105 The linear fit for inhibitor A is: 1 ?0 = 757.8 1 [?] + 2.03 × 105 And the linear fit for inhibitor B is: 1 ?0 = 1015.3 1 [?] + 5.95 × 105 a) Determine the...
20.8 2) Consider the following data for an enzyme-catalyzed hydrolysis reaction in the presence and absence of inhibitor I using a Michaelis-Menten plot, determine Kn for both inhibited and uninhibited reactions. What kind of inhibition is this? [Substrate)(M) vo (umol/min) Vos (moles/min) 6x106 4.2 1x105 29 5.8 2x105 6x109 13.6 1.8x10* 16.2
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...
The kinetics of enzyme catalyzed reactions can be described the Michaelis-Menten equation and the Eadie-Hofstee equation as shown below: V0 = (-Km) V0 / [S] + Vmax a). Please derive the Eadie-Hofstee equation starting from the Michaelis-Menten equation. b). The Vmax and Km of the enzyme catalyzed reaction can be derived from a plot of V0 versus V0/[S]. Please draw one of these plots and explain how do you use it to derive Vmax and Km. c). Please draw a...
Determine the type of inhibition that has occurred in a first order Michaelis-Menten enzyme catalyzed reaction that has yielded the following data. Vi is the velocity in the presence of inhibitor, V is the velocity when run without inhibitor and [S] refers to the substrate concentration. [S] V Vi 5.00 0.29 0.16 1.25 0.27 0.15 0.45 0.23 0.13 0.22 0.19 0.10 0.13 0.14 O.08 Uncompetitive No inhibition at all O None the above ONon-competitive O Competitive Determine the type of...
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...
An enzyme catalyzed reaction was performed in the presence and in the absence of an inhibitor. The Lineweaver Burk plot showed competitive kinetics with x-intercepts of -10mm -1 and -3.5mm -1 in the presence and absence of the inhibitor respectively. If the inhibitor concentration used was 2micro molar (UM), calculate KI for the inhibitor enzyme binding? a. none of the above b. 0.135nM c. 0.054nM d. 0.225nM e. 1077 nM
An enzyme-catalyzed reaction to the presence of 5 nM of reversible inhibitor yields a Vmax value that is 80% of the value in absence of the inhibitor. The KMvalue is unchanged. a) what type of inhibition is occurring? b) what proportion of the enzyme molecule will have bound inhibitor? c) Draw the Lineweaver-Burk (known as double-reciprocal plot) for uninhibited and inhibited reaction. SHOW ALL YOUR WORK PLEASE