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- Velocity (mmol/minute) [S], (mM) No inhibitor Inhibitor 3 10.4 4.1 5 14.5 6.4 10 22.5 11.3 30 33.8 22.6 90 40.5 33.8 The kinetics of an enzyme are measured as a function of substrate in the presence and the in absence of 2mM inhibitor (I). What are the values of Vmax and KM in the absence of inhibitor? In its presence? In its presence? What is the type of inhibition?1) what is the Vmax of the enzyme WITHOUT inhibitor 2) What is the Km of the enzyme WITHOUT the inhibitor 3) The specificity constant for enzyme X is (8*10^7) /(M*seconds); what is the kcat of the enzyme WITHOUT the inhibitor? 4) what was the concentration of the enzyme used for measuring the kinetics of enzyme X without inhibitor? 5) the dashed line represents enzyme with inhibitor. The concentration of the inhibitor is 5 micromolar. Calculate the equilibrium constant for the inhibitor Please show work and unitsBriefly describe the effects of a linear noncompetitive inhibitors on the kinetic parameters Km and Vmax. breifly discuss the reasons behind the effect of this type of inhibition on the kinetic parameters
- 1. Provided in the Table below kinetic data for an enzymatic reaction that was carried out in the presence (last two columns) and absence (second column = control) of enzyme inhibitor. Both inhibitors were added in eachreaction at a concentration of 2 mM. The enzyme concentration was similar in all and was approximately 0.001 µM. a. Calculate both Vmax and KM for the control using Lineweaver-Burk curve. b. Provide the type of inhibition for both? c. 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 KMfor the enzyme.1. Provided in the Table below kinetic data for an enzymatic reaction that was carried out in the presence (last two columns) and absence (second column = control) of enzyme inhibitor. Both inhibitors were added in eachreaction at a concentration of 2 mM. The enzyme concentration was similar in all and was approximately 0.001 µM. a. Calculate both Vmax and KM for the control using Lineweaver-Burk curve. b. Provide the type of inhibition for both? c. 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 KM for the enzyme.If an enzyme catalyzed reaction has a KM of 5mM and a Vmax of 60 nm/sec, the substrate concentration at 30 nM/sec is? Thank you.
- WriteC if only statement A is correct, H if only statement B is correct, E if both statements are correct, M if both statements are incorrect. A. An inhibitor that binds somewhere in the enzyme other than the active site is an uncompetitive inhibitor. B. With this mode of inhibitor binding, the substrate's affinity to the enzyme is affected and it decreases the maximum reaction velocity.A biochemist wants to determine the effect of inhibitor A to enzyme B which catlyzes the conversion of C to D. The effect of A to the rate of formation of D is shown below: 1. The Km (report to the nearest whole number) for the enzyme-catalyzed reaction in the absence of inhibitor A is _____ mM. 2. The Km for the enzyme catalyzed reaction in the presence of inhibitor A is ____mM. 3. The Vmax for the enzyme catalyzed reaction in the absence of inhibitor A is ____ mM/min 4. The Vmax for the enzyme catalyzed reaction in the presence of inhibitor A is ____mM/min 5. Inhibitor A is a/an ________ inhibitor of enzyme BPlease find the Vmax and Km values of the enzyme without/minus an inhibitor, and the enzyme with/plus an inhibitor. (The Vmax may be the same value).
- 2. an enzyme-catalyzed reaction is studied in the presence and absence of an inhibitor. The following data was obtained. (S)[M] V (umol/min) V (+inhibitor)(umol/min) 6 x 10-6 20.8 12 1 x 10-5 29 15 2 x 10-5 45 20 6 x 10-5 67.6 24 1.8 x 10-4 87 28 plot 1/[S] as abscissa and 1/V as ordinate for both catalyzed reaction and reaction with inhibitor. Use the same graph for both plots. calculate the Km of enzyme in the reaction without inhibitor Km1 of the enzyme in the reaction with inhibitor Vmax of the uninhibited reaction Vmax of the inhibited reaction what kind of inhibitor was added to the enzyme-catalyzed reaction? explain your answer in terms of changes in Km and Vmax.The Lineweaver-Burk plot and other linear transformation of the Michaelis-Menten curve of kinetics are valuable for _____. A. determination of Vmax. B. determination of Km. C. determination of kcat. D. determination of types of enzyme inhibition. E. All of the above An inhibitor binds to a site other than the active site of the enzyme. Which statement below correlates with this observation? A. The inhibition must be irreversible. B. It must be a competitive inhibitor. C. It could be noncompetitive or uncompetitive inhibition. D. It could be irreversible, competitive, noncompetitive or uncompetitive. The data do not relate to the type of inhibition.1. Inhibitor Impact Factor Practice calculations with the inhibitor impact factor (IIF).(a) For Ki = 2 μM and [I] = 0.1 μM, what is IIF?(b) For Ki = 2 μM and [I] = 10 μM, what is IIF?(c) Calculate impact on KM-app and Vmax-app for a competitive inhibitor for the conditiondescribed in (a) and as described in part (b).(d) Calculate impact on KM-app and Vmax-app for a non-competitive inhibitor for the conditiondescribed in (a) and as described in part (b).(e) Briefly explain in terms of molecules why the condition described in (a) has a negligibleimpact on enzyme performance AND why the condition described in (b) has a much largerimpact on enzyme performance. Pictures and words.