question is attached 8. Show how the addition of a competitive inhibitor would affect the reaction velocity anddouble-reciprocal plots shown below.1Reaction velocity (V)VmaxVmax/2- KMVmaxSubstrate concentration [S] -1/Vo Slope=KM/VmaxIntercept = -1/KM0Intercept = 1/Vmax1/[S]

Enzymes are high molecular weight proteins that catalyse biochemical reactions. They contain an…

Answered: Show how the addition of a competitive…

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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1.1)the following data duscribe an enzyme-catalyzed reaction(hydrolysis of cabobenzoxyglycyl-L-tryptophan) Plot these results using a lineweaver-Burk method, and determine values for Km and Vmax. substrate concenrate(mM) Velocity(mM.sec-1) 2,5 0.024 5 0.036 10 0.053 15 0.060 20 0.061 25 0.062 1.2) If the Km of an enzyme for it's substrate remains constant as the concentration of the inhibitor icreaces, what can be said about the mode of inhibition and why? 1.3) calculate the turnover number for an enzyme, assuming Vmax is 0.5M.sec-1 and the concentration of the enzyme used is 0.002M . why is it usefull to know this? 1.4) discuss the mechanism of the bohr effect that occurs during the interactions of Hb with oxygen under physiological conditions in the lungs and tissues. make use of relavant graphs and diagrams to explain your answer.
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
2) Below are kinetic data at three different inhibitor concentrations. Graph the data in an appropriate form to determine whether the inhibitor is competitive or uncompetitive. a (μm) 0.4 0.67 1.00 2.00 v (μM/min) (no inhibitor) 0.22 0.29 0.32 0.40 v (μM/min) (10 nM inhibitor) 0.21 0.26 0.30 0.36 v (μM/min) (20 nM inhibitor) 0.20 0.24 0.28 0.32
The typical Michaelis-Menten equation mathematically describes the overall rate of the reaction as V (this is because biologists don't like math). What does V actually mean? (write the definition of V in differential equation form). V= d( )/dt Reaction rate Substrate concentration V max ·½V TURK
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 each reaction at a concentration of 2 mM. The enzyme concentration was similar in all and was approximately 0.001 им. 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. (S] (mM) (3) V. [(umol/(ml.s)] (1) V. (2) V. [(µmol/(ml.s)] [(µmol/(ml.s)] 7.6 4.4 6.6 14.6 8.6 11.4 26.6 16.4 17.8 16 45.8 29.8 24.6 24 60 40.8 28.2
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 each reaction at a concentration of 2 mM. The enzyme concentration was similar in all and was approximately 0.001 им. a. Calculate both Vmax and KM for the control using Lineweaver-Burk curve. b. Provide the type of inhibition for both?
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 = reaction at a concentration of 2 mM. The enzyme concentration was similar in all and was approximately 0.001 control) of enzyme inhibitor. Both inhibitors were added in each ИМ. 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). Draw a velocity versus [S] showing Michaelis-Menten curve for the Control. Clearly show Vmax and KM for the enzyme. a. c. e. [S] (mM) (1) V. [(umol/(ml.s)] (2) V. [(umol/(ml.s)] (3) V. [(umol/(ml.s)] 7.6 4.4 6.6 4 14.6 8.6 11.4 26.6 16.4 17.8 16 45.8 29.8 24.6 24 60 40.8 28.2
An enzyme catalyzes a reaction with a Km of 9.50 mM and a Vmax of 2.10 mM · s-1. Calculate the reaction velocity, vo, for each substrate concentration. [S] = 3.25 mM vo : mM · s-1 [S] = 9.50 mM mM · s-1 Vo :
1). The initial velocity of an enzyme-catalyzed reaction has been determined at several substrate concentrations with and without an inhibitor I. The total enzyme concentration [E]ot present in each experiment is 1.20 x 10 M. [1] = 5.00 x10 M. (Note: v initial rate or velocity.) [S], M 1.25E-3 2.50E-3 5.00E-3 10.0E-3 v, M/min, no inhibitor 0.480E-3 0.660E-3 0.810E-3 0.920E-3 v, M/min, 5.00x10 M 9.43E-5 1.41E-4 1.70E-4 2.10E-4 b). What kind of inhibition occurred. c). Calculate the value of Ki = a). Use the Lineweaver-Burk plot to determine the values of Vmax and KM at [1] = 0.00 mM, and the values of Vmax and KM at 0.500 mM of I. it in 'How many molecules of
Consider the given data for an enzyme-catalyzed reaction. Determine the Vm, Km and the type of inhibition based on the given data below Substrate concentration, uM 30 50 100 300 900 slope y-intercept Complete the table below (include correct units). Experiment A Vm Km Experiment A (Initial velocity without inhibitor, uM-min) Type of Inhibition: 10.4 14.5 22.5 33.8 40.8 Experiment B (Initial velocity with inhibitor, uM-min) 5.1 7.3 13.3 25.7 37.2 Experiment B
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.
The enzyme triosephosphate isomerase (TIM) catalyzes the following reaction in glycolysis, where it converts dihydroxyacetone phosphate (DHAP) to glyceraldehyde-3-phosphate (GAP). CH₂OH C=O CH₂OPO²- DHAP triose phosphate isomerase [DHAP] (MM 1.00 2.00 3.00 6.00 O V. (mM/s) 3.700 6.727 9.250 14.800 = H HCOH CH₂OPO²- Kinetics experiments were performed on TIM. Enzyme activity (initial velocity, V.) was measured at varying concentrations of DHAP. The enzyme kinetics were also measured in the presence of two inhibitors, A and B. The enzyme concentration used in all experiments was 25.00 μM. The data are shown below. GAP V. (mM/s) + A 1.452 2.794 4.038 7.281 V₁ (mM/s) + B 0.755 1.379 1.905 3.077

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Show how the addition of a competitive inhibitor would affect the reaction velocity and double-reciprocal plots shown below. 1 Reaction velocity (Vo) Vmax Vmax/2 max KM Substrate concentration [S]->> 1/Vo Slope=KM/Vmax Intercept = -1/KM 0 Intercept = 1/Vmax 1/[S]