1. Explain what happens to the velocity in the followingscenarios.a. More substrate is added when the substrateconcentration is low.b. More substrate is added when the enzyme is saturatedwith substrate.2. If an enzyme has a K = 9.00mM and Vmax= = 1.85mM s',what would the velocity be if you had a substrateconcentration of 3.0 mM?b. What would happen to the velocity if K, decreased to3.0mM?3. A researcher recorded the following velocity (R) data withan enzyme whose substrate is ATP. Find V and K, andshow work.CMI4. How would each of the following effect the rate of anenzymatic reaction?a. Increase of temperature (from 0C-100C)b. Increase in pHc. Increase in substrate concentrationd. Increase in enzyme concentration

General enzyme kinetics are assumed to follow the Michaelis-Menten kinetics and its steady state…

Answered: 1. Explain what happens to the velocity…

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. Enzyme X has a molecular weight of 35,000 Da. When this enzyme is assayed for enzyme activity, the corresponding line of the double reciprocal plot has the equation y = 75,253X + 102,392. The substrate concentration was in mM and the velocity was measured in mM min". From these data calculate the following: a. KM and Vmax b. kcat if the enzyme concentration was 2 mg/mL. 2. When you run enzyme X from question one on an SDS-PAGE you find that, after Coomassie staining, there is only one band on the gel that runs just below the 20,000 Dalton molecular weight marker. What does this result tell you about the nature of the quaternary structure of your enzyme?
1. Explain why the maximum initial reaction rate cannot be reached at low substrate concentrationsPredict or describe the absorbance or enzyme activity at: pH = 2 pH = 14 Explain your predictions 2. Explain why the maximum initial reaction rate cannot be reached at low substrate concentrations.
An enzymatic reaction follows M-M kinetics with Vmax= 2.5 mol m-3s-1and Km = 5 mM.Calculate the time required for 50% conversion of the substrate in a batch reactor if theinitial substrate concentration is0.2 M.Show your calculation steps.
Acetazolamide is a drug which inhibits carbonic anhydrase. Carbonic anhydrase participates in regulation of the pH and bicarbonate content of a number of body fluids. Figure 2 shows the experimental curve of initial reaction velocity (as percentage of Vma) versus [S] (concentration) for the carbonic anhydrase reaction. The graph also shows the curve in the presence of acetazolamide. 100 No inhibitor 50 Acetazolamide 0.2 0.4 0.6 0.8 [S] (mM) Figure 2 (i) Compare the maximal velocities and Michaelis Menten constants of the enzyme in the absence and the presence of the inhibitor acetazolamide. Determine the nature of inhibition by acetazolamide. Explain your answer. (ii) Name TWO (2) other types of inhibitions besides the inhibition shown by acetazolamide. Sketch a graph of V versus [S] showing curves in the absence of an inhibitor and in the presence of the types of inhibitors not shown by acetazolamide. ("AJO %) A
Acetazolamide is a drug which inhibits carbonic anhydrase. Carbonic anhydrase participates in regulation of the pH and bicarbonate content of a number of body fluids. Figure 2 shows the experimental curve of initial reaction velocity (as percentage of Vmax) versus [S] (concentration) for the carbonic anhydrase reaction. The graph also shows the curve in the presence of acetazolamide. 100 No inhibitor 50 Acetazolamide 0.2 0.4 0.6 0.8 (S] (mM) Figure 2 (i) Compare the maximal velocities and Michaelis Menten constants of the enzyme in the absence and the presence of the inhibitor acetazolamide. Determine the nature of inhibition by acetazolamide. Explain your answer. (*"A JO %) A
Substrate Initial velocity Vo concentration [S] µM s-1 10 0.13 25 0.27 50 0.45 100 0.65 150 0.77 200 0.85 300 0.94 500 1.03 1. Calculate Vmax and Km??? The enzyme is dissolved at a concentration of 1 mg/ml and has a molecular weight of 50 kDa. a) What is the turnover number of the enzyme? b) What is the specificity constant of the enzyme? c) Is the enzyme operating near the maximum rate possible, i.e. is the enzyme diffusion controlled? please show all working and formulas as I am trying to learn. thank you
Consider the Michaelis-Menten equation, below: Vmaz (S V. k + [S] %3D What is the relationship between changes in substrate concentration and velocity when the concentration of substrate, [S), is well below k7 The S terms cancel out in this equation, so there is no effect of changing substrate concentration. The S] term in the numerator is negligible, so there is no impact of changing substrate concentration. Because the enzyme has reached Vr there is no effect of changing substrate concentrations on enzyme velocity. OThe [S term in the denominator is negligible compared to k There is a linear relationship between substrate concentration and velocity.
SUBSTRATE CONCENTRATION [S] µM INITIAL VELOCITY V0 s-1 10 0.13 25 0.27 50 0.45 100 0.65 150 0.77 200 0.85 300 0.94 500 1.03 (i) a) Construct an empty table with the following column headings: Substrate concentration [S] and initial velocity (Vi) where [S] has the unit µM, and Vi has the unit mM/s. (ii) The table provided is the enzyme kinetic data for your mutated enzyme, whereby Vi was expressed using the unit ∆A(405 nm)/s. Using the standard curve, express Vi with the unit mM/s rather than ∆A(405 nm)/s. Place your answer in the table above alongside the appropriate [S]. Hint: To answer this question you need to use this standard curve equation=0.0419x (The slope of the line is= 0.0419) (iii) The unmutated form of your protein has a Km of 25 µM and a Vmax of 43 mM/s. The enzyme kinetic data for your enzyme with the amino acid substitution should now be displayed in the table above. Based on these data, what is Vmax? Km? and…
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.
The enzyme – catalyzed conversion of a substrate at 25°C has Michaelis constant of 0.04 mol L-!. The rate of the reaction is 2.45x104mol Ls1when the substrate concentration is 0.890 mol L. What is the Enzyme concentration and what is the maximum velocity? إجابتك
Which of the following is incorrect about the Michaelis-Menten plot? a. The y-axis is velocity and the x-axis is [substrate] b. It is based on E + S to reversibly form ES and then this to form E + P O c. The data is plotted using the Michaelis-Menten equation Od. It has a sigmoidal shape

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