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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The 2 eynzymes are affected by a substrate. Choose all correct answers.
What is the optimal substrate concentration for the enzymatic reaction presented in the Lineweaver-Burk plot below? a. -0.3211 units/mL b. –3.114 units/mL c. None of these values represent the optimal substrate concentration shown in the Lineweaver-Burk plot d. 3.114 units/mL e. 0.3211 units/mL
1. Make a Lineweaver-Burk plot and use the plot to complete the information in the table and the following questions. a. Is it possible for the enzyme to overcome the effect of the inhibitor in question from the chart. Explain. b. What prevents this enzyme from being an even more catalytically efficient enzyme? c. What do single molecule data indicate about the validity of ensemble data?d. What is the reason that humans are insensitive to sulfa drugs?
4. An enzyme-catalyzed reaction is studied in the absence and presence of an inhibitor and the following data was obtained. [S] in mmoles/L Velocity in mmoles/L/min-1 No inhibitor With inhibitor 1.25 1.72 0.98 1.67 2.04 1.17 2.50 2.63 1.47 5.00 3.33 1.96 10.00 4.17 2.38 Calculate the a. Km of the enzyme in the reaction without inhibitor b. Km' of the enzyme in the reaction with inhibitor C. Vmax of the uninhibited reaction d. Vmax' of the inhibited reaction 1/V 1/[S] What kind of inhibitor was added to the enzyme-catalyzed reaction in #4?
1. Start with the Michaelis-Menten equation and convert it to a double-reciprocal equation. Show how you would make a linear Lineweaver-Burk plot using this equation. 2. Based on th chart make a Lineweaver-Burk plot and later use the plot to complete the information in the table.
4. Below is a Michaelis-Menten plot for a wild-type (WT) and mutant (V105A) enzyme isolated from the bacterium Staphylococcus aureus. The enzyme is involved in carbohydrate metabolism and is a potential biocatalyst for the large-scale production of rare sugars. (8) mg V₂ μmol s1 1.50- 1.25- 1.00- 0.75- 0.50- 0.25- 0.00 0 100 200 300 [s], mM 400 500 WT (a) Estimate the KM and Vmax for the wild-type and mutant enzyme from the graph. V105A (b) Calculate the keat and keat/KM for the wild-type and mutant enzyme based on your estimated values in (a) if the total enzyme concentration is 0.5 µmol/mg. (c) Is the mutant enzyme a more or less efficient catalyst than the wild-type enzyme? Briefly explain.
2. Enzyme-catalyzed reactions. Answer the following with true or false. If false, explain why. (a) The initial rate of an enzyme-catalyzed reaction is independent of substrate concentration. (b) At saturating levels of substrate, the rate of an enzyme-catalyzed reaction is proportional to the enzyme concentration. (c) The Michaelis constant Km equals the substrate concentration at which velocity (v) = Vmax/2. (d) The Km for a regulatory enzyme varies with enzyme concentration. (e) If enough substrate is added, the normal Vmax of an enzyme-catalyzed reaction can be attained even in the presence of a noncompetitive inhibitor. (f) The Km of some enzymes may be altered by the presence of metabolites structurally unrelated to the substrate. (g) The rate of an enzyme-catalyzed reaction in the presence of a rate-limiting concentration of substrate decreases with time. (h) The sigmoidal shape of the v versus [S] curve for some regulatory enzymes indicates that affinity of the enzyme for the…
3. An enzyme with a Km of 0.06 mmol/L hydrolyzed a substrate of a concentration 0.03 mmol/L. The initial velocity of the reaction was 0.0015 mmol/(L.min). Calculate the substrate concentration which gives an initial velocity of 0.003 mmol/(L.min). 2. An enzyme hydrolyzed a substrate concentration of 0.03 mmol/L, the initial velocity was 1.5x10-3 mmol/(L.min) and the maximum velocity was 4.5x10 mmol/(L.min). Calculate the km value. pr:4
3. Estimate the Vmax and Km of the enzyme-catalyzed reaction for which the following data were obtained: [S] (M) Vo (uM / min) 2.5 x 106 4.0 x 106 28 40 1 x 105 2 x 105 4 x 105 1 x 104 2х 103 1x 10-2 70 95 112 128 139 140 A. Vmax = 140 and Km =1 x 10s B. Vmax = 70 and Km = 1 x 105 C. Vmax = 140 and Km =1 x 102 D. Vmax = 70 and Km = 1 x 102 %3D %3!
Given the parameters below:1. u(max) = 1.0/ h Ks = 10 uM2. u(max) = 0.7/h Ks = 2 uM) a. sketch the comparative Substrate Concentration vs.u(max) graphs for 1. b. sketch the comparative Substrate Concentration vs.u(max) graphs for 2. (answer a and b)
The enzymatic activity of an enzyme with Kg = 2 mM that converts substrate S into product P is measured at an initial substrate concentration S, of 10 µM. After 5 min, the substrate concentration is halved. What is the rate constant k, the maximal velocity vmax and the concentration of product after 12 min?
6. An enzyme catalyzed reaction has a KM of 1 mM and a Vmax of 5 nM/s. What is the reaction velocity when the substrate concentration is (a) 0.25 mM (b) 1.5 mM, and (c) 10 mM?

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