1. The optimal conditions for salivary lysozyme (hydrolyzing glycoproteins ofbacterialwall) are 37 C- temperature and pH is 5.2. Explain the decrease in this enzymeactivity if the temperature will rise up to 60 °C and pH will be changed to 8.0. Toanswer the question:a) draw the graph of the velocity dependency on temperature and pH;b) calculate the relative enzyme activity if 10 mg of lysozyme catalyzes theformation of 5 uM of the product per 2 minutes.2 Consider thematic reaction schee: Asnaragine + H20Aspartate+ NH3:

Enzymes are the biological catalysts that increase the speed of a reaction. The rate of an…

Answered: . The optimal conditions for salivary…

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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I need help with parts d-g a.) For Ado: catalytic efficiency = 4.18 x 106 M-1s-1 For ATP: catalytic efficiency = 12.1 x 107 M-1s-1 b.) Both specificity constants are below the diffusion limit so neither substrate is limiting the reaction rate due to diffusion c.) Line weaver Burk equation for AdoK enzyme with Ado substrate: y = 0.68x + (2.04 x 104), where y = 1/vo and x = 1/[Ado]
.When saturated with substrate, an enzyme has a maximum initial rate of 110 umoles of substrate converted to product per second. At a substrate concentration of 100 µM, the same enzyme converts substrate to product at a rate of 0.010 mmoles/sec. Assuming that Michaelis- Menten kinetics are followed, calculate the reaction rate when substrate concentration is 2 x 10 M.
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
Calculcate Kcat for PNP substrate for both enzyme concentrations. enzyme volume: 20 ul Bovine Intensince Alkaline phosphatase molecular weight: 140,000 Bovine intenstine Alkaline phosphatase activity: 300 units/ml and 14 units/mg extinction coefficient PNP: 18.5 abs (mM-1 cm-1) Vmax: 0.332 moles/sec a) enzyme 1 concentration: undiluted b) enzyme 2 concentration: 1:1 dilution
Km value should be more than 10% apart, use non-competitive inhibitor
Please handraw this graph with all the necessary detailed information: Imagine that I text enzyme rate for four different temperatures: 10 degrees celsius, 20 degrees celsisus, 30 degree celsius, and 40 degree celsius, in separate tubes. The enzyme appears to work faster as temperature increases, but completely ceases activity at 40 degrees celcius. Sketch a graph to show this outcome, but here you will graph product formation (nmoles/mL) vs. time (minutes). The graph should be 4 lines and HANDDRAWN. Include a legend if necessary. You do not need precise quantitivate values, but most show the correct trends on the graph.
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.
assume that for an enzyme immobilized on the surface of a nonporous support material, the external mass-transfer resisitance for substrate is not negligible as compared to the reaction rate.The enzyme is subject to substrate inhibition are multiple states possible?why or why not? could the effectiveness factor be greater than one?
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…
. Consider the enzymatic reaction scheme: Asparagine + H20 Aspartate + NH3: a) calculate the specific activity of the enzyme, if in 30 seconds as a result of a reaction involving 3 mg of the enzyme under optimal conditions (pH 8.0, 37 °C) 75 umol aspartate is obtained; b) describe the reasons for the decrease in enzyme activity after incubation for 6. 10 minutes at 70 °C (provide an appropriate graph).
5. For a Michaelis-Menten enzyme, k1 = 5.2 ⅹ 108 M-1 s-1, k-1 = 3.1 ⅹ 104 s-1, and k2 = 3.4 ⅹ 105 s-1. a) Write out the reaction, showing k1, k-1, and k2. Calculate Ks and Km. Does substrate binding approach equilibrium or the steady state? Justify your answer. b) What is kcat for this reaction? Justify your answer. c) Calculate Vmax for the enzyme. The total enzyme concentration is 25 pmol L-1, and each enzyme has two active sites. d) What substrate concentration would be required for the reaction in (c) to reach half of Vmax. Justify your answer mathematically. e) A second Michaelis-Menten enzyme has k1 = 4.2 ⅹ 107 M-1 s-1, k-1 = 6.1 ⅹ 104 s-1, and k2 = 5.3 ⅹ 102 s-1. Which enzyme is most efficient? 6. A pharmaceutical company is trying to develop a
The process of protein decomposition by pepsin enzymes in stomach is assumed and modeled as a batch reactor. If the protein concentration over time is measured as follows: Write the relationship between time (t), protein concentration (CA). Assuming that the enzyme reaction follows Michaelis-Menten kinetics, write the required constant (Vmax, Km), and the initial concentration of the protein is CA0.

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