Kindly refer to the photo attached. thank you Question 1 of 13Fill in the blanks:WriteCif only statement A is correct,Hif only statement B is correct,E if both statements are correct,Mif both statements are incorrect.CA. When an inhibitor binds to the enzyme-substrate complex, theinhibition mode is uncompetitive.B. As a consequence, the enzyme's efficiency is decreased along with the maximumvelocity.Continue > Question 2 of 13Fill in the blanks:WriteCif only statement A is correct,Hif only statement B is correct,E if both statements are correct,M if both statements are incorrect.MA. The dissociation of the ES complex to the product is moreenergetically favored than its dissociation into the separate enzyme and substrate.B. The rate determining step in enzymatic catalysis is the binding of the substrate to theactive site of the enzyme.< PreviousContinue >

An enzyme inhibitors are the molecules which binds to the enzyme and decrease it's activity. NB: As…

Answered: Question 1 of 13 Fill in the blanks:…

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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-Inhibitor +Inhibitor [S] (mM). V&νβσπ:(μmol/sec) V0&νβσπ&ν βσπ;(μmol/sec) 0.0001 33 17 0.0005 71 50 0.001 83 67 0.005 96 91 0.01 98 95 What is the Vmax of this enzyme WITHOUT iinhibitor?
Question 8 of 13 Fill in the blanks: Write Cif only statement A is correct, Hif only statement B is correct, E if both statements are correct, Mif both statements are incorrect. M A. A competitive inhibitor would bind at the enzyme's active site. B. As a result, the affinity of the substrate to the active site decreases.
Which statements are false? Initial velocities of enzyme reactions are best obtained in the absence of product because it simplifies analysis. Initial velocities refer to the velocity of the reaction right after it is initiated. The velocity of the reaction as a function of measuring time are curved just like an isothermal binding curve because of substrate binding to the enzyme. Initial velocities correspond to the pre-steady state condition for free enzyme. Initial velocities can sometimes be measured by spectroscopy such as UV/Vis spectroscopy when monitoring the production of NADH from NAD+. The velocity of the reaction will eventually go to zero. The reaction will reach equilibrium because of the presence of the enzyme. It is always better to use substrate rather than product to measure enzyme kinetics.
Question 13 of 13 Fill in the blanks: Write C if only statement A is correct, Hif 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 purely competitive inhibitor of an enzyme has which of the following kinetic effects? decrease in Km increase in Vmax decrease in Vmax increase in Km Question 60 The Michaelis-Menten constant (KM) has the following characteristics, EXCEPT: The dimension for KM is concentration, such as molarity It is equal to ½ of Vmax It is the substrate concentration necessary to reach ½ of Vmax
QUESTION 5 Consider the graph below. Reaction rate (v) Vmax 0 Effector 3 mM Effector 1 mM. Control 0 mM Ko.5 (3) Ko.5 (1) Ko.5 (0) [S] Which of the following conclusion(s) can be drawn from the data illustrated in the figure?
Maximum velocity of an enzyme-catalyzed reaction dolgomsH 7 T (8 a. Is determined from the slope of the line of product formation zouza11 901 ml,0,.201 over time for a particular substrate concentration. vx011(e b. Is determined from reaction rate late in the reaction d c. Is the rate where addition of more substrate does not cause a rate increase. SO 121 91 to ydinitis of zomit 001 vainitts d. Changes with increases in substrate concentration (II Which of the following is not an assumption in Michaelis Mentens kinetics?91 21 noi to 926 v basylsts noitsbyri riguard (SE a. [ES]~ constant b. [E] >> [S] 00 to fu291 6 26 9022it ni[*] 92691 T (EI c. [E] << [S]gnul art ni a.. Hq o bot Hq edt 1swol in d. [S] + [ES] [Sbaid atidinni slusslom 398-E 900 T antern anibnid yd 29tie gnibnid
Question 2. Answer the following questions: A. The following experimental data was collected during a study of the catalytic activity of anintestinal peptidase with the substrate glycylglycine. Plot the data as a graph, and use it toestimate the Km and the Vmax for this enzyme. B. Now transform this data to plot it as a straight line (Lineweaver-Burk plot). Determine Km andthe Vmax for this enzyme using this new plot. Do your results agree with the estimates made fromthe first graph of the raw data (from 2A)? C. Now assume that the activity of this intestinal peptidase is regulated by covalent modificationof its catalytically active amino acid. Upon phosphorylation, the Km of the catalyzed reaction has been observed to increase by a factor of 3 without any effect on its Vmax. Is the enzyme getting activated or inhibited upon phosphorylation? Justify your answer. D. How will the Lineweaver-Burk plot of the phosphorylated enzyme differ from the plot of the unmodified enzyme (from 2B)?…
PART IV. HOW FAST DOES IT GO?Another member of your research group studied the kinetics of theGAPDH from the organism. They also determined if the GAPDH fromthe organism is also inhibited by the known inhibitor of GAPDH fromhumans. A. From the following data, determine the KM (Michaelis-Menten Constant) and the Vmax(maximum velocity) of the enzyme without and with the inhibitor. B. If GAPDH is inhibited, what specific type of inhibition is observed?
Which of the following statements are true about the relationships of [S], KM, and Vmax? (Choose all that are true) As the [S] is increased, vo approaches the limiting value, Vmax KM = Vmax/2 The rate of product formed, vo, is at Vmax when [S] <<< KM KM and Vmax assist in finding the rate of the enzyme catalyzed reaction only if the reaction is considered irreversible.
When k2 >> k-1, KM approximates the affinity of the enzyme•substrate complex.The (circle one) higher / lower the KM, the more tightly the enzyme binds to its substrate
Practice Mira Gendy 1 of 1 Directions: This short free-response question requires about 6 minutes to answer. The question is worth 3 points. Read the question carefully and completely. Answers must be written out in paragraph form. Outlines, bulleted lists, or diagrams alone are not acceptable. II Substrate Concentration [S] The graph above shows the initial rate of an enzyme-catalyzed reaction at different substrate concentrations in the presence of a constant concentration of the enzyme. Connect the primary structure of the enzyme to its overall shape. I U x X2 5 Initial Rate of Reaction

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