Part E please!! 1.A substrate is converted to product using an enzyme that follows the mechanism below when an inhibitor (1)and an activator (A) are both present in the reaction mixture.ES (2)→→ E + PE+S (1)E +1 < (3) → EIE+A← (4)→ EA{the inhibitor and activator do not bind simultaneously}EI + SEA+S(5) → EIS -(6)→ EI + P(7)→ EAS-(8)→ EA + Pwith reaction rate constants of k₁ and k.₁ (and so on) for each of the reactions:A. Although this mechanism does not match exactly any of the inhibitor mechanisms discussed in class, whichtype of inhibitor is this most like (competitive, uncompetitive or non-competitive)?B. Write the enzyme balance equation.C. Write the total rate of product, P, formation based on the kinetic rate constants and concentrations ofintermediate species.D. Write each of the equations that result from applying the rapid equilibrium and quasi steady stateassumptions.E. Knowing that I is an inhibitor and A is an activator, discuss the relative values of k₂, k6 and kg.

Rate of a reaction is the product of substrate concentration and rate constant. For example,…

Answered: Knowing that I is an inhibitor and A is…

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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4. An enzyme-substrate complex has a Kd = 100 nM. A competitive inhibitor with which of the following Ki values will be most effective at inhibiting this enzyme? A) K₁ = 10 nM B) K₁ = 100 nM C) K₁ = 1000 nM D) None of the above - only the KM is important Briefly explain:
7. An enzyme-catalyzed reaction proceeds by the mechanism below: E+S1ES --2E+P E+A 3 EA EA+S4→ EAS --5→ EA + P E+I6 → EI EAS +17→ EAIS -8 EIS + P A. B. C. E = enzyme, S = substrate, I = inhibitor, P = product and A = activator Rate constants (k's) for the forward reactions are: K1, K2, k3, K4, k5, k6, k7, and k8 Rate constants (k's) for the reverse reactions are: k-1, k-3, K.4, k.6, and k.7 Write the enzyme balance for this mechanism. How many total equations will result from applying the RAPID EQUILIBRIUM ASSUMPTION? Using any concentrations of species in the mechanism and any of the rate constants (k's), write ONE of the equations that would result from applying the QUASI STEADY STATE ASSUMPTION. (ONLY ONE EQUATION; ANY OF THEM ARE FINE)
5. Which of the following statements is/are correct regarding allosteric regulation?a) Allosteric effector controls the activity of an enzyme by irreversible binding.b) Allosteric effector binds to the regulatory sitec) Allosteric activator causes changes in the catalytic site enhancing the substrate binding.d) Allosteric inhibitor causes changes in the catalytic site decreasing the substrate binding. explain each option
6. Which of the following is true of the binding energy derived from enzyme-substrate interactions? A) It cannot provide enough energy to explain the large rate accelerations brought about by enzymes. B) It is sometimes used to hold two substrates in the optimal orientation for reaction. C) It is the result of covalent bonds formed between enzyme and substrate. D) Most of it is derived from covalent bonds between enzyme and substrate. E) Most of it is used up simply binding the substrate to the enzyme. B
3. Draw a properly-labeled reaction progress diagram with two lines: one line for the enzyme-catalyzed reaction, and one line for the enzyme-uncatalyzed reaction. The simplified expression for the reaction is S→ P. Assume this reaction is thermodynamically favorable. Show all appropriate species for the enzymatic reaction. Then, answer these questions: A) Are AG and AG# the same thing? B) Which of these properties is related to reaction velocity (k), and what equation describes that relationship? C) Finally, exactly how do enzymes speed up reaction rates? In your answer, please provide both a thermodynamic argument AND a structural argument.
All of the following statements about competitive and non-competitive inhibitors are true EXCEPT:(a) Competitive inhibitors are structurally similar to anenzyme’s substrate and bind to the enzyme’s allostericsite.(b) Competitive inhibitors work by competing with a sub-strate for binding to an enzyme’s active site.(c) Noncompetitive inhibitors can bind at sites other thanthe active site of an enzyme, distorting the tertiary pro-tein structure, which alters the shape of the active site,rendering it ineffective for substrate binding.(d) Some noncompetitive inhibitors bind reversibly whilesome bind irreversibly to their enzyme.(e) b and d.
1. In zero order reaction, the reaction rate depends only on enzyme concentration. In first order reaction the reaction rate is directly porportional to substyrate concentration a. first statement is false and second statement is true b. both statement is true c. both statement is false d. first statement is true and second statement is false 2. These are catalyst that can be used in the monitoring and diagnosis of disease and their remarkable properties make them sensitive indicators of pathologic changes. a. enzymes b. electrolytes c. substrate d. none of these 3. ALT is stavle in serum at refrigirator or temp for up to 3 weeks, indefinitely if frozen AST has the same stability but markedly decreases with freezing a. both statement are true b. both statement are false c. first statement is true second is false d. second statement is true first statement is false
Which model for enzyme-substrate chemical complementarity is described by the following: Before substrate binding, some enzyme molecules have active sites complementary to substrates and other enzyme molecules have non-complementary active sites. Substrate molecules preferentially bind to the enzyme molecules with complementary active sites. Non-complementary enzyme molecules undergo a structural change to become complementary to maintain conformational equilibrium. a) conformational selection b) induced fit c) lock and key...
1. Consider the following parameters related to an enzyme that follows Michaelis-Menten kinetics for the reaction: k(1) k(2) S ----> ES ----> P k(-1)
A medicinal chemist is trying to determine the mechanism of action of inhibitors she has synthesized. The relative change in KM and Vmax upon incubation of the targeted enzyme with each inhibitor is shown in the table below. Inhibitor A Inhibitor B Inhibitor C Using this data, the mechanism of action of Inhibitor C is: Uncompetitive TS‡ analog Mixed Inhibition Competitive Кмарр- Км 0 Non-competitive app - Vmax <0 <0 0 Vmax
One of the hallmarks of competitive inhibition is that there is constant competition betweenthe substrate and the inhibitor for binding to the enzyme active site.a) If [inhibitor] >> [substrate], which compound “wins” (i.e., occupies the active site a greaterpercentage of the time)?b) If [substrate] >> [inhibitor], which compound “wins” (i.e., occupies the active site a greaterpercentage of the time)?
1. Consider an enzyme-catalyzed reaction giving the following results at a fixed enzyme concentration of 1 x 10-6 M in the presence or absence of 5 mM or 10 mM concentrations of an inhibitor I [S] (mol/L) 0.0010 0.0025 0.0050 0.0100 0.0500 0.1000 a) Control 0.00167 0.00333 0.00500 0.00667 0.00909 0.00952 v (m/s) [I] = 5 mM 0.00090 0.00200 - 0.00333 0.00500 0.00833 0.00909 [I] = 10 mM 0.00062 0.00142 0.00250 0.00400 0.00769 0.00869 Estimate Vmax and KM for all cases. What type inhibitor is [I]? Estimate K₁ and/or Kı' depending on the type inhibitor. Estimate Kcat. Estimate Kcat/KM.

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Knowing that I is an inhibitor and A is an activator, discuss the relative values of k₂, k6 and ks.