7. An enzyme-catalyzed reaction proceeds by the mechanism below:E+S1ES --2E+PE+A 3 EAEA+S4→ EAS --5→ EA + PE+I6 → EIEAS +17→ EAIS -8 EIS + PA.B.C.E = enzyme, S = substrate, I = inhibitor, P = product and A = activatorRate constants (k's) for the forward reactions are:K1, K2, k3, K4, k5, k6, k7, and k8Rate constants (k's) for the reverse reactions are:k-1, k-3, K.4, k.6, and k.7Write 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 theequations that would result from applying the QUASI STEADY STATE ASSUMPTION.(ONLY ONE EQUATION; ANY OF THEM ARE FINE)

The Rapid Equilibrium Assumption (REA) refers to the assumption that the formation of the…

Answered: 7. An enzyme-catalyzed reaction…

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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6. Examine the plot of the enzyme-catalyzed reaction below: Wheat-germ acid phosphatase shows Michaelis-Menten kinetics when acting on para-nitrophenol phosphate 16 14 12 10 8 4 2 0.0 0.5 1.0 1.5 2.0 2.5 3.0 3.5 (S] / mM a) Is this reaction better characterized by Michaelis-Menten kinetics or simple mass action? b) What is the approximate value of Vmax? Km? c) Assuming that this plot was made at 100 nM enzyme, draw the curve, including axis labels, for 300 nM enzyme. d) Imagine that this enzyme is inhibited by a competitive inhibitor with Ki (for inhibitor) = Km (for substrate). Note that v = (kcat [E] tot [S]/Km) / (1 + [S]/Km + [I]/Ki). Draw the curve of reaction velocity (v) versus [S] for [I] = 1 mM. e) Now consider an experiment where you simultaneously introduce substrate and competitive inhibitor at equal concentrations. Make a plot of v versus concentration of [S] = [I], i.e. the X-axis should be the concentration of both I and S, which are equal. v/ uM min-
Which of the following best explains why enzyme catalysis is affected by a change in pH? A. Change in pH alters ionization states of serine in the active site involved in nucleophilic catalysis B. The ionization states of his, asp and glu involved in acid/base catalysis are altered with change in pH C. Change in pH alters ionization states of contact amino acids in the active site D. All enzymes have optimum pH
All of the following are ways of controlling enzyme mechanism, except A. Edman degradation B. zymogens C. phosphorylation D. allosteric
7
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7. To what main enzyme class do the enzymes that catalyze the following reaction belong? (Oxidoreductases, transferases, hydrolases, lyases, isomerases, ligases) со о 8. Label the following as examples of a "lock and key" model or an "induced fit" enzyme model? substrate a. b. tive sihe a. b. yme-bstrate comples
This assay is the most common method of detection in enzyme assays: A. рН B. spectrophotometric assay C. radiation D. electromagnetism The structure of THF comes from which derivatives: A. Pteridine derivative B. p-Aminobenzoic acid C. Glutamate D. All of the above Role of coenzyme, except for: A. Electron transfer reactions B. Allow precise orientation of the substrate at the active site C. Chemical group transfer reactions D. None of the above
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
Proteases are one of the main drug targets. Choose the False statement regarding proteases. A. Proteases are enzymes that cleave peptide bonds. B. Water is a reactant in the reaction catalyzed by proteases. C. Proteases, like all enzymes show substrate specificity, meaning they cleave only substate that fit the bonding product. D. Proteases rely on the proton transfer from NADH to the substrate. E. Protease mechanism involves only acid-base catalysis.
15) The graph at right shows the results of reaction rate vs. substrate concentration for a Michaelis-Menten type enzyme 16) Th a. True b. False* reaction rate substrate concentration
7. Chalcone isomerase catalyzes the reaction illustrated below. A series of modification experiments were performed on this enzyme to identify which amino acid residues might be in the active site and which might promote the cyclization reaction. OH Ho. Но Explain the following results: A) Acetic anhydride treatment inhibited enzyme activity. B) Pyrocarbonate inhibited activity and was found to modify 7 residues. However, this enzyme only contains 6 His and modification of these did not affect activity. C) lodoacetate inhibited activity but this effect coult be decreased in the presence of substrate or product. D) Methane methanethiol sulfonate modified the enzyme but did not inhibit catalytic turnover. In addition, this modification was reversed in the presence of B-mercaptoethanol. keNyons Rengent
3. b. If chymotrypsin is treated with disopropylfluorophosphate, catalysis cannot occur even in the presence of excess substrate concentration. Is this Inhibltion reversible or Irreversible?. Dilsopropylfluorophosphate Hyd

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