11. For a reaction A + B → P +Q, which is catalyzed by an enzyme (E), the following observations aremade: i) a AEB complex is formed during the reaction; ii) The product Q is always released before theproduct P is released. Based on the observations, the mechanism of the reaction is:A. Random mechanismB. Ping-pong mechanismC. Both A and BD. Neither A nor B

A)First understand both the mechanismPing-pong mechanism- In this type of reaction proceeds through…

Answered: 11. For a reaction A + B → P +Q, which…

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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28. Describe the role of an amplifier enzyme.
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-
6. Consider the reaction: H H SCOA a. What kind of reaction is being performed here? b. What enzyme performs this reaction? c. What cofactors, if any, are required for this reaction? H H SCOA
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:
3
36. If other conditions were to remain constant, which one of the foilowing changes would explain a reduced rate of activity in an enzyme-controiled reaction? a. increase in concentration of end-product b. increase in substrate concentration c. increase in enzyme concentration d. increase in temperature towards the optimum
5. Draw the reaction curve for the follow a) A reaction with an activation energy (EA) = 50 and free energy ( G) = 20 %3D %3D b) A reaction with an activation energy (EA) = 30 and free energy ( G) = - 40 c) Indicate whether the reactions above are anabolic or catabolic Reaction a) %D Reaction b) = %3D
37. Consider the following energy diagram for an enzyme-catalyzed reaction. D B A C E G Which step is probably the slowest? a. A →B →C b. C D E c. E F G d. G H I
2. an enzyme-catalyzed reaction is studied in the presence and absence of an inhibitor. The following data was obtained. (S)[M] V (umol/min) V (+inhibitor)(umol/min) 6 x 10-6 20.8 12 1 x 10-5 29 15 2 x 10-5 45 20 6 x 10-5 67.6 24 1.8 x 10-4 87 28 plot 1/[S] as abscissa and 1/V as ordinate for both catalyzed reaction and reaction with inhibitor. Use the same graph for both plots. calculate the Km of enzyme in the reaction without inhibitor Km1 of the enzyme in the reaction with inhibitor Vmax of the uninhibited reaction Vmax of the inhibited reaction what kind of inhibitor was added to the enzyme-catalyzed reaction? explain your answer in terms of changes in Km and Vmax.
3. Which of the following statements regarding enzymes and transition states is true? a. stabilization of the transition state must be less than stabilization of ES for catalysis to occur b. binding of substrate to an enzyme often causes strain, thus promoting transition state formation c. the transition state conformation of an enzyme catalyzed reaction is identical to the conformation seen in the uncatalyzed transition state d. formation of the transition state always assures that the reaction will proceed to product e. none of the above are true 4. What is the starting point for selection of a suitable ion-exchange chromatography matrix for purification of a recombinant protein? a. Prediction of isoelectric point (pl) from the amino acid sequence. b. Test protein binding to an ion-exchange matrix at a range of pHs and salt concentrations. c. Test protein binding to a selection of anion and cation exchange matrices. d. Pass your sample through a preparative column and elute with a…
1. Why do we need to repeat the measurements of reaction of times ten times?
1. Which of the following statements is/are TRUE for both the concerted and sequential models of allosteric enzymes? a. follows the induced-fit model b. the activator can only bind to the R form c. the inhibitor can only bind to the T form d. the substrate can only bind to the R form 2. Which of the following describes the efficiency of enzymatic catalysis? a. [S] b. KM c. Vmax d. kcat

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