28. Describe the role of an amplifier enzyme.

Enzymes are proteins that help in accelerating chemical reactions. An enzyme is called an amplifier…

Answered: 28. Describe the role of an amplifier…

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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Similar questions

1. Compare and contrast the activation free energy and the free energy change for an enzyme-catalyzed reaction.
111 The Michaelis constant is represented by what variable, and is comprised of which rate constants in the overall enzyme rate equation? e. Km, kf, kr and k_cat f. Vmax, kf and kcat g. Km, kf, kr and kcat h. Vmax, kf, kr and kcat Km, kf and kcat i.
12.
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
11.Discuss three mechanisms through which lactate can be used as an energy source.
How Tightly Do Transition-State Analogs Bindto the Active Site? 4
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
15. The second high energy intermediate metabolite of glycolysis that can be used for substrate level phosphorylation is also a precursor molecule for the synthesis of several amino acids. Name 5 of these amino acids.
8.Choose the False statement about enzyme binding sites Binding at an allosteric site ca affect binding and catalysis at the Ortho steric site. In addition to ortho steric sites , some enzymes have other sites where catalysis can be conducted. They are called , allosteric sites, from “allo,” the other. In principle, allosteric ligands can have structures that do not resemble those of substrates. Ligand binding at an allosteric site can cause a conformational change of an enzyme. Enzyme can be inhibited by an allosteric ligand that does not complete with substrate.
1. Describe the two ways by which the activity of an enzyme can be inhibited.
15. Dodgerase is an enzyme that is exquisitely inhibited by a class of cheaters (Astrozolamide and Redsoxin). Dodgerase plays an important role in the civic pride of one of the greatest and most diverse cities in the world. The experimental curve of initial reaction velocity (as percentage of Vmax) versus [S] for the Dodgerase reaction is shown (upper curve). When the experiment was run in 2017, in the presence of inhibitor, the lower curve was obtained. From an inspection of the curves and your knowledge of the kinetic properties of competitive, uncompetitive and mixed inhibitors, determine the nature of the inhibition by Astrozolamide and explain your reasoning! 100 No inhibitor 50 Astrozolamide 0.2 0.4 0.6 0.8 [S] (mm) pee"A JO %) A
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…

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