Connect with Learnsmart Labs Access Anatomy & Physiology : An Integrative Approach
Connect with Learnsmart Labs Access Anatomy & Physiology : An Integrative Approach
2nd Edition
ISBN: 9781259657269
Author: Valerie Dean O'Loughlin, Theresa Stouter Bidle Michael P. McKinley
Publisher: Mcgraw-Hill
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Chapter 3, Problem 4DYKB

ATP inhibits phosphofructokinase by binding to an allosteric site in glycolysis. ATP is functioning as a

  1. a. competitive inhibitor.
  2. b. competitive activator.
  3. c. noncompetitive inhibitor.
  4. d. noncompetitive activator.
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Which of the following is incorrect about the ATP synthase mechanism?   a. It explains how ATP is hydrolyzed into ADP and Pi   b. At any moment, each catalytic site has a different conformation and binding affinity   c. It is called the binding change mechanism   d. It involves rotation-driven conformational changes that alter the affinity of each catalytic subunit
Which of the following reactions is the most exergonic? a   Conversion of PEP to Pyruvate b   Conversion of Glucose-6-phosphate to Glucose c   All of the reactions are equally exergonic. d   Hydrolysis of ATP
Which of the following statements concerning ATP synthesis is NOT true? a. The open conformation of the ATP synthase is for releasing ATP. b.   The gamma subunit in the stalk responds to the flow of H+ and rotates the assembly counterclockwise and thus change the conformations of the active site to synthesize ATP.   c.   The tight conformation of the ATP synthase is for converting ADP and phosphate to ATP.   d.   The loose conformation of the ATP synthase is for binding ADP and phosphate.   e. Ten protons are required to catalyze the rotation of the subunits so that one ATP is synthesized. Clear my choice

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