Question 22 2 pts You are a scientist studying the effects of arsenic on muscle cells. You read an article online claiming that arsenic is a competitive inhibitor of pyruvate dehydrogenase. You read another article claiming that arsenic is an allosteric inhibitor of pyruvate dehydrogenase. Match the following observations with the claim they would support if true. A. An effective treatment against arsenic poisoning is the addition of large amounts of pyruvate. Allosteric Inhibitor B. Arsenic binds to pyruvate dehydrogenase at a different site than where pyruvate binds. Competitive Inhibitor C. Arsenic reversibly binds to pyruvate dehydrogenase in the active site. Competitive Inhibitor D. Arsenic has a very different chemical structure than pyruvate. Allosteric Inhibitor
Question 22 2 pts You are a scientist studying the effects of arsenic on muscle cells. You read an article online claiming that arsenic is a competitive inhibitor of pyruvate dehydrogenase. You read another article claiming that arsenic is an allosteric inhibitor of pyruvate dehydrogenase. Match the following observations with the claim they would support if true. A. An effective treatment against arsenic poisoning is the addition of large amounts of pyruvate. Allosteric Inhibitor B. Arsenic binds to pyruvate dehydrogenase at a different site than where pyruvate binds. Competitive Inhibitor C. Arsenic reversibly binds to pyruvate dehydrogenase in the active site. Competitive Inhibitor D. Arsenic has a very different chemical structure than pyruvate. Allosteric Inhibitor
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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You can choose either allosteric or competitive inhibitor for all questions.
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Pyruvate is acted upon by pyruvate dehydrogenase to convert pyruvate to acetyl-CoA. The acetyl-CoA enters The TCA cycle to generate ATP, NADH, and FADH2.
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