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A patient exhibiting all of the symptoms of beriberi is placed on a thiamine- rich diet, but it does not ameliorate the symptoms. Genetic testing indicates the patient has a defect in the enzyme pyruvate dehydrogenase phosphatase. How does this finding explain the symptoms of beriberi and the observation that thiamine supplements did not work? The patient is unable to use thiamine as a coenzyme in the pyruvate dehydrogenase reaction because defective pyruvate dehydrogenase phosphatase keeps the pyruvate dehydrogenase in R state, which does not bind thiamine; adding more thiamine does not ameliorate the beriberi symptoms. O A defect in pyruvate dehydrogenase phosphatase means that pyruvate dehydrogenase remains in the phosphorylated inactive state; thiamine supplements cannot substitute for a defective pyruvate dehydrogenase phosphatase enzyme. A defect in pyruvate dehydrogenase phosphatase means that pyruvate dehydrogenase remains in the phosphorylated active state, which uses up too much thiamine; adding more thiamine doesn't work because pyruvate dehydrogenase metabolizes it quicker than it can be used. The enzyme pyruvate dehydrogenase phosphatase converts thiamine to

A patient exhibiting all of the symptoms of beriberi is placed on a thiamine- rich diet, but it does not ameliorate the symptoms. Genetic testing indicates the patient has a defect in the enzyme pyruvate dehydrogenase phosphatase. How does this finding explain the symptoms of beriberi and the observation that thiamine supplements did not work? The patient is unable to use thiamine as a coenzyme in the pyruvate dehydrogenase reaction because defective pyruvate dehydrogenase phosphatase keeps the pyruvate dehydrogenase in R state, which does not bind thiamine; adding more thiamine does not ameliorate the beriberi symptoms. O A defect in pyruvate dehydrogenase phosphatase means that pyruvate dehydrogenase remains in the phosphorylated inactive state; thiamine supplements cannot substitute for a defective pyruvate dehydrogenase phosphatase enzyme. A defect in pyruvate dehydrogenase phosphatase means that pyruvate dehydrogenase remains in the phosphorylated active state, which uses up too much thiamine; adding more thiamine doesn't work because pyruvate dehydrogenase metabolizes it quicker than it can be used. The enzyme pyruvate dehydrogenase phosphatase converts thiamine to

Biochemistry
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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A patient exhibiting all of the symptoms of beriberi is placed on a thiamine- rich diet, but it does not ameliorate the symptoms. Genetic testing indicates the patient has a defect in the enzyme pyruvate dehydrogenase phosphatase. How does this finding explain the symptoms of beriberi and the observation that thiamine supplements did not work? The patient is unable to use thiamine as a coenzyme in the pyruvate dehydrogenase reaction because defective pyruvate dehydrogenase phosphatase keeps the pyruvate dehydrogenase in R state, which does not bind thiamine; adding more thiamine does not ameliorate the beriberi symptoms. A defect in pyruvate dehydrogenase phosphatase means that pyruvate dehydrogenase remains in the phosphorylated inactive state; thiamine supplements cannot substitute for a defective pyruvate dehydrogenase phosphatase enzyme. A defect in pyruvate dehydrogenase phosphatase means that pyruvate dehydrogenase remains in the phosphorylated active state, which uses up too much thiamine; adding more thiamine doesn't work because pyruvate dehydrogenase metabolizes it quicker than it can be used. The enzyme pyruvate dehydrogenase phosphatase converts thiamine to
Transcribed Image Text:A patient exhibiting all of the symptoms of beriberi is placed on a thiamine- rich diet, but it does not ameliorate the symptoms. Genetic testing indicates the patient has a defect in the enzyme pyruvate dehydrogenase phosphatase. How does this finding explain the symptoms of beriberi and the observation that thiamine supplements did not work? The patient is unable to use thiamine as a coenzyme in the pyruvate dehydrogenase reaction because defective pyruvate dehydrogenase phosphatase keeps the pyruvate dehydrogenase in R state, which does not bind thiamine; adding more thiamine does not ameliorate the beriberi symptoms. A defect in pyruvate dehydrogenase phosphatase means that pyruvate dehydrogenase remains in the phosphorylated inactive state; thiamine supplements cannot substitute for a defective pyruvate dehydrogenase phosphatase enzyme. A defect in pyruvate dehydrogenase phosphatase means that pyruvate dehydrogenase remains in the phosphorylated active state, which uses up too much thiamine; adding more thiamine doesn't work because pyruvate dehydrogenase metabolizes it quicker than it can be used. The enzyme pyruvate dehydrogenase phosphatase converts thiamine to
The patient is unable to use thiamine as a coenzyme in the pyruvate dehydrogenase reaction because defective pyruvate dehydrogenase phosphatase keeps the pyruvate dehydrogenase in R state, which does not bind thiamine; adding more thiamine does not ameliorate the beriberi symptoms. A defect in pyruvate dehydrogenase phosphatase means that pyruvate dehydrogenase remains in the phosphorylated inactive state; thiamine supplements cannot substitute for a defective pyruvate dehydrogenase phosphatase enzyme. A defect in pyruvate dehydrogenase phosphatase means that pyruvate dehydrogenase remains in the phosphorylated active state, which uses up too much thiamine; adding more thiamine doesn't work because pyruvate dehydrogenase metabolizes it quicker than it can be used. The enzyme pyruvate dehydrogenase phosphatase converts thiamine to thymidine, which is required for pyruvate dehydrogenase reaction and prevention of beriberi; adding thiamine does not help because it is the missing thymidine causing beriberi.
Transcribed Image Text:The patient is unable to use thiamine as a coenzyme in the pyruvate dehydrogenase reaction because defective pyruvate dehydrogenase phosphatase keeps the pyruvate dehydrogenase in R state, which does not bind thiamine; adding more thiamine does not ameliorate the beriberi symptoms. A defect in pyruvate dehydrogenase phosphatase means that pyruvate dehydrogenase remains in the phosphorylated inactive state; thiamine supplements cannot substitute for a defective pyruvate dehydrogenase phosphatase enzyme. A defect in pyruvate dehydrogenase phosphatase means that pyruvate dehydrogenase remains in the phosphorylated active state, which uses up too much thiamine; adding more thiamine doesn't work because pyruvate dehydrogenase metabolizes it quicker than it can be used. The enzyme pyruvate dehydrogenase phosphatase converts thiamine to thymidine, which is required for pyruvate dehydrogenase reaction and prevention of beriberi; adding thiamine does not help because it is the missing thymidine causing beriberi.
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