tatements are TRUE?
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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Which of the following statements are TRUE?
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When palmitic acid and radioactive CoA are added to a liver
homogenate the palmitoyl CoA isolated from the cytoplasm will be
a
radioactive.
When palmitic acid and radioactive CoA are added to a liver
b
homogenate the palmitoyl CoA isolated from the mitochondria will be
radioactive.
When acetyl-COA produced by B-oxidation in the liver exceeds the
capacity of the citrate cycle to use acetyl-CoA the excess acetyl-CoA is
used to form acetoacetate and D-B-hydroxybutyrate.
High rates of ketogenesis are observed in severe uncontrolled diabetes
because the tissues cannot use glucose and must use fats for energy
instead.
High-fat/low carbohydrate diets lead to acetyl-CoA accumulation from
fatty acid degradation because carbohydrates are limiting resulting in
low oxaloacetate levels via Pyruvate Carboxylase and increased flux
through the ketogenic pathway.
e
Acetyl-CoA Carboxylase is the principal regulation point in the

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When acetyl-CoA produced by B-oxidation in the liver exceeds the
capacity of the citrate cycle to use acetyl-CoA the excess acetyl-COA is
used to form acetoacetate and D-B-hydroxybutyrate.
High rates of ketogenesis are observed in severe uncontrolled diabetes
because the tissues cannot use glucose and must use fats for energy
d
instead.
High-fat/low carbohydrate diets lead to acetyl-CoA accumulation from
fatty acid degradation because carbohydrates are limiting resulting in
low oxaloacetate levels via Pyruvate Carboxylase and increased flux
through the ketogenic pathway.
m
Acetyl-CoA Carboxylase is the principal regulation point in the
biosynthesis of fatty acids and as such addition of citrate reduces the
Vmax for the Acetyl-CoA carboxylase reaction.
Conversion of one mole B-ketoacyl-ACP to one mole fully saturated
g
acyl-ACP requires one mole of NADPH.
The thermodynamic driving force for the B-ketoacyl-ACP synthase
(condensing enzyme) is coupled release of CO, and hydrolysis of ATP
h
to ADP.
The product of odd-chain fatty acid degradation (proprionyl CoA) is
converted to succinyl-CoA and then to the gluconeogenic precursor
i
oxaloacetate via the citric acid cycle.
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