3. Glycogen phosphorylase converts glycogen into glucose monomers and is the rate limiting step in glycogenolysis (that will be treated later in the course). It catalyzes the following reaction: (a-1,4 glycogen chain), + P, (a-1,4 glycogen chain) 1 +a-D-glucose-1-phosphate a. Glycogen phosphorylase is a K-system allosteric enzyme. Draw a plot of the rate for Glycogen phosphorylase versus inorganic phosphate concentration. Explain why the curve you drew is similar or different from the normal Michaelis-Menten curve. b. Based on the fact that glycogen phosphorylase is a k-system inhibitor and the plot you drew for part a, do you expect the enzyme to be a monomer or a dimer (note that a

Biochemistry
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Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
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Chapter1: Biochemistry: An Evolving Science
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single glycogen phosphorylase chain has I single Pi substrate binding site)?
c. Given that ATP and Glucose is an inhibitor of glycogen phosphorylase and AMP is a
positive effector draw a new curve showing schematically the rate of glycogen
phosphorylase versus phosphate concentration in the presence of Glucose and AMP,
and explain how and why the curve is affected.
d. Considering that glycogenolysis helps make glucose stored as glycogen available for
glycolysis, what rational might explain why ATP and glucose are inhibitors and AMP
a positive effector?
e. If glycogen phosphorylase was a V-system enzyme how would a plot of plot of the
rate for Glycogen phosphorylase versus inorganic phosphate concentration change in
the presence of ATP and AMP?
Transcribed Image Text:single glycogen phosphorylase chain has I single Pi substrate binding site)? c. Given that ATP and Glucose is an inhibitor of glycogen phosphorylase and AMP is a positive effector draw a new curve showing schematically the rate of glycogen phosphorylase versus phosphate concentration in the presence of Glucose and AMP, and explain how and why the curve is affected. d. Considering that glycogenolysis helps make glucose stored as glycogen available for glycolysis, what rational might explain why ATP and glucose are inhibitors and AMP a positive effector? e. If glycogen phosphorylase was a V-system enzyme how would a plot of plot of the rate for Glycogen phosphorylase versus inorganic phosphate concentration change in the presence of ATP and AMP?
3. Glycogen phosphorylase converts glycogen into glucose monomers and is the rate limiting
step in glycogenolysis (that will be treated later in the course). It catalyzes the following
reaction:
(a-1,4 glycogen chain), + P,= (a-1,4 glycogen chain).-1+a-D-glucose-1-phosphate
a. Glycogen phosphorylase is a K-system allosteric enzyme. Draw a plot of the rate for
Glycogen phosphorylase versus inorganic phosphate concentration. Explain why the
curve you drew is similar or different from the normal Michaelis-Menten curve.
b. Based on the fact that glycogen phosphorylase is a k-system inhibitor and the plot you
drew for part a, do you expect the enzyme to be a monomer or a dimer (note that a
Transcribed Image Text:3. Glycogen phosphorylase converts glycogen into glucose monomers and is the rate limiting step in glycogenolysis (that will be treated later in the course). It catalyzes the following reaction: (a-1,4 glycogen chain), + P,= (a-1,4 glycogen chain).-1+a-D-glucose-1-phosphate a. Glycogen phosphorylase is a K-system allosteric enzyme. Draw a plot of the rate for Glycogen phosphorylase versus inorganic phosphate concentration. Explain why the curve you drew is similar or different from the normal Michaelis-Menten curve. b. Based on the fact that glycogen phosphorylase is a k-system inhibitor and the plot you drew for part a, do you expect the enzyme to be a monomer or a dimer (note that a
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