intracellular concentration of P. The increase in P, concentration would drive the unfavorable phosphorylation of glucose b Is increasing the P concentration a reasonable way to couple ATP hydrolysis and glucose phosphorylation? O No. The phosphate salts of divalent cations would be present in excess and precipitate out. Yes. The extra ATP hydrolysis would provide enough free energy to drive the phosphorylation reaction. Yes. Increasing the concentration of P, would decrease K'e and shift equilibrium to the right. No. The extra P would give a negative AG, but would give a positive AG. In hepatocytes, the enzyme glucokinase catalyzes the ATP-coupled phosphorylation of glucose. Glucokinase binds both A and glucose, forming a glucose-ATP-enzyme complex. The enzyme then transfers the phosphoryl group directly from AT

Human Anatomy & Physiology (11th Edition)
11th Edition
ISBN:9780134580999
Author:Elaine N. Marieb, Katja N. Hoehn
Publisher:Elaine N. Marieb, Katja N. Hoehn
Chapter1: The Human Body: An Orientation
Section: Chapter Questions
Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...
icon
Related questions
Question
Coupling ATP hydrolysis to glucose phosphorylation makes thermodynamic sense, but consider how the coupling might
take place.
Given that coupling requires a common intermediate, one conceivable mechanism is to use ATP hydrolysis to raise the
intracellular concentration of P,. The increase in P, concentration would drive the unfavorable phosphorylation of glucose by P.
Is increasing the P concentration a reasonable way to couple ATP hydrolysis and glucose phosphorylation?
No. The phosphate salts of divalent cations would be present in excess and precipitate out.
Yes. The extra ATP hydrolysis would provide enough free energy to drive the phosphorylation reaction.
Yes. Increasing the concentration of P, would decrease K'e and shift equilibrium to the right.
No. The extra P, would give a negative AG, but would give a positive AG.
In hepatocytes, the enzyme glucokinase catalyzes the ATP-coupled phosphorylation of glucose. Glucokinase binds both ATP
and glucose, forming a glucose-ATP-enzyme complex. The enzyme then transfers the phosphoryl group directly from ATP
to glucose.
In hepatocytes, the enzyme glucokinase catalyzes the ATP-coupled phosphorylation of glucose. Glucokinase binds both ATP
and glucose, forming a glucose-ATP-enzyme complex. The enzyme then transfers the phosphoryl group directly from ATP
to glucose.
Select the advantages of phosphoryl group transfer compared to hydrolysis and subsequent phosphorylation?
O Reaction intermediates do not need to be present in excess.
Glucokinase increases the transition state energy, favoring glucose phosphorylation.
O ATP hydrolysis is thermodynamically unfavorable compared to group transfer.
The process takes advantage of the high phosphoryl group transfer potential of ATP.
Transcribed Image Text:Coupling ATP hydrolysis to glucose phosphorylation makes thermodynamic sense, but consider how the coupling might take place. Given that coupling requires a common intermediate, one conceivable mechanism is to use ATP hydrolysis to raise the intracellular concentration of P,. The increase in P, concentration would drive the unfavorable phosphorylation of glucose by P. Is increasing the P concentration a reasonable way to couple ATP hydrolysis and glucose phosphorylation? No. The phosphate salts of divalent cations would be present in excess and precipitate out. Yes. The extra ATP hydrolysis would provide enough free energy to drive the phosphorylation reaction. Yes. Increasing the concentration of P, would decrease K'e and shift equilibrium to the right. No. The extra P, would give a negative AG, but would give a positive AG. In hepatocytes, the enzyme glucokinase catalyzes the ATP-coupled phosphorylation of glucose. Glucokinase binds both ATP and glucose, forming a glucose-ATP-enzyme complex. The enzyme then transfers the phosphoryl group directly from ATP to glucose. In hepatocytes, the enzyme glucokinase catalyzes the ATP-coupled phosphorylation of glucose. Glucokinase binds both ATP and glucose, forming a glucose-ATP-enzyme complex. The enzyme then transfers the phosphoryl group directly from ATP to glucose. Select the advantages of phosphoryl group transfer compared to hydrolysis and subsequent phosphorylation? O Reaction intermediates do not need to be present in excess. Glucokinase increases the transition state energy, favoring glucose phosphorylation. O ATP hydrolysis is thermodynamically unfavorable compared to group transfer. The process takes advantage of the high phosphoryl group transfer potential of ATP.
Expert Solution
trending now

Trending now

This is a popular solution!

steps

Step by step

Solved in 2 steps

Blurred answer
Similar questions
  • SEE MORE QUESTIONS
Recommended textbooks for you
Human Anatomy & Physiology (11th Edition)
Human Anatomy & Physiology (11th Edition)
Biology
ISBN:
9780134580999
Author:
Elaine N. Marieb, Katja N. Hoehn
Publisher:
PEARSON
Biology 2e
Biology 2e
Biology
ISBN:
9781947172517
Author:
Matthew Douglas, Jung Choi, Mary Ann Clark
Publisher:
OpenStax
Anatomy & Physiology
Anatomy & Physiology
Biology
ISBN:
9781259398629
Author:
McKinley, Michael P., O'loughlin, Valerie Dean, Bidle, Theresa Stouter
Publisher:
Mcgraw Hill Education,
Molecular Biology of the Cell (Sixth Edition)
Molecular Biology of the Cell (Sixth Edition)
Biology
ISBN:
9780815344322
Author:
Bruce Alberts, Alexander D. Johnson, Julian Lewis, David Morgan, Martin Raff, Keith Roberts, Peter Walter
Publisher:
W. W. Norton & Company
Laboratory Manual For Human Anatomy & Physiology
Laboratory Manual For Human Anatomy & Physiology
Biology
ISBN:
9781260159363
Author:
Martin, Terry R., Prentice-craver, Cynthia
Publisher:
McGraw-Hill Publishing Co.
Inquiry Into Life (16th Edition)
Inquiry Into Life (16th Edition)
Biology
ISBN:
9781260231700
Author:
Sylvia S. Mader, Michael Windelspecht
Publisher:
McGraw Hill Education