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

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Chapter1: The Human Body: An Orientation
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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.
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