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Macmillan Learning The phosphorylation of glucose to glucose 6-phosphate is the initial step in the catabolism of glucose. The direct phosphorylation of glucose by P, is described by the equation Glucose + P ← glucose 6-phosphate + H₂O AG = 13.8 kJ/mol 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 Pi. The increase in P; concentration would drive the unfavorable phosphorylation of glucose by Pi- 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. Increasing the concentration of P; would decrease K'eq and shift equilibrium to the right. Yes. The extra ATP hydrolysis would provide enough free energy to drive the phosphorylation reaction. 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. Select the advantages of phosphoryl group transfer compared to hydrolysis and subsequent phosphorylation? Reaction intermediates do not need to be present in excess. The process takes advantage of the high phosphoryl group transfer potential of ATP. ATP hydrolysis is thermodynamically unfavorable compared to group transfer. Glucokinase increases the transition state energy, favoring glucose phosphorylation.

Macmillan Learning The phosphorylation of glucose to glucose 6-phosphate is the initial step in the catabolism of glucose. The direct phosphorylation of glucose by P, is described by the equation Glucose + P ← glucose 6-phosphate + H₂O AG = 13.8 kJ/mol 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 Pi. The increase in P; concentration would drive the unfavorable phosphorylation of glucose by Pi- 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. Increasing the concentration of P; would decrease K'eq and shift equilibrium to the right. Yes. The extra ATP hydrolysis would provide enough free energy to drive the phosphorylation reaction. 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. Select the advantages of phosphoryl group transfer compared to hydrolysis and subsequent phosphorylation? Reaction intermediates do not need to be present in excess. The process takes advantage of the high phosphoryl group transfer potential of ATP. ATP hydrolysis is thermodynamically unfavorable compared to group transfer. Glucokinase increases the transition state energy, favoring glucose phosphorylation.

Biochemistry
Biochemistry
6th Edition
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Reginald H. Garrett, Charles M. Grisham
Chapter20: Electron Transport And Oxidative Phosphorylation
Section: Chapter Questions
Problem 13P
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Macmillan Learning The phosphorylation of glucose to glucose 6-phosphate is the initial step in the catabolism of glucose. The direct phosphorylation of glucose by P, is described by the equation Glucose + P ← glucose 6-phosphate + H₂O AG = 13.8 kJ/mol 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 Pi. The increase in P; concentration would drive the unfavorable phosphorylation of glucose by Pi- 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. Increasing the concentration of P; would decrease K'eq and shift equilibrium to the right. Yes. The extra ATP hydrolysis would provide enough free energy to drive the phosphorylation reaction. 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. Select the advantages of phosphoryl group transfer compared to hydrolysis and subsequent phosphorylation? Reaction intermediates do not need to be present in excess. The process takes advantage of the high phosphoryl group transfer potential of ATP. ATP hydrolysis is thermodynamically unfavorable compared to group transfer. Glucokinase increases the transition state energy, favoring glucose phosphorylation.
Transcribed Image Text:Macmillan Learning The phosphorylation of glucose to glucose 6-phosphate is the initial step in the catabolism of glucose. The direct phosphorylation of glucose by P, is described by the equation Glucose + P ← glucose 6-phosphate + H₂O AG = 13.8 kJ/mol 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 Pi. The increase in P; concentration would drive the unfavorable phosphorylation of glucose by Pi- 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. Increasing the concentration of P; would decrease K'eq and shift equilibrium to the right. Yes. The extra ATP hydrolysis would provide enough free energy to drive the phosphorylation reaction. 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. Select the advantages of phosphoryl group transfer compared to hydrolysis and subsequent phosphorylation? Reaction intermediates do not need to be present in excess. The process takes advantage of the high phosphoryl group transfer potential of ATP. ATP hydrolysis is thermodynamically unfavorable compared to group transfer. Glucokinase increases the transition state energy, favoring glucose phosphorylation.
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