Is increasing the P; concentration a reasonable way to couple ATP hydrolysis and glucose phosphorylation? Yes. Increasing the concentration of P; would decrease K'eq and shift equilibrium to the right. No. The phosphate salts of divalent cations would be present in excess and precipitate out. No. The extra P; would give a negative AG", but would give a positive AG. Yes. The extra ATP hydrolysis would provide enough free energy to drive the phosphorylation reaction.

Is increasing the P; concentration a reasonable way to couple ATP hydrolysis and glucose phosphorylation? Yes. Increasing the concentration of P; would decrease K'eq and shift equilibrium to the right. No. The phosphate salts of divalent cations would be present in excess and precipitate out. No. The extra P; would give a negative AG", but would give a positive AG. Yes. The extra ATP hydrolysis would provide enough free energy to drive the phosphorylation reaction.

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter27: Metabolic Integration And Organ Specialization

Section: Chapter Questions

Problem 20P: Figure 27.3 illustrates the response of R (ATP-regenerating) and U (ATP-utilizing) enzymes to energy...

See similar textbooks

Similar questions

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 P₁. The increase in P; concentration would drive the unfavorable phosphorylation of glucose by P₁.
.Intramitochondrial ATP concentrations are about 5 mM, and phosphate con- centration is about 10 mM. If ADP is five times more abundant than AMP, calculate the molar concentrations of ADP and AMP at an energy charge of 0.85. Calculate AG for ATP hydrolysis at 37 °C under these conditions. The energy charge is the concentration of ATP plus half the concentration of ADP divided by the total adenine nucleotide concentration: [ATP] + 1/2[ADP] [ATP] + [ADP] + [AMP]
The AG of the reaction C6H12O6 + 60₂ --> 6CO₂ + 6H₂O is -686 kcal/mol glucose oxidized. The AG of the reaction ADP + P₁ --> ATP + H₂O is + 7.3 kcal/mol ATP synthesized. The oxidation of glucose can be coupled to the synthesis of ATP. If the coupling is 50% efficient, how many molecules of ATP can be synthesized per molecule of glucose oxidized? Round your answer to the nearest whole number.
The AG of the reaction C6H1206+602 --> 6 CO2 + 6H₂O is -686 kcal/mol glucose oxidized. The AG of the reaction ADP + P --> ATP + H₂O is + 7.3 kcal/mol ATP synthesized. The oxidation of glucose can be coupled to the synthesis of ATP. If the coupling is 50% efficient, how many molecules of ATP can be synthesized per molecule of glucose oxidized? Round your answer to the nearest whole number. Type your answer... rces K esc Q 7 c с 72 W #3 E 14 R LL Search or type URL % 65 T G A MacBook Pro 6 Y H & 7 U * 8 + - ( 9 J ၂ ။ K 0 ) 0 L P { + 11 } ] Submit delete return
. Because of the position of arsenic in the periodic table, arsenate (AsO}-) is chemically similar to inorganic phosphate and is used by phosphate-requiring enzymes as an alternative substrate. However, organic arsenates are quite unstable and spontaneously hydrolyze. Arsenate is known to inhibit ATP production in glycolysis. Identify the target enzyme, and explain the mechanism of inhibition.
During a 20-minute workout, a person burns 350 calories. What is the number of grams of glucose undergoing glycolysis in muscle cells with ample supply of oxygen? NADH in muscle cells is transported via the glycerol phosphate shuttle (which byhpasses Complexes I and II of the ETC). The human ATP synthase has 8 c subunits. Take note: Molar mass of glucose is 180 g/mol 1 calorie = 4.184 J phosphorylation potential in muscle cells is ~55 kJ/mol
Give all the reactions that will produce ATP either by substrate-level phosphorylation (SLP) or by oxidative phosphorylation (OP). If the given require a shuttle system, please indicate both MA shuttle and GP shuttle and give the ATP produced. Given: fructose 6-phosphate to 2pyruvate
Free energy changes under intracellular conditions differ markedly from those determined under standard conditions. AG" =-30.5 kJ/mol for ATP hydrolysis to ADP and P,. Calculate AG for ATP hydrolysis in a cell at 37 °C that contains [ATP] =3 mM, [ADP] =1mM, and [P] =1 mM.
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…
Allosteric regulation plays a very important role in the regulation of glycogen metabolism. Which of thefollowing is correct? -AMP allosterically inhibits glycogen phosphorylase -Glucose-6-phosphate allosterically activates glycogen synthase -Both A and B -Neither A nor B The value of standard free energy change for reaction A --> B is +3.7 kJ/mol. Under which of thefollowing conditions, the reaction will most likely become exergonic in the direction as written? -Mass action ratio is larger than the equilibrium constant -Couple with ATP hydrolysis -Both A and B -Neither A nor B
Give all the reactions that will produce ATP either by substrate-level phosphorylation (SLP) or by oxidative phosphorylation (OP). If the given require a shuttle system, please indicate both MA shuttle and GP shuttle and give the ATP produced. Given: glucose 6-phosphate to 2succinly CoA
Enzymes normally enhance the rates of biochemical reactions by preferentially binding and stabilizing the transition states rather than either the substrates or the products of a reaction. The F|-subunit of ATP synthase does not fit this norm so well as tight binding to ATP rather than a transition state is employed to make ATP. Explain the binding-change model of the mechanism of ATP-synthase. How and why is the proton-motive force used in the reaction cycle of ATP synthase?