Q24 Muscle glycogen phosphorylase, an enzyme that provides glucose to the muscle for energyproduction, gives the following activity. The middle curve shows activity with no AMP or ATPpresent. The other curves show either AMP or AMP + ATP as labeled. Based on this, AMP is a(n)[Select]of glycogen phosphorylase and ATP is a(n)[Select]V✓ [Select]allosteric activatorallosteric inhibitorcompetitive inhibitornoncompetitive inhibitoruncompetitive inhibitor1 mM AMPV1 mM AMPMuscle glycogen phosphorylase, an enzyme that provides glucose to the muscle for energyproduction, gives the following activity. The middle curve shows activity with no AMP or ATPpresent. The other curves show either AMP or AMP + ATP as labeled. Based on this, AMP is a(n)of glycogen phosphorylase and ATP is a(n)✓ [Select ]of glycogen phosphorylase.allosteric activatorallosteric inhibitorcompetitive inhibitornoncompetitive inhibitoruncompetitive inhibitorV[S]1 mM AMP +1 mM ATPof glycogen phosphorylase.Muscle glycogen phosphorylase, an enzyme that provides glucose to the muscle for energyproduction, gives the following activity. The middle curve shows activity with no AMP or ATPpresent. The other curves show either AMP or AMP + ATP as labeled. Based on this, AMP is a(n)[Select]of glycogen phosphorylase and ATP is a(n)1 mM AMP +1 mM ATP[S]of glycogen phosphorylase.[S]1 mM AMP +1 mM ATP

Enzymes are highly specialized proteins that have extraordinary catalytic power, greater than that…

Answered: Muscle glycogen phosphorylase, an…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Intracellular concentrations in resting muscle are as follows: fructose- 6-phosphate, 1.0 mM; fructose-1,6-bisphosphate, 10 mM; AMP, 0.1 mM; ADP, 0.5 mM; ATP, 5 mM; and P, 10 mM. Is the phosphofructokinase reac- tion in muscle more or less exergonic than under standard conditions? By how much?
Intramitochondrial ATP concentrations are about 5 mM, and phosphate concentration 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 ∆G 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.
The drug troglitazone was used to treat diabetes but was withdrawn from the market when patientswho took the drug suffered from severe side effects. The data below show the activity of an enzymein the steroid biosynthetic pathway in the presence and absence of 10 µM troglitazone.[S] (µM) v0 (pmol min-1)Create a plot of 1/v0 vs. 1/[S]. Calculate KM and vmax in presence and absence of inhibitor. Whattype of inhibitor is troglitazone? Clearly support your answer.
Intramitochondrial ATP concentrations are about 5 mM, and phos- phate concentration 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 concentra- tion of ATP plus half the concentration of ADP divided by the total adenine nucleotide concentration: [ATP] + 1/2[ADP] [ATP] + [ADP] + [AMP]
Intracellular concentrations in resting muscle are as follows: fructose6-phosphate, 1.0 mM; fructose-1,6-bisphosphate, 10 mM; AMP, 0.1 mM;ADP, 0.5 mM; ATP, 5 mM; and Pi, 10 mM. Is the phosphofructokinasereaction in muscle more or less exergonic than under standard conditions?By how much?
What is the rationale for the inhibition of muscle glycogen phosphorylase by glucose 6- phosphate when glucose 1- phosphate is the product of the phosphorylase reaction?
The final step in the pathway for the synthesis of glucose from lactate (gluconeogenesis) is: Glucose-6-phosphate + H20 5 Glucose + Pi When glucose-6-phosphate is incubated with the proper enzyme and the reaction runs until equilibrium has been reached, the final concentrations are found to be: glucose-6-phosphate (0.035 mM), glucose (100 mM), and Pi (100 mM). Calculate AG" at 25°C and pH 7. 10:21 PM 4/21/2021 F5 F6 F7 F8 F10 F9 7 8. Backspace ーの

A critical reaction in the production of energy to do work or drive chemical reactions in biological systems is the hydrolysis of adenosine triphosphate, ATP, to adenosine diphosphate, ADP, as described by the reaction ATP(aq)+H2O(l)⟶ADP(aq)+HPO2−4(aq)ATP(aq)+H2O(l)⟶ADP(aq)+HPO42−(aq) for which Δ?∘rxn=−30.5 kJ/molΔGrxn∘=−30.5 kJ/mol at 37.0 °C and pH 7.0. Calculate the value of Δ?rxnΔGrxn in a biological cell in which [ATP]=5.0 mM,[ATP]=5.0 mM, [ADP]=0.10 mM,[ADP]=0.10 mM, and [HPO2−4]=5.0 mM.[HPO42−]=5.0 mM. Δ?rxn=ΔGrxn= kJ/mol
phosphofructokinase is an allosteric enzyme that catalyzes the conversion of fructose 6-phosphate to fructose 1,6-bisphosphate and represents the key control point in mammalian glycolysis. The enzyme is a homotetramer that is inhibited by ATP binding, activated by AMP binding, negatively regulated by phosphorylation, and competitively inhibited by 2,5-anhydro-D-glucitol-1,6-diphosphate. (a) Would you expect a plot of the initial rate of fructose 1,6-bisphosphate formation as a function of substrate concentration to show a sigmoidal or hyperbolic curve? (b) How would each of the regulators above affect the dynamics of the T state to R state equilibrium of phosphofructokinase? Briefly explain your reasoning. (c) If it were possible to isolate phosphofructokinase monomers in an active form, how would you expect the kinetics in (a) to be affected? How would the rate of the reaction be affected by ATP, AMP, and 2,5-anhydro-D-glucitol-1,6-diphosphate? Briefly explain your answers.
The glutamate dehydrogenase (GDH) catalyses the following reaction: +H₂N- H - - CH₂ - CH₂ COO acide glutamique COO™® + NAD+ + H₂O GDH COO C: CH₂ CH₂ COO™ O + NH4+ NADH + H* The activity of GDH is monitored in the sense of the formation of glutamate using the following conditions: -0.2 mL of 5 M ammonium sulphate 2.4 mL of buffer at pH 8 0.1 mL of NADH at 6.15 mg.mL-¹ (M = 709 g.mol-¹) 0.2 mL of 1 M a-ketoglutarate solution Warm mixture at 25 °C for 5 min - Add 0.1 mL of GDH solution containing 1.6 mg.mL-¹protein to start the reaction. acide a-cétoglutarique The change in absorbance at 340 nm is monitored, in a 1-cm cuvette, every minute for 10 min. Results are given in the table below: Data: ENADH at 340 nm = 6220 M¹.cm¹ Time (min) 1 2 3 4 5 6 7 8 9 1.760 1.718 1.675 1.635 1.595 1.550 1.510 1.489 1.476 A340 10 1.451 - Draw the graph A = f(t). Calculate A340 at t = 0 and place this point on the curve. - Comment the shape of the curve, particularly the portion that corresponds to a…
The effect of ATP on the allosteric enzyme PFK-1 is shown below. For a given concentration of fructose 6-phosphate, the PFK-1 activity increases with increasing concentrations of ATP, but a point is reached beyond which increasing the concentration of ATP inhibits the enzyme. (a) Explain how ATP can be both a substrate and an inhibitor of PFK-1. How is the enzyme regulated by ATP? (b) In what ways is glycolysis regulated by ATP levels? (c) The inhibition of PFK-1 by ATP is diminished when the ADP concentration is high, as shown in the illustration. How can this observation be explained? *A graph is included for this question*
ATP is a (+) allosteric effector, and CTP is a (-) allosteric effector of theenzyme ATCase. Both of these heterotropic effectors bind to the regulatorysubunits on ATCase. The substrates of ATCase, aspartate and carbamoylphosphate, bind the enzyme active site with positive cooperativity (i.e.,they exert a “+” homotropic effect on activity). As the concentrations ofthe substrates change from values where [S] ≪ KM to values where [S] issaturating ([S]≫ KM), how will the binding constants for each of the twoallosteric effectors change? In other words, does ATP bind ATCase withhigher affinity when [S] is low or high? Does CTP bind ATCase with higheraffinity when [S] is low or high?

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