QUESTION 28Recall the reaction catalyzed by phosphoglucomutase:glucose-1-phosphate <--> glucose-6-phosphateAssume that in liver cells under fed conditions, the G1P concentration = 2.5x10-2 M, and the G6P concentration = 1x10-3 M. Using the equation AG = AGO + RTIN([product)/freactant]), calculate AG for thereaction, given that:AGO = -7.1 kJ mol-1R = 8.315x10-3 kJ mol-1 K-1T = 310 K (37°C)In which direction will the reaction proceed spontaneously under these conditions?O +1.2 kl mol1; reverse reaction spontaneous.O -3.5 kl mol-1: forward reaction spontaneous.O -10.7 k) mol1; forward reaction spontaneous.O -15.4 kJ mol1; forward reaction spontaneous.

The enzyme phosphoglucomutase is involved in glycogenolysis and glycogenesis. It catalyzes both…

Answered: QUESTION Recall the reaction catalyzed…

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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Question:- 33) Glucose-6-phosphate has different pathways that it can enter in the liver during the fed state. All of the following are possible except OA.) it is oxidized to acetyl CoA for fatty acid biosynthesis O B). it can enter the pathway for glycogen biosynthesis O c.) it is a substrate for glucose-6-phosphatase OD. )it is oxidized in glycolysis to provide energy for the body
QUESTION NO. 1L-Carnitine is synthesized primarily in the liver but also in the kidneys and then transported to other tissues. It is most concentrated in tissues that use fatty acids as their primary fuel, such as skeletal and cardiac muscle. In this regard, L-carnitine plays an important role in energy production by conjugating to fatty acids for transport from the cytosol into the mitochondria. L-carnitine shuttle is an example of A. ion driven active transport B. facilitated diffusion C. simple diffusion D. ATP driven active transportE. symport F. antiportQUESTION NO.2 Statements: (1) Glucose is both a hexose and a aldose. (2) There can never be more than three enantiomers for a molecule. (3) All common disaccharides have beta-one-four linkages. Which statements are true?
Question 1: When the CAC is run in reverse by microorganisms that use it to fix carbon, the citrate synthase reaction is different and is catalyzed by an enzyme called ATP-citrate lyase. Write the reaction catalyzed by ATP-citrate lyase, then briefly (in one sentence) explain why the use of different chemistry (different from the ‘normal’ direction) makes sense here.
QUESTION 22 When the final product of a series of enzymatically-catalyzed reactions binds to the first enzyme in the pathway to limit its production, it generally uses ___ because the structure of this final product is generally not similar to that of any of the enzyme's normal substrates. Allosteric activation Zymogen activation Covalent modification Competitive inhibition Allosteric inhibition
Question 1: The 4 kinase steps in glycolysis are catalyzed by hexokinase, phosphofructokinase, phosphoglycerate kinase, and pyruvate kinase. Write each of these four reactions, including all participants. i. ii. iii. iv.
Question 29 options: If 6 molecules of acetyl CoA were completely oxidized by the CAC, how many molecules of FADH2 would be produced?
Question: A. To explore the consequences of coupling ATP hydrolysis under physiological conditions to a thermodynamically unfavorable biochemical reaction, consider the hypothetical transformation X⟶Y, for which Δ?′°=20.0 kJ/mol. What is the ratio of [Y]/[X][Y]/[X] at equilibrium? B. Suppose XX and YY participate in a sequence of reactions during which ATP is hydrolyzed to ADP and Pi. The overall reaction is X+ATP+H2O⟶Y+ADP+Pi Calculate [Y]/[X] for this reaction at equilibrium. Assume that the temperature is 25.0 °C and the equilibrium concentrations of ATP, ADP, and Pi are 1.00 M each. C. We know that [ATP], [ADP], and [Pi] are not 1.00 M under physiological conditions. Calculate [Y]/[X] for the ATP‑coupled reaction when the values of [ATP], [ADP], and [Pi] are those found in rat myocytes. Metabolite Concentration in rat myocytes (M) ATP 8.05x10-3 ADP 0.93x10-3 Pi 8.05x10-3
Question 1: The standard reduction potential for the the cytochrome c Fe3+/Fe2+ redox couple and for the dioxygen/water redox couple. Part a: Use these values, and the relevant equation, to compute the standard free energy change for the transfer of 4 electrons from cytochrome c to dioxygen. Part b: Next, compute the free energy needed to pump four protons across the mitochondrial membrane, using the relevant equation and values of -.14V for Δψ and 1.4 for ΔpH. Part c: If energy conservation by cytochrome c oxidase involved only the four pumped protons (and standard conditions applied), what would be the efficiency of energy conservation at this step? (what is the ratio [energy conserved in the gradient] / [redox energy used] ?)
Question 1: In some microorganisms, carbon fixation occurs by reversal of the citric acid cycle. This reversal is accomplished in part by the use of a strong reductant (ferredoxin) to drive the alpha-ketoglutarate dehydrogenase reaction in the reductive direction. Part a: ΔG°‘ for reaction as it occurs in the ‘normal’ (oxidative) citric acid cycle is -30.1 kJ/mol. The standard reduction potential for NADH is -0.32 V. In order to drive the reaction in the reverse direction, the reductant (a ferredoxin) must have a lower reduction potential than NADH/NAD+. Remembering that this is a two-electron reduction, and using the numbers given just above, compute the value of the ferredoxin reduction potential that would be needed to make the standard free energy zero (so that the reductive reaction is enegetically just as favorable as the oxidative reaction). Assume that all of the other reactants are the same in the reductive as in the oxidative reaction. Write out the steps in your calculation;…
Question:- The enzyme aromatase is found in the cytoplasm of some cells and converts testosterone to estrogen. You decide to test aromatase from a particular cell, and oops, your lab partner admits he drastically increased the pH in all the test tubes. Which of the following is a likely result? a. The enzyme will be denatured and the substrate will not bind to the active site. b. The enzyme will convert testosterone to estrogen at a faster rate. c. The mistake will have no effect on the experiment, because enzymes are not sensitive to pH. d. The free energy will be lowered and the reaction will not proceed spontaneously.
QUESTION 2An isocitrate dehydrogenase assay was performed on the enzyme sample and found to give an absorbance change at 340nm of 0.5 absorbance units perminute. Given that the molar absorption coefficient (E) is 6220 M-1 cm-1 and the pathlength is 1cm, what is the rate of the enzyme catalysed reaction in umol perminute per mL?

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