How can an unfavorable reaction (AG°¹ > 0) still occur in a metabolicpathway?By increasing the temperature under physiological conditions.This reaction cannot be used in metabolic pathway reactions.It is linked to a favorable reaction.It is linked to another unfavorable reaction.

Metabolic reactions are the biochemical reactions that are essential for our cells to get energy…

Answered: How can an unfavorable reaction (AG°¹ >…

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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An allosteric enzyme that follows the concerted mechanism has a T/R ratio of 500 in the absence of substrate. Suppose that a mutation reversed the ratio. How would this mutation affect the relation between the rate of the reaction and substrate concentration? The mutant enzyme would behave like an enzyme that obeys Michaelis Menton kinetics. The mutant enzyme would have a smaller vmax There would be no difference in the mutant enzyme in terms of substrate binding and catalysis. More than one answer is correct. The mutant enzyme would display cooperativity more than the wild type. MacBook Air 888 F5 F4 F3 F2 %23 2$ %
Discuss the role of enzymes in metabolic regulation by describing the following five mechanisms.11.1Cascade systems11.2 Futile cycle11.3Cellular compartmentalization 11.4 Covalent modification11.5 Zymogens
In a biochemical pathway, three ATP molecules are hydrolyzed. The endergonic reactions in the pathway require a total of 17.3 kcal/mole of energy to drive the reactions of the pathway. What is the overall change in free energy of the biochemical pathway? Is the overall pathway endergonic or exergonic?
All metabolic pathways must be regulated to maintain homeostasis. The catalytic activity of anenzyme can be controlled allosterically and/or by reversible covalent modification. Provide anexample of each type of regulation (allosteric and reversible covalent modification) in the contextof a metabolic pathway. Be specific, and be sure to explain the rationale behind the regulatorystrategy.
The following reaction coordinate diagram charts the energy of a substrate molecule (S) as it passes through a transition state (X‡) on its way to becoming a stable product (P) alone or in the presence of one of two different enzymes (E1 and E2). How does the addition of either enzyme affect the change in Gibbs free energy (ΔG) for the reaction? Which of the two enzymes binds with greater affinity to the substrate? Which enzyme better stabilizes the transition state? Which enzyme functions as a better catalyst?
When reviewing a Michaelis-Menten Saturation Curve, at first the rate of the reaction is relatively constant, but the rate decreases as the substrate is used up and eventually reaches a plateau. Afte reaching this plateau, what would speed up the reaction again? Adding more substrate Adding heat Adding more enzyme Adding cofactors
Although as a whole, metabolic pathways are thermodynamically favorable, there’s at least onereaction in each pathway that is thermodynamically unfavorable under standard conditions.Provide two different strategies that allow for non-spontaneous reactions to be used as part of anenergy-generating pathway.
A certain metabolic pathway can be diagrammed as: X Y Z A B C D C²D where A, B, C, and D are the metabolic intermediates and X, Y, and Z are the enzymes responsible for each conversion. The physiological free energies for each enzyme catalyzed reaction are: X AG = -0.2 kJ/mol Y AG¹ = -1.3 kJ/mol ZAG' = -12.3 kJ/mol a. Which reaction likely represents a major regulatory point for this pathway? b. If your answer for part a. was, in fact, the case, if an inhibitor of Enzyme Z was present, would the concentrations of metabolites A, B, C, and D be increased, decreased, or not affected? c. Identify which of the enzymes X, Y, and Z, if any, would likely need to be bypassed for the metabolite D to be converted to A.
One way of expressing the rate at which an enzyme can catalyze a reaction is to state its turnover number. The turnover number is the maximum number of substrate molecules that can be acted on by one molecule of enzyme per unit of time. The table gives the turnover number of four representative enzymes. Enzyme Substrate Turnover number (per second) Ribonuclease RNA 100 Fumarase fumarate 800 Lactate dehydrogenase lactate 1000 Urease urea 10,000 How many molecules of urea can one molecule of urease act on in 12.0 min ?
Which of these statements about enzyme-catalyzed reactions is false? The activation energy for the catalyzed reaction is the same as for the uncatalyzed reaction, but the equilibrium constant is more favorable in the enzyme-catalyzed reaction. The Michaelis-Menten constant Km equals the [S] at which V = 1/2 V, max: At saturating levels of substrate, the rate of an enzyme-catalyzed reaction is proportional to the enzyme concentration. The rate of a reaction decreases steadily with time as substrate is depleted. If enough substrate is added, the normal V, of max a reaction can be attained even in the presence of a competitive inhibitor.
For a lot of enzymes that work on fatty acids, the rate determining step is the release of the product from the active site. This means that the activation energy for product release is much higher than the free energy of catalysis. What enthalpic or entropic contributions would make the activation energy for product release so high and explain?
Which of the following statements regarding enzyme catalysis is false? All options are false. Once formed, the transition state slowly proceeds to forming the product at a rate determined by cofactor binding The free energy of binding of the enzyme to the transition state is more favorable than the free energy of binding of the enzyme to the substrate The substrate and active site of the enzyme are solvated to promote enzyme-substrate interaction Once formed, the product dissociates from the enzyme after ATP hydrolysis in order to regenerate the active site

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How can an unfavorable reaction (AG°¹ > 0) still occur in a metabolic pathway? By increasing the temperature under physiological conditions. This reaction cannot be used in metabolic pathway reactions. It is linked to a favorable reaction. It is linked to another unfavorable reaction.