Many reactions in metabolism are thermodynamically unfavorable (ie-the reactionDOES NOT favor the products).1) Explain how these reactions are driven in metabolism.(THIS CAN BE ANSWERED IN ONE SENTENCE CONTAINING APPROX 8-10WORDS!)2) Evolution has selected for a particular molecule to be the "energy currency" oflife.What is that molecule? Briefly describe what makes this molecule the favored"energy currency" over other similar types of molecules.

The thermodynamically unfavorable reaction where ∆G°>0 is driven in metabolism by coupling with…

Answered: Many reactions in metabolism are…

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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Many reactions in metabolism are thermodynamically unfavorable (ie-the reaction DOES NOT favor the products). 1) Explain how these reactions are driven in metabolism. (THIS CAN BE ANSWERED IN ONE SENTENCE CONTAINING APPROX 8-10 WORDS!) I 2) Evolution has selected for a particular molecule to be the "energy currency" of life. What is that molecule? Briefly describe what makes this molecule the favored "energy currency" over other similar types of molecules. Edit View Insert Format Tools Table 12pt ✓ Paragraph BIUA T²
A hypothetical three-step metabolic pathway consists of intermediates W, X, Y, and Z and enzymes A, B, and C. Deduce the order of the enzymatic steps in the pathway from the following information: 1. Compound Q, a metabolic inhibitor of enzyme B, causes Z to build up. 2. A mutant in enzyme C requires Y for growth. 3. An inhibitor of enzyme A causes W, Y, and Z to accumulate. 4. Compound P, a metabolic inhibitor of enzyme C, causes W and Z to build up.
As biological catalysts, enzymes play a fundamental role in many cellular processes. Which of the following statements about enzymes is correct? 1. Enzymes are essential for anabolic pathways; they are not required for catabolic pathways. 2. While an increase in temperature can increase the rate of an uncatalyzed reaction, it can’t increase the rate of an enzyme-catalyzed reaction. 3. Enzymes force substrates into unique conformations that do not occur in the absence of an enzyme. 4. Enzymes decrease the free energy of a reaction’s transition state. A. 1, 2 and 3 B. 1 and 3 C. 2 and 4 D. 4 only E. All of 1, 2, 3 and 4 are correct
Many of the coenzymes we have explored have very complicated structures, yet the chemistry we have discussed typically happens in a very small part of the coenzyme. Why are the coenzymes so complicated? O Nature designed them this way to torture students attempting to understand biochemical reactions. O The structures are probably just evolutionary artifacts. O The structures "shield" the active part of the coenzymes so that they don't catalyze reactions by themselves, without the enzyme. O The complicated structures allow the enzymes that use them to bind the coenzyme in the right place for catalysis.
You know that very high and very low pH values are outside of the normal ranges for life and the biochemistry of life (especially protein catalysts, namely enzymes). This is largely due to the effects of pH on interactions of the backbones of peptide chains, R-group interactions and polypeptide assembly/folding (secondary to quaternary protein structure of polypeptide chains). What do you think will happen to the shape of the active sites in the enzyme at high or low pH?
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?
In the meantime, here's a sneak peak: you will be investigating the enzyme called catalase. Write a paragraph or more to introduce the enzyme catalase. Include the following details in your introduction: • the substrate and products of catalase, • the type of reaction performed by catalase, • factors that could increase or decrease the activity of an enzyme like catalase, • how catalase is used by cells, • in what type of cells is catalase found, • an industrial use of catalase.
Consider a hypothetical metabolic pathway involving four enzymes to convert molecule A into molecule E: Enz, E Enz 1 Enz 2 Enz 3 A 1) A O2) B Which molecule is most likely to be a feedback inhibitor that, when present in high concentrations, will reduce the flow of material through the pathway? 3) C 04) D B 05) E C D 6) none of these The activity of an allosteric enzyme will be greatest when 1) the pH is optimal for the enzyme. 2) most of the enzyme molecules are in the R conformation. 3) most of the enzyme molecules are in the T conformation. 4) there are equal numbers of enzyme molecules in the R and T conformations. puiss What will be the effect on the structure of an allosteric enzyme if a negative allosteric effector is added to a solution of the enzyme? 1) There will be a shift in the equilibrium between the R and T forms; the amount of T will increase. 2) There will be a shift in the equilibrium between the R and T forms; the amount of R will increase. 3) The enzyme will be…
One of the examples that we have used to illustrate the concept of equilibrium is the isomerization of glucose-6-phosphate (G6P) to fructose-6-phosphate (F6P), which is the second step in g ycolysis. Draw a graph to show how the reaction Gibbs energy varies with the fraction fof F6P in solution.Label the regions of the graph that correspond to the formation of F6P and G6P being spontaneous, respectively.
When biological enzymes are heated, they lose their catalytic activity. The change that occurs is an ENDOTHERMIC and SPONTANEOUS process. Based on the given information, what is the sign of Δ˚G? Based on the given information, what is the sign of Δ˚H? Is the structure of the original enzyme MORE or LESS ordered than the new form? Explain your answer.
Which of the following statements about isozymes is correct? (Select all that apply.) (a) Isozymes allow reactions to be optimized under different conditions. (b) The main reason for isozymes is so that a given reaction is never completely inhibited. (c) Isozymes have completely different active sites. (d) Bind the same substrates but form different products. (e) Isozymes display different physical properties, such as kinetic parameters.
What is the molecular logic that makes a pathway with a number of comparatively small energy changes more likely than a single reaction with a large energy change?

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