Biology (MindTap Course List)
11th Edition
ISBN: 9781337392938
Author: Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg
Publisher: Cengage Learning
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Textbook Question
Chapter 7, Problem 11TYU
PREDICT In the following reaction series, which enzyme(s) is/are most likely to have an allosteric site to which the end product E binds? (a) enzyme 1 (b) enzyme 2 (c) enzyme 3 (d) enzyme 4 (e) enzymes 3 and 4
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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?
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Is the structure of the original enzyme MORE or LESS ordered than the new form? Explain your answer.
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?
Rearrange the following terms to show the process of enzymatic reaction.
Use
and + to complete the equation.
enzyme enzyme-substrate complex
enzyme
product
substrate
Several important things should be noted about this reaction:
1. A/an
because of the fit between their structures;
2. As a result, something happens to the
example, it might be split in two at a particular location.
3. Then the
and
4. The enzyme is
again.
5. Note that the arrows in the formula for enzyme reaction point
acts on a specific
to form a/an
molecule. For
comes apart, yielding the
in the reaction and is now free to react
_- This means that the reaction is
6. An enzyme-substrate complex can simply go back to the
the
7. The products of an enzymatic reaction can react with the enzyme to
form the
and
again;
8. It, in turn, may again form the
9. Therefore, the same.
and the
may act to cause a
to go either
way.
Chapter 7 Solutions
Biology (MindTap Course List)
Ch. 7.1 - Define energy, emphasizing how it is related to...Ch. 7.1 - Use examples to contrast potential energy and...Ch. 7.1 - Prob. 1CCh. 7.2 - Prob. 3LOCh. 7.2 - Prob. 1CCh. 7.2 - Life is sometimes described as a constant struggle...Ch. 7.3 - Prob. 4LOCh. 7.3 - Prob. 5LOCh. 7.3 - Prob. 6LOCh. 7.3 - Prob. 1C
Ch. 7.3 - Prob. 2CCh. 7.4 - Explain how the chemical structure of ATP allows...Ch. 7.4 - Prob. 1CCh. 7.4 - Prob. 2CCh. 7.5 - Relate the transfer of electrons (or hydrogen...Ch. 7.5 - PREDICT Which has the most energy, the oxidized...Ch. 7.6 - Explain how an enzyme lowers the required energy...Ch. 7.6 - Describe specific ways enzymes are regulated.Ch. 7.6 - Prob. 1CCh. 7.6 - How does the function of the active site of an...Ch. 7.6 - How are temperature and pH optima of an enzyme...Ch. 7.6 - Prob. 4CCh. 7 - Which of the following can do work in a cell? (a)...Ch. 7 - Prob. 2TYUCh. 7 - Prob. 3TYUCh. 7 - Test Your Understanding 4. Diffusion is an (a)...Ch. 7 - Prob. 5TYUCh. 7 - Prob. 6TYUCh. 7 - Prob. 7TYUCh. 7 - Test Your Understanding 8. Induced fit means that...Ch. 7 - Prob. 9TYUCh. 7 - Prob. 10TYUCh. 7 - PREDICT In the following reaction series, which...Ch. 7 - Test Your Understanding 12. EVOLUTION link All...Ch. 7 - EVOLUTION LINK Some have argued that evolution is...Ch. 7 - Prob. 14TYUCh. 7 - Prob. 15TYUCh. 7 - Prob. 16TYU
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- The total concentration of enzyme in a reaction, [E], is made up of the concentration of enzyme bound to substrate, [ES], and the concentration of enzyme still free in solution, [Ef]. Similarly, the total amount of substrate is made up of [Sf] and [ES]. We can assume that the concentration of enzyme is much less than that of the substrate, [E] << [S] Explain why [S] >> [ES] Hence explain why [Sf] ~ [S]arrow_forwardExplain how the observation that reaction (B) runs faster than reaction (A) is related to the enzyme catalysis.arrow_forwardYou are working on an enzyme that obeys standard Michaelis-Menten kinetics. What variable is the V, dependant on if the concentration of the substrate is substantially higher than the concentration of the enzyme? [S] [E] [ES] O [P] O not enough information providedarrow_forward
- To calculate the turnover number (kcat) of an enzyme, you need to know: O A) the enzyme concentration ○ B) the initial velocity of the catalyzed reaction at [S] >> Km ○ C) the initial velocity of the catalyzed reaction at [S] O D) A, B and C O E) A and B, but not Carrow_forwardThe total concentration of enzyme in a reaction, [E], is made up of the concentration of enzyme bound to substrate, [ES], and the concentration of enzyme still free in solution, [Ef]. Similarly, the total amount of substrate is made up of [Sf] and [ES]. We can assume that the concentration of enzyme is much less than that of the substrate, [E] << [S]. Assuming the steady state condition and the relationships between [E], [Ef] and [ES], and similar ones for S, given in lectures, derive an expression for the saturation factor, , in terms of [S] and . (Note that [E] and [S] denote the total amounts of enzyme and substrate added to the reaction, respectively. You may assume that [S]>>[E].)arrow_forwardPlease label (a) from (b)arrow_forward
- Consider two enzymes catalyzing two reactions (A --> B --> C ) in a metabolic cascade with their properties summarized below: Keg (for reaction) Enzyme Reaction KM Kcat / KM 102 M-1s-1 108 M-1s-1 1 A --> B 1 1 mM 2 B --> C 10 10 mM Initial concentrations are [A] = 0.1 mM and [B] = [C] = 0 and both enzymes are present at concentrations of 1 mM. After waiting for 1 ms, the concentrations of A, B, and C are measured. How do you expect the concentrations to be ordered? O [B] > [A] > [C] O [C] > [B] > [A] O [A] > [B] > [C] O [A] > [C] > [B] [C] > [A] > [B]arrow_forwardIn enzyme kinetics, for the reversible with two central complexes mechanism, please provide complete proof that the rate equation is the equation below. The variables denoted with f indicate forward direction while the variables denoted with b indicate backward direction.arrow_forwardYou have obtained experimental kinetic data for two versions of the same enzyme, a wild‑type and a mutant differing from the wild‑type at a single amino acid. The data are given in the table. Compare the kinetic parameters of the two versions using the data in the table. Assuming a two-step reaction scheme in which ?−1 is much larger than ?2, which of the following statements are correct? The mutant version has a higher affinity for the substrate. The wild‑type version requires a greater concentration of substrate to achieve ?maxVmax. The wild‑type version has a higher affinity for the substrate. The mutant version requires a greater concentration of substrate to achieve ?maxVmax. Calculate the initial velocity of the reaction catalyzed by the wild‑type enzyme when the substrate concentration is 10 mM. The reaction equilibrium is reached once there is no net change in the concentration of the substrate or the product. Based on the data table and your initial…arrow_forward
- (i) Which graph indicates an enzymatic reaction without inhibitor?(ii) Which type of inhibitor is it? Briefly explain.(iii) Which graph indicates the highest concentration of inhibitor?(iv) Calculate the Vmax and Km of the graph showing an enzymatic reaction with the lowest concentration of inhibitor. Show the steps of calculation and unit in your answers. Keep 2 decimal places in your answers.arrow_forwardA certain metabolic pathway can be diagrammed as (see pic1), where A, B, C, and D are the intermediates, and X, Y, and Z are the enzymes that catalyze the reactions. The physiological free energy changes for the reactions are (see pic.2). Solve, (a) Which reaction is likely to be a major regulatory point for the pathway? (b) If your answer in Part a was in fact the case, in the presence of an inhibitor that blocks the activity of enzyme Z, would the concentrations of A, B, C, and D increase, decrease, or not be aff ected?arrow_forwardWhat general kinds of reactions do the following types of enzymes catalyze?(a) Kinases (b) Isomerases(c) Synthetasesarrow_forward
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