Biological Science (7th Edition)
7th Edition
ISBN: 9780134678320
Author: Scott Freeman, Kim Quillin, Lizabeth Allison, Michael Black, Greg Podgorski, Emily Taylor, Jeff Carmichael
Publisher: PEARSON
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Textbook Question
Chapter 8, Problem 3TYK
How does pH affect enzyme-catalyzed reactions?
a. Protons serve as substrates for most reactions.
b. Energy stored in protons is used to drive endergonic reactions.
c. Proton concentration increases the kinetic energy of the reactants, enabling them to reach their transition state.
d. The concentration of protons affects an enzyme's folded structure and reactivity.
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Students have asked these similar questions
If the environmental temperature gets too high, what will happen to an enzyme and the chemical reaction it catalyzes?
Group of answer choices
A. It will not encounter its substrates often, and the reaction will slow down.
B. It will crystallize, the active site will become inflexible and slow down the reaction.
C. It will denature, lose its shape, and the reaction will not occur.
D. It will become less fluid, and be unable to transport substances easily.
E. It will become more fluid, and speed up the reaction.
What distinguishes a linear metabolic pathway from a cyclic metabolic pathway?
A. The last step of the pathway regenerates a reactant for the first step.
B. The product inhibits an enzyme in the pathway, slowing or stopping the metabolic pathway.
C. A linear pathway runs straight in one direction from reactant to product.
D. Enzymes convert reactants into intermediates before separate enzymes convert intermediates into products.
FoF1 ATPase is the enzyme that catalyzes ATP
synthesis. The enzyme itself is deactivated by ATP.
What mode of enzyme regulation is being
exemplified?
Select the correct response:
Trasncriptional control
Covalent modification
Proteolytic modification
Allosteric regulation
Compartmentation
Chapter 8 Solutions
Biological Science (7th Edition)
Ch. 8 - 2. What is a transition state?
a. the shape...Ch. 8 - 3. How does pH affect enzyme-catalyzed...Ch. 8 - Explain how feedback inhibition regulates...Ch. 8 - 5. Explain the lock-and-key model of enzyme...Ch. 8 - If you were to expose glucose to oxygen on your...Ch. 8 - Using what you have learned about changes in Gibbs...Ch. 8 - Prob. 10TYPSSCh. 8 - 15. The functional form of PAH contains four...
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Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biology and related others by exploring similar questions and additional content below.Similar questions
- Enzymes can be regulated in a many different ways. Covalent modification is one way. Here, the functional groups are attached to or removed from the enzyme. A phosphate group is an example of a functional group that can be added to an enzyme. Depending on the enzyme, addition of a phosphate group can either increase or decrease an enzyme's activity. Evaluate the following names and identify the general name of an enzyme that functions to add phosphate groups to its substrate? A. isomerase B. phosphatase C. kinase D. ligasearrow_forwardEvaluate the following statements concerning enzyme kinetics. Which one of the statements is false? a. Enzyme saturation fluctuates. b. In an uninhibited enzymatic reaction system, adding an excess of substrate will increase the reaction velocity beyond Vmax. c. The Vmax of an enzyme kinetics graph represents the point at which the enzyme is saturated with substrate. d. Non-competitive inhibition of an enzymatic reaction can be overcome by adding more unaltered enzyme. e. The activation energy of a reaction can be reduced by the presence of an enzyme.arrow_forwardExamine the graph showing the rate of reaction versus temperature for an enzyme–catalyzed reaction in a human. a. Describe what is happening to the enzyme at around 40°C. b. Explain why the line touches the x-axis at approximately 20°C and 45°C. c. Average body temperature for humans is 37°C. Suggest a reason why the temperature optimum of this enzyme is greater than 37°C.arrow_forward
- The concept of “induced fit” refers to the fact that: a. enzyme specificity is induced by enzyme-substrate binding. b. enzyme-substrate binding induces an increase in the reaction entropy, thereby catalyzing the reaction. c. enzyme-substrate binding induces movement along the reaction coordinate to the transition state. d. substrate binding may induce a conformational change in the enzyme, which then brings catalytic groups into proper orientation. e. when a substrate binds to an enzyme, the enzyme induces a loss of water (desolvation) from the substrate.arrow_forwardWhich of the following will happen if the concentration of an enzyme increases for a given substrate?? a. the reaction rate increases similarly b. the rate of the reaction decreases to a point. c. there is no change in the reaction. d. the turnover number decreases at the same rate that the enzyme concentration increases. e. the reaction stops.arrow_forwardIndicate whether each of the following statements about an enzyme active site is true or false. a. It is the location where substrate molecules are produced. b. It always has a fixed, rigid geometry. c. It always has a geometrical shape exactly complementary to that of substrate. d. It always accomodates several structurally related substrates. e. It is the location where substrate molecules are converted to product molecules. f. It always has a shape that has a degree of flexibility to it. g. it always accomodates only one specific substrate.arrow_forward
- Enzymes play a fundamental role in cell function. Regarding the biochemistry of enzymes, which of the following statements is correct? A. Enzymes increase the number of molecules that get to the transition state. B. Enzymes increase the rate of a spontaneous reaction by lowering the ΔG. C. Enzymes increase the enthalpy (H) of the products compared to the reactants. D. Most enzymes can bind and react with a wide range of different substrate molecules.arrow_forwardWhich statement defines a coenzyme? a. An enzyme precursor b. A unit consisting of an enzyme bound to reactants plus ATP c. An inactive enzyme that becomes functional upon contact with specific cofactors d. The active part of an enzyme e. An organic molecule closely associated with enzymesarrow_forwardwhat is the first step in an enzyme-catalyzed reaction? a. formation of enzyme-substrate complex b. ionization of enzyme c. dimerizing the substance d. catalysis of enzymearrow_forward
- How does a non-competitive inhibitor decrease the rate of an enzyme reaction? O A. by binding at the active site of the enzyme B. by changing the shape of the active site on the enzyme, without binding to active site O C. by changing the free energy change of the reaction D. by acting as a coenzyme for the reactionarrow_forwardWhich of the following statements concerning enzymes is TRUE? a. Enzymes can increase the equilibrium constant of a reaction by 1000-fold. b. The activity of many enzymes can be regulated. c. Many enzymes are consumed in the reactions they catalyze. d. The rate of enzymatic catalysis is independent of pH.arrow_forwardWhich of the following accurately describes how an enzyme functions? a. reduces the energy content of the products b. allows for the exothermic reaction of materials that are usually endothermic c. changes the reaction mechanism effectively reducing the activation energy d. shifts the equilibrium for the reactionarrow_forward
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