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 6TYU
If you were to expose glucose to oxygen on your lab bench, whywould you not expect to see it burn as shown in Figure 8.6?
a. The reaction is endergonic and requires an input of energy.
b. The reaction is not spontaneous unless an enzyme is added to the substrates.
c. The sugar must first be phosphorylated to increase its potential energy.
d. Activation energy is required for the sugar and oxygen to reach their transition state.
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Students have asked these similar questions
As you change the temperature from a low temperature to a high temperature what happens to the rate of an enzymatic reaction, in general terms?
A
The reaction rate will steadily increase as the temperature increases.
B
The reaction rate will steadily decrease as the temperature increases.
C
The reaction rate will start low, then increase, and then decrease again as the temperature increases.
D
The reaction rate will not change as the temperature increases.
Based on their roles in the metabolic process, classify the following substances as an oxidizing agent, reducing agent or neither.
a. FADH2
b. ATP
c. NAD+
d. NADH
e. GTP
In order for ATP to effectively deliver energy to an enzyme, the following needs to be the case:
a.
a.
ATP hydrolysis is spatially close to the enzyme’s active site
b.
There must be a separate protein present whose task is ATP hydrolysis
c.
There must be a phosphate acceptor present
d.
ATP must be formed during the reaction
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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- Which of the following statements about folic acid is not true? a. Folic acid is activated by folate synthase. b. Folic acid structure contains a pteridine ring and para-amino benzoic acid. c. NADPH is required in the reactions activating folic acid. d. Tetrahydrofolate is the biologically active derivative of folic acid.arrow_forwardThe reaction catalyzed by glyceraldehyde 3-phosphate dehydrogenase involves two "sub-reactions", one of which is unfavourable. How is the energy barrier of this unfavourable sub reaction overcome? A. through the formation and hydrolysis of a thioester bond using a cysteine molecule in the enzyme B. through the hydrolysis of an ATP molecule C. through the hydrolysis of a thioester bond in the substrate molecule D. the enzyme catalyzes the formation of a thioester bond E. none of these explanations describe how the energy barrier is overcome Please answer asaparrow_forwardYou are studying a biochemical pathway that requires ATP as an energy source. To your dismay, the reactions soon stop, partly because the ATP is rapidly used up and partly because an excess of ADP builds up and inhibits the enzymes involved. You are about to give up when the following table from a biochemistry textbook catches your eye. A. ذن فه B. Substrates C. Creatine + ATP ATP + H₂O Pyrophosphate + H₂O Glucose-6-phosphate + H₂O Enzyme A Enzyme B Enzyme C Enzyme D Products Creatine-phosphate + ADP Which of the following reagents is/are most likely to revitalize your reaction? a vast excess of ATP glucose 6-phosphate and enzyme D creatine phosphate and enzyme A D. pyrophosphate ADP + Phosphate 2 Phosphate Glucose + Phosphate AG (kJ/mol) +3 -7.3 -7.0 -3.3arrow_forward
- Glycogen phosphorylase degrades glycogen by: a. An hydrolysis reaction. b. An oxidation-reduction reaction. c. A phosphorolysis reaction. d. A transferase reactionarrow_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_forwardWhy does the velocity reach a plateau (asymptote) at high substrate concentrations? a. At high substrate concentrations, the product becomes an inhibitor of the reaction that created it. b. At high substrate concentrations, all enzymes are saturated with substrates. c. At high substrate concentrations, all substrates have been converted to products. d. At high substrate concentrations, the product concentration is high and the reaction starts running in reverse.arrow_forward
- As you change the pH from a low pH to a high pH what happens to the rate of an enzymatic reaction, in general terms? A The reaction rate will steadily increase as the pH increases. B The reaction rate will steadily decrease as the pH increases. C The reaction rate will start low, then increase, and then decrease again as the pH increases. D The reaction rate will not change as the pH increases.arrow_forwardChoose only the letter, no explanation needed. Enzyme activity is affected by a variety of factors. What factor causes the enzyme to denature if it becomes extremely high? * Choices: A. Water's Effect B. pH C. Temperature D. Activator's Effect An inhibitor binds to the enzyme's active site, preventing the substrate from binding to it. What conclusions can you make from this situation? * A. No reaction occurred B. Non-competitive inhibition occurred C. Enzyme activity occurred D. Competitive inhibition occurred Each enzyme is very selective when it comes to its substrate. What can you conclude from this statement? * A. Any substrate can bind to the active site. B. Enzymes are used up in the reaction. C. Only a specific substrate can bind to the active site. D. Enzymes break down when not used. Lock : Key :: Active Site : _____________________________ * A. Substrate B. Active Site C. Coenzyme D. Cofactor Enzymes only speed up biological functions, so they are NOT used up in the…arrow_forwardWhich of the following is true about allosteric enzymes? A. Allosteric enzymes are always multimeric. B. Regulatory sites (allosteric sites) on an allosteric enzyme are always different from the catalytic site. C. Allosteric enzymes always change the conformation of the active site in response to binding of an allosteric modulator. D. Suicide inactivators are examples of allosteric modulators.arrow_forward
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