Biology - Study Guide
8th Edition
ISBN: 9780321501561
Author: Martha R. Taylor
Publisher: PEARSON EDUCATION (COLLEGE)
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Textbook Question
Chapter 8, Problem 10TYK
What is meant by an induced fit?
- a. The binding of the substrate is an energy-requiring process.
- b. A competitive inhibitor can outcompete the substrate for the active site.
- c. The binding of the substrate changes the shape of the active site, which can stress or bend substrate bonds.
- d. The binding of an activator to an allosteric site induces a more active form of the subunits of an enzyme.
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Students have asked these similar questions
When you heat a solution past the optimum for an enzyme?
A. the active site permanently binds substrate via covalent bonding
B. the enzyme stiffens and slows down
C. the enzyme starts to denature
A) Which substrate A or B had the greater affinity for the enzyme? How did you make your conclusion?
B) Define enzyme competition.
compare the state of an enzyme active site at a low substrate concentration and at a high substrate concentration. How does this affect the rate of the reaction?
Chapter 8 Solutions
Biology - Study Guide
Ch. 8 - Complete the following concept map that summarizes...Ch. 8 - Complete the following table to indicate how the...Ch. 8 - Develop a concept map on free energy and G. The...Ch. 8 - Prob. 4IQCh. 8 - Prob. 5IQCh. 8 - In the following graph of an exergonic reaction...Ch. 8 - In the following diagram of a catalytic cycle,...Ch. 8 - Return to the diagram in Interactive Question 3.7,...Ch. 8 - Both ATP and ADP serve as regulators of enzyme...Ch. 8 - What is the relationship between the concept of...
Ch. 8 - What role do enzymes play in metabolism?Ch. 8 - ________ the totality of an organisms chemical...Ch. 8 - _______ pathways that use energy to synthesize...Ch. 8 - Prob. 3TYKFCh. 8 - _______ the most random form of energyCh. 8 - _______ term for the measure of disorder or...Ch. 8 - Prob. 6TYKFCh. 8 - _______ inhibitors that decrease an enzymes...Ch. 8 - Prob. 8TYKFCh. 8 - Prob. 9TYKFCh. 8 - Prob. 10TYKFCh. 8 - Catabolic and anabolic pathways are often coupled...Ch. 8 - Which statement most closely reflects the first...Ch. 8 - When a cell breaks down glucose, only about 34% of...Ch. 8 - Prob. 4TYKCh. 8 - Prob. 5TYKCh. 8 - Prob. 6TYKCh. 8 - One way in which a cell maintains metabolic...Ch. 8 - Prob. 8TYKCh. 8 - Prob. 9TYKCh. 8 - What is meant by an induced fit? a. The binding of...Ch. 8 - In an experiment, changing the pH from 7 to 6...Ch. 8 - Prob. 12TYKCh. 8 - Penicillin binds to the active site of an enzyme...Ch. 8 - Prob. 14TYKCh. 8 - Prob. 15TYKCh. 8 - Which line in the diagram indicates the G of the...Ch. 8 - Prob. 17TYKCh. 8 - Prob. 18TYKCh. 8 - Prob. 19TYKCh. 8 - Prob. 20TYK
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- Which statement describes a competitive inhibitor? a. A competitive inhibitor has a structure similar to that of the substrate. b. A competitive inhibitor distorts the shape of the enzyme. c. The addition of more substrate does not reverse the inhibition. d. Both a and c describe a competitive inhibitor.arrow_forwardDifferentiate the concerted model and sequential model by illustrating the difference in terms of R and T forms of the enzyme when a substrate is about to bind. Write a shortdescription for each.arrow_forwardIn general, how would an increase in substrate alter enzyme activity? Draw a graph to illustrate this relationship.arrow_forward
- Why does the substrate bind to the enzyme? 1. The shape of the active site fits the shape of the substrate 2. None are true 3. The shape of the reaction site fits the shape of the substrate 4. The shape of the allosteric site fits the shape of the substratearrow_forwardPlease answer clearly and directlyAn enzyme that works best at pH 2 and temperature 35-39°C was dissolved in water then boiled. Afterwards, the substrate was added. After a while, no reaction occurred and the substrate wasn't converted to products. Explain why the result was negative assuming that the enzyme is correct for the substratearrow_forward1a.Sketch a graph that shows an enzyme that functions at an optional pH of b. which organ of the body does it likely to work at? 2. On the same graph from la, sketch another line/curve that shows what happen to the enzyme activity (in #1a) if a constant [ ] of inhibitors is added.arrow_forward
- Which statement is/are TRUE about inhibitors? A. Mode of action of penicillin on bacteria is an example of irreversible inhibition. B. Increasing the substrate concentration does not affect competitive inhibitors C. Uncompetitive inhibitors bind only to the enzyme-substrate complex D. In the Lineweaver-Burke plot, the lines for enzymes in the presence and absence of noncompetitive inhibitor have different x-intercepts.arrow_forwardWhat is the reason why the transition state of a catalyzed reaction is lower has lower energy compared to an uncatalyzed reaction? A. because enzymes only work at low temperatures B. because of favorable interactions with the substrate C. because of enthalpic interactions between the enzyme and the transition state D. A and Barrow_forwardWhat is the function of the active site of an enzyme? a. Involved in the catalytic reaction of the enzyme b. Inhibit the enzymatic activity c. Binding of regulators d. Binding of products after the reactionarrow_forward
- Research the enzyme Caspase-2 Indicate i) the class of enzymes to which it belongs to, ii) name the kind of bond that is modified due to its activity, iii) indicate the substrate that is recognised by the enzyme using the amino acid three letter code and iv) whether the enzyme displays high or low substrate specificity.arrow_forwarddraw the enzyme binding pocket and active site draw the curved arrows showing the reaction proceeding toward the products show how the enzyme facilitates the reaction write a description of how the enzyme works Propose a name for the enzyme based on the rules from classarrow_forwardExplain the mechanism by whicha single substrate reaction catalyzed by an enzyme with a single binding site for the substrate is able to exhibit sigmoidal kinetics.arrow_forward
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