Principles of Biology
2nd Edition
ISBN: 9781259875120
Author: Robert Brooker, Eric P. Widmaier Dr., Linda Graham Dr. Ph.D., Peter Stiling Dr. Ph.D.
Publisher: McGraw-Hill Education
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Textbook Question
Chapter 6.2, Problem 2TYK
An inhibitor raises the Km for an enzyme but has no effect on the Vmax. This inhibitor probably binds to
- the active site.
- an allosteric site.
- the substrate.
- all of the above.
- both a and b.
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Indicate whether each of the following statements about an enzyme active site is true or false.
It is the location where substrate molecules are produced.
It always has a fixed, rigid geometry.
It always has a geometrical shape exactly complementary to that of substrate.
It always accommodates several structurally related substrates.
It is the location where substrate molecules are converted to product molecules.
It always has a shape that has a degree of flexibility to it.
It always accommodates only one specific substrate.
The effect of
on the activity of an enzyme can usually be overcome by increasing the concentration of substrate(s). Choose the best answer
the phosphorylation of the R groups of serine (S), threonine (T) and tyrosine (Y)
an allosteric effector
a noncompetitive inhibitor
a competitive inhibitor
Which of the following is characteristic of competitive inhibitors?
the inhibitor could bind to the active site or to an allosteric site on the enzyme.
the enzyme will mistake the inhibitor for its substrate, so that the inhibitor will
end up covalently bound to the enzyme.
the inhibitor can bind only AFTER the substrate has bound (i.e. it binds only to
the ES complex).
the inhibitor can bind reversibly at the substrate-binding site (the active site).
the inhibitor will lower the characteristic Vmax of the enzyme.
Chapter 6 Solutions
Principles of Biology
Ch. 6.1 - Which do you think has more entropy, an NaCl...Ch. 6.1 - Prob. 1TYKCh. 6.1 - Prob. 2TYKCh. 6.2 - Prob. 1CCCh. 6.2 - Prob. 2CCCh. 6.2 - Prob. 3CCCh. 6.2 - Prob. 1TYKCh. 6.2 - An inhibitor raises the Km for an enzyme but has...Ch. 6.3 - Prob. 1CCCh. 6.3 - Prob. 1TYK
Ch. 6.3 - Prob. 2TYKCh. 6.3 - Prob. 3TYKCh. 6.4 - Prob. 1CCCh. 6.4 - Prob. 1BCCh. 6.4 - Prob. 1TYKCh. 6.4 - Prob. 2TYKCh. 6.4 - Prob. 2CCCh. 6.5 - Prob. 1TYKCh. 6.6 - During the citric acid cycle, what happens to...Ch. 6.7 - Prob. 1CCCh. 6.7 - Prob. 2CCCh. 6.7 - Prob. 3CCCh. 6.7 - Prob. 1TYKCh. 6.7 - Prob. 2TYKCh. 6.7 - Prob. 3TYKCh. 6.8 - Prob. 1CCCh. 6.8 - Prob. 1TYKCh. 6 - According to the second law of thermodynamics....Ch. 6 - Reactions that release free energy are exergonic....Ch. 6 - Prob. 3TYCh. 6 - Prob. 4TYCh. 6 - Prob. 5TYCh. 6 - Prob. 6TYCh. 6 - Prob. 7TYCh. 6 - Prob. 8TYCh. 6 - Prob. 9TYCh. 6 - Prob. 10TYCh. 6 - Describe the mechanism and purpose of feedback...Ch. 6 - What causes the rotation of the y subunit of ATP...Ch. 6 - PRINCIPLES A principle of biology is that living...Ch. 6 - Discuss how life can maintain its order in spite...Ch. 6 - Prob. 2CBQ
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- Competitive inhibitors bind to the active site of the enzyme. None of the answers listed are correct. bind with substrate molecules. change the shape of the enzyme by binding at the allosteric site. O act like the active site and take substrates away from the enzyme.arrow_forwardWhich of the following statements are true about enzyme regulation via noncovalent interactions? Select all that apply. Molecules can cause a change in enzyme shape because they're able to bind to the enzyme somewhere other than the active site The function of an enzyme is altered by a chemical change in its primary structure, which is called phosphorylation Molecules that are similar to the substrate in both size and shape can compete with the substrate for access to the enzyme's active site Molecules that are similar to the substrate in both size and shape can compete with the substrate for access to a location other than the active sitearrow_forwardAn inhibitor was added to an enzyme and the expected rate of the reaction was not detected and the substrate was not utilized at all. This inhibitor is (choose one answer only): Is un-competitive, meaning the inhibitor binds to a site near the active site. Is competitive, meaning the inhibitor binds directly to the same active site as the subtrate. Is non-competitive, meaning the inhibitor binds to site other than the active site as the subtrate. Is irreversible, meaning the inhibitor binds covalently to the enzyme keeping the enzyme inactive permanently.arrow_forward
- All of the following are characteristics of the active site of an enzyme EXCEPT? Select the correct response. It has a complementary shape to its substrate. It is the binding site for many different kinds of molecules. It is found somewhere in the interior of the enzyme. It has less water content compared to the cytoplasm.arrow_forwardClassify the items as competitive or noncompetitive inhibitors for control of enzyme action. Bind to the allosteric site on the enzyme Not influenced by the concentration of substrate Resemble the substrate Do not resemble thhe substrate Bind to active site of the enzymearrow_forwardWhich statement describes enzyme inhibitors? O They bind to the active site of an enzyme and decrease its activity. O They block access to the substrate and slow the rate of the reaction. O They change the shape of an enzyme reducing its ability to bind efficiently. All of the above.arrow_forward
- Which of the following statements regarding enzymes and transition states is true? stabilization of the transition state must be less than stabilization of ES for catalysis to occur binding of substrate to an enzyme often causes strain, thus promoting transition state formation the transition state conformation of an enzyme catalyzed reaction is identical to the conformation seen in the uncatalyzed transition state formation of the transition state always assures that the reaction will proceed to product none of the above are truearrow_forwardAll of the following are characteristics of the active site of an enzyme EXCEPT? It has less water content compared to the cytoplasm. It is found somewhere in the interior of the enzyme. It is the binding site for many different kinds of molecules. It has a complementary shape to its substrate.arrow_forwardA transition-state analog— resembles the active site of general acid-base enzymes. is less stable when binding to an enzyme than the normal substrate. stabilizes the transition state for the normal enzyme-substrate complex. reacts more rapidly with an enzyme than the normal transition state intermediate. resembles the transition-state structure of the normal substrate in the enzyme-substrate complex.arrow_forward
- What does the Km of an enzyme measure? The affinity (strength of binding) of an enzyme for its substrate. The substrate concentration when AG is 0. The point at which activation energy is overcome. The amount of substrate needed to achieve Vmax- When half of the available enzyme is bound by substrate.arrow_forwardThe image shows the rate of an enzyme reaction under conditions of no inhibition, competitive inhibition, and noncompetitive inhibition as reactions labeled uninhibited, A, and B. Which of the following best explains what has occurred in the enzyme reactions? Reaction B shows competitive inhibition, where increased substrate competes with inhibitors for the active site. Reaction A shows noncompetitive inhibition, where increased substrate competes with inhibitors for the active site. Reaction A shows competitive inhibition, where increased substrate does not affect the enzyme’s binding with the inhibitor. Reaction B shows noncompetitive inhibition, where increased substrate does not affect the enzyme’s binding with the inhibitor.arrow_forwardIn the following example an enzyme is being inhibited. This is an example of Active site Inhibitor Altered active site O Non-competitive inhibition O Competitive inhibition MacBook Airarrow_forward
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