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What conclusion can be drawn concerning an inhibitor if the Vmax is the same in the presence and absence of the inhibitor?


A) The inhibitor binds to the substrate.
B) The inhibitor can be overcome with sufficiently high concentrations of substrate.
C) The inhibitor reacts with a critical residue of the enzyme.
D) The inhibitor binds to the same active site as the substrate.
E) The KM is smaller in the presence of inhibitor.

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The Circe effect enhances what aspect of enzyme catalysis?


A) catalysis of substrate to product
B) binding of substrate
C) removal of product(s) from active site
D) prevention of enzyme inhibition
E) None of the answers is correct.

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The kcat is often referred to as the _____.


A) turnover number
B) Michaelis constant
C) dissociation constant
D) rate constant
E) None of the answers is correct.

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Give an example of a reaction catalyzed by a hydrolase.

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Hydrolases catalyze a reaction where a w...

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There are six basic categories of enzymes. List the categories, and define the type of reaction.

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The categories include oxidoreductases (...

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What term describes an enzyme without its required cofactor?


A) holoenzyme
B) coenzyme
C) isozyme
D) apoenzyme
E) None of the answers is correct.

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D

In this type of inhibition, the inhibitor can only bind to the ES complex to form an ESI complex.


A) competitive
B) noncompetitive
C) mixed
D) uncompetitive
E) None of the answers is correct.

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Compounds that resemble the transition state of a catalyzed reaction and inhibit enzyme activity are called ____________________________.

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transition...

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In many enzyme assays, the natural substrate and product are not used. Why?

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Many products are difficult to measure a...

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Explain what an abzyme is and give an example.

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Catalytic antibodies are abzymes and are...

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A(n) _____ requires an input of energy to proceed.


A) reaction at equilibrium
B) irreversible reaction
C) spontaneous reaction
D) exergonic reaction
E) endergonic reaction

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Five KM values are given for the binding of substrates to a particular enzyme. Which has the strongest affinity when k 1 is greater than k2?


A) 150 mM
B) 0.15 mM
C) 150 μ\mu M
D) 1.5 nM
E) 15000 pM

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If a reaction is exergonic at specific reactant concentrations, it is considered _____.


A) at equilibrium
B) nonspontaneous
C) spontaneous
D) irreversible
E) None of the answers is correct.

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What is the common strategy by which catalysis occurs?


A) increasing the probability of product formation
B) shifting the reaction equilibrium
C) stabilization of transition state
D) All of the answers are correct.
E) None of the answers is correct.

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Most known enzymes are proteins; however, some ___________ molecules have been shown to possess catalytic activity.

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The difference between the standard-state free energy, ΔGº, and the biochemical standard-state free energy is that ΔGº′ refers to the standard free-energy change at ________.

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pH 7

What is an affinity label?

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This is a substrate analog that is structurally similar to the substrate, binds to the active site, and chemically reacts with a residue in the active site. It is used to study enzyme structure and mechanism.

You believe a substrate fits rigidly into a cleft like a key into a lock, but your roommate believes that the structure of the enzyme adapts to the substrate. Who is right?

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You are both partially correct. Like a l...

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What term is used to describe the dynamic recognition of the substrate when binding to an enzyme occurs?


A) allosteric modulation
B) transition state enhancement
C) sequential binding
D) induced fit
E) None of the answers is correct.

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Which of the following is true under the following conditions: the enzyme concentration is 5 nM, the substrate concentration is 5 mM, and the KM is 5 μ\mu 0M?


A) The enzyme is saturated with substrate.
B) Most of the enzyme does not have substrate bound.
C) There is more enzyme than substrate.
D) All of the answers are correct.
E) None of the answers is correct.

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