Deck 8: Enzymes: Basic Concepts and Kinetics

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سؤال
A __________________ inhibitor often has a structure similar to the substrate and often reversibly binds to the active site of the enzyme but can be displaced by substrate.
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سؤال
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.
سؤال
What term describes an enzyme without its required cofactor?

A) holoenzyme
B) coenzyme
C) isozyme
D) apoenzyme
E) None of the answers is correct.
سؤال
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.
سؤال
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.
سؤال
A tightly bound cofactor for an enzyme is often called a(n)_____.

A) prosthetic group
B) coenzyme
C) allosteric activator
D) inorganic cofactor
E) None of the answers is correct.
سؤال
When ΔG for a system is zero,the system is at ______________________.
سؤال
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 ________.
سؤال
Compounds that resemble the transition state of a catalyzed reaction and inhibit enzyme activity are called ____________________________.
سؤال
The site on an enzyme where the reaction that is catalyzed by the enzyme occurs is the _____.

A) binding site
B) substrate site
C) allosteric site
D) regulatory site
E) active site
سؤال
Allosteric enzymes can be identified because the plot of initial velocity,V0,versus substrate concentration,S,is not hyperbolic but __________________ -shaped.
سؤال
What type of enzymes often display sigmoidal plots of activity versus substrate concentration?

A) holoenzymes
B) monomeric enzymes
C) allosteric enzymes
D) Michaelis-Menten enzymes
E) isozymes
سؤال
What term describes the substance that is bound by an enzyme and converted to product?

A) inhibitor
B) substrate
C) coenzyme
D) prosthetic group
E) cofactor
سؤال
The straight-line kinetic plot of 1/ V0 versus 1/S is called a ________________________.
سؤال
A reaction can occur spontaneously only if ΔG is __________________.
سؤال
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
سؤال
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.
سؤال
Organic cofactors are referred to as __________________.
سؤال
Enzymes accelerate the rate of a chemical reaction by __________________ the activation energy of the reaction.
سؤال
Most known enzymes are proteins; however,some ___________ molecules have been shown to possess catalytic activity.
سؤال
In many enzyme assays,the natural substrate and product are not used.Why?
سؤال
The formula K'eq = <strong>The formula K'<sub>eq</sub> =   indicates the relationship between</strong> A) the free energy and the equilibrium constant. B) the reaction equilibrium and the isomerization rate. C) the equilibrium constant and standard free energy. D) All of the answers are correct. E) None of the answers is correct. <div style=padding-top: 35px> indicates the relationship between

A) the free energy and the equilibrium constant.
B) the reaction equilibrium and the isomerization rate.
C) the equilibrium constant and standard free energy.
D) All of the answers are correct.
E) None of the answers is correct.
سؤال
Give an example of a reaction catalyzed by a hydrolase.
سؤال
Riboflavin is a water-soluble organic substance that is not synthesized by humans.Metabolically,it is chemically converted into a substance called flavin adenine dinucleotide,which is required by succinate dehydrogenase.Which of the following statements is most correct?

A) Riboflavin is a coenzyme.
B) Flavin adenine dinucleotide is a vitamin.
C) Succinate dehydrogenase is a coenzyme.
D) Flavin adenine dinucleotide is a coenzyme. Succinate dehydrogenase is a vitamin.
سؤال
Multiple substrate enzyme reactions are divided into two classes which are called

A) sequential displacement and double displacement.
B) double displacement and concerted displacement.
C) sequential displacement and concerted displacement.
D) sequential displacement and double as well as sequential displacement and concerted displacement are correct.
E) None of the answers is correct.
سؤال
Which of the following is true?

A) Enzymes force reactions to proceed in only one direction.
B) Enzymes alter the equilibrium of the reaction.
C) Enzymes alter the standard free energy of the reaction.
D) All of the answers are correct.
E) None of the answers is correct.
سؤال
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.
سؤال
Examples of cofactors include

A) Zn2+, Mg2+, and Ni2+.
B) biotin and thiamine pyrophosphate.
C) pyridoxal phosphate and coenzyme A.
D) biotin and thiamine pyrophosphate and pyridoxal phosphate and coenzyme A
E) All of the answers are correct.
سؤال
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.
سؤال
How is the substrate bound to the active site?
سؤال
The Gibbs-free energy of activation is the difference between the

A) substrate and the transition state.
B) substrate and the product.
C) product and the transition state.
D) All of the answers are correct.
E) None of the answers is correct.
سؤال
What type(s)of inhibition can be reversed?

A) competitive
B) noncompetitive
C) mixed
D) All of the answers are correct.
E) None of the answers is correct.
سؤال
The KM is

A) equal to the product concentration at initial reaction conditions.
B) equal to the substrate concentration when the reaction rate is half its maximal value.
C) proportional to the standard free energy.
D) All of the answers are correct.
E) None of the answers is correct.
سؤال
When substrate concentration is much greater than KM,the rate of catalysis is almost equal to

A) Kd.
B) kcat / KM.
C) Vmax.
D) All of the answers are correct.
E) None of the answers is correct.
سؤال
When the kcat / KM ratio is at its upper limit,it is referred to as

A) Circe limits.
B) Michaelis rate.
C) kinetic perfection.
D) All of the answers are correct.
E) None of the answers is correct.
سؤال
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
سؤال
There are six basic categories of enzymes.List the categories,and define the type of reaction.
سؤال
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?
سؤال
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 M?

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.
سؤال
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.
سؤال
In an enzymatic reaction in a test tube,the reaction will eventually reach equilibrium.Why does this not happen in living organisms?
سؤال
How do the intermediate steps in multisubstrate enzyme mechanisms differ?
سؤال
What are transition-state analogs?
سؤال
How are the types of inhibition kinetically distinguishable?
سؤال
.What is the upper limit of kcat / KM?
سؤال
Explain what an abzyme is and give an example.
سؤال
What is the Michaelis-Menten equation? Define all parameters.
سؤال
What is an affinity label?
سؤال
What does Vmax indicate?
سؤال
.Enzyme populations are studied with the use of ensemble methods.How would the data differ from a single-enzyme study?
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ملء الشاشة (f)
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Deck 8: Enzymes: Basic Concepts and Kinetics
1
A __________________ inhibitor often has a structure similar to the substrate and often reversibly binds to the active site of the enzyme but can be displaced by substrate.
competitive
2
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.
D
3
What term describes an enzyme without its required cofactor?

A) holoenzyme
B) coenzyme
C) isozyme
D) apoenzyme
E) None of the answers is correct.
D
4
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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5
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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6
A tightly bound cofactor for an enzyme is often called a(n)_____.

A) prosthetic group
B) coenzyme
C) allosteric activator
D) inorganic cofactor
E) None of the answers is correct.
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7
When ΔG for a system is zero,the system is at ______________________.
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8
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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9
Compounds that resemble the transition state of a catalyzed reaction and inhibit enzyme activity are called ____________________________.
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10
The site on an enzyme where the reaction that is catalyzed by the enzyme occurs is the _____.

A) binding site
B) substrate site
C) allosteric site
D) regulatory site
E) active site
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11
Allosteric enzymes can be identified because the plot of initial velocity,V0,versus substrate concentration,S,is not hyperbolic but __________________ -shaped.
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12
What type of enzymes often display sigmoidal plots of activity versus substrate concentration?

A) holoenzymes
B) monomeric enzymes
C) allosteric enzymes
D) Michaelis-Menten enzymes
E) isozymes
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13
What term describes the substance that is bound by an enzyme and converted to product?

A) inhibitor
B) substrate
C) coenzyme
D) prosthetic group
E) cofactor
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14
The straight-line kinetic plot of 1/ V0 versus 1/S is called a ________________________.
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15
A reaction can occur spontaneously only if ΔG is __________________.
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16
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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17
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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18
Organic cofactors are referred to as __________________.
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19
Enzymes accelerate the rate of a chemical reaction by __________________ the activation energy of the reaction.
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20
Most known enzymes are proteins; however,some ___________ molecules have been shown to possess catalytic activity.
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21
In many enzyme assays,the natural substrate and product are not used.Why?
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22
The formula K'eq = <strong>The formula K'<sub>eq</sub> =   indicates the relationship between</strong> A) the free energy and the equilibrium constant. B) the reaction equilibrium and the isomerization rate. C) the equilibrium constant and standard free energy. D) All of the answers are correct. E) None of the answers is correct. indicates the relationship between

A) the free energy and the equilibrium constant.
B) the reaction equilibrium and the isomerization rate.
C) the equilibrium constant and standard free energy.
D) All of the answers are correct.
E) None of the answers is correct.
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23
Give an example of a reaction catalyzed by a hydrolase.
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24
Riboflavin is a water-soluble organic substance that is not synthesized by humans.Metabolically,it is chemically converted into a substance called flavin adenine dinucleotide,which is required by succinate dehydrogenase.Which of the following statements is most correct?

A) Riboflavin is a coenzyme.
B) Flavin adenine dinucleotide is a vitamin.
C) Succinate dehydrogenase is a coenzyme.
D) Flavin adenine dinucleotide is a coenzyme. Succinate dehydrogenase is a vitamin.
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25
Multiple substrate enzyme reactions are divided into two classes which are called

A) sequential displacement and double displacement.
B) double displacement and concerted displacement.
C) sequential displacement and concerted displacement.
D) sequential displacement and double as well as sequential displacement and concerted displacement are correct.
E) None of the answers is correct.
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26
Which of the following is true?

A) Enzymes force reactions to proceed in only one direction.
B) Enzymes alter the equilibrium of the reaction.
C) Enzymes alter the standard free energy of the reaction.
D) All of the answers are correct.
E) None of the answers is correct.
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27
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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28
Examples of cofactors include

A) Zn2+, Mg2+, and Ni2+.
B) biotin and thiamine pyrophosphate.
C) pyridoxal phosphate and coenzyme A.
D) biotin and thiamine pyrophosphate and pyridoxal phosphate and coenzyme A
E) All of the answers are correct.
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29
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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30
How is the substrate bound to the active site?
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31
The Gibbs-free energy of activation is the difference between the

A) substrate and the transition state.
B) substrate and the product.
C) product and the transition state.
D) All of the answers are correct.
E) None of the answers is correct.
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32
What type(s)of inhibition can be reversed?

A) competitive
B) noncompetitive
C) mixed
D) All of the answers are correct.
E) None of the answers is correct.
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33
The KM is

A) equal to the product concentration at initial reaction conditions.
B) equal to the substrate concentration when the reaction rate is half its maximal value.
C) proportional to the standard free energy.
D) All of the answers are correct.
E) None of the answers is correct.
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34
When substrate concentration is much greater than KM,the rate of catalysis is almost equal to

A) Kd.
B) kcat / KM.
C) Vmax.
D) All of the answers are correct.
E) None of the answers is correct.
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35
When the kcat / KM ratio is at its upper limit,it is referred to as

A) Circe limits.
B) Michaelis rate.
C) kinetic perfection.
D) All of the answers are correct.
E) None of the answers is correct.
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36
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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37
There are six basic categories of enzymes.List the categories,and define the type of reaction.
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38
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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39
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 M?

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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40
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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41
In an enzymatic reaction in a test tube,the reaction will eventually reach equilibrium.Why does this not happen in living organisms?
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42
How do the intermediate steps in multisubstrate enzyme mechanisms differ?
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43
What are transition-state analogs?
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44
How are the types of inhibition kinetically distinguishable?
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45
.What is the upper limit of kcat / KM?
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46
Explain what an abzyme is and give an example.
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47
What is the Michaelis-Menten equation? Define all parameters.
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48
What is an affinity label?
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49
What does Vmax indicate?
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50
.Enzyme populations are studied with the use of ensemble methods.How would the data differ from a single-enzyme study?
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افتح القفل للوصول البطاقات البالغ عددها 50 في هذه المجموعة.