Deck 14: Enzyme and Rate Analyses

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Question
During embryonic and fetal development,changes in isoenzyme distribution patterns are common.These changes are thought to result from:

A) mutation-driven gene expression that reoccurs in adult malignancies.
B) altered production due to a genetic defect.
C) increased production and secretion from all undifferentiated proliferating cells.
D) differential expression and changes in the relative activities of gene loci within developing cells.
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Question
Regarding enzyme kinetics,the Michaelis-Menten plot of the relationship between reaction velocity and substrate concentration is correctly expressed as which one of the following formulae?

A). v = Vmax[S]/Km + [S]
B). v = Km[S]/Vmax + [S]
C) .v = Vmax + [S]/Km[S]
D). v = Km + [S]/Vmax[S]
Question
Regarding measurement of a property related to substrate concentration such as fluorescence production,the assay that,although more technically demanding,theoretically provides the most accurate measurement of enzyme activity is the:

A) fixed-time assay.
B) equilibrium method.
C) discontinuous-monitoring assay.
D) two-point kinetic method.
Question
An example of a posttranslational modification of an enzyme that produces an enzyme isoform would be:

A) association of different types of subunits in various combinations in an oligomer.
B) modification of genes at different loci.
C) alteration of carbohydrate side chains.
D) the existence of different allelic genes.
Question
True isoenzymes,which are multiple forms of an enzyme that possesses the ability to catalyze an enzyme's characteristic reaction,are formed by:

A) alteration of a carbohydrate side chain.
B) the existence of more than one gene locus coding for the structure of the enzyme protein.
C) association with other proteins and cofactors.
D) changes in the phosphorylation pattern of associated proteins.
Question
How does pH alter an enzymatic reaction rate?

A) By affecting key amino acids in the enzyme protein at the active center and other sites
B) By causing thermal inactivation through reconfiguration of the prosthetic group
C) By promoting the formation of the most active state of the enzyme
D) By decreasing the Km needed for maximum velocity to be reached
Question
When a coenzyme binds to an enzyme,the enzyme portion of the resulting molecule is referred to as the:

A) activator.
B) holoenzyme.
C) apoenzyme.
D) prosthetic group.
Question
Regarding enzyme kinetics,the substrate concentration at which the reaction velocity is equal to 0.5 Vmax is referred to as:

A) Km.
B) Vmax association constant.
C) 1/v.
D) first order concentration.
Question
Zero-order kinetics occurs during the beginning of an enzyme-catalyzed reaction when a substrate concentration is high and the rate of the reaction is _____ on the _____ concentration.

A) dependent; substrate
B) dependent; coenzyme
C) independent; substrate
D) independent; enzyme
Question
In the reciprocal plot pictured below,the solid line indicates a normal enzyme reaction with no inhibition,and the dotted line indicates a decrease in Vmax and no change in Km.This plot is an example of which type of inhibition?

A) Competitive
B) Noncompetitive
C) Uncompetitive
D) The type of inhibition cannot be determined with this information.
Question
When determining the activity of an enzyme in serum as in a bisubstrate reaction,measurement of two different substances can be made.One measurement determines the decrease in substrate concentration acted upon by the enzyme and the other:

A) analyzes the disappearance of enzyme used in the reaction.
B) measures the increase in the concentration of a second substrate.
C) measures the increase in the concentration of the second product formed.
D) measures the amount of enzyme/substrate complex formed.
Question
In a continuous-monitoring assessment of an enzyme reaction rate,which one of the following is the preferable measurement?

A) Measurement of the decreasing concentration of substrate
B) Measurement of the increasing concentration of product
C) Direct measurement of enzyme protein
D) Calculation of Km and Vmax
Question
The reciprocal plot pictured below indicates a decrease in Vmax and a decrease in Km.The solid line indicates a normal enzymatic reaction.What type of enzymatic inhibition is this?

A) Competitive
B) Noncompetitive
C) Uncompetitive
D) The type of inhibition cannot be determined with this information.
Question
Any condition,such as extreme temperature or extremes of pH,which changes the shape of the enzyme protein structure generally causes loss of enzymatic activity.This is referred to as:

A) activation.
B) inhibition.
C) denaturation.
D) optimization.
Question
In regard to factors that govern the rate of an enzymatic reaction,first-order reaction kinetics occur at that part of the reaction during which the rate of the reaction is:

A) directly proportional to the substrate concentration.
B) proportional to the concentration of the enzyme present.
C) independent of either the enzyme or substrate concentration.
D) dependent upon the pH and temperature of the system.
Question
Activators increase the rates of enzyme-catalyzed reactions.In some cases,these activators interact with the nonenzymatic component of the reaction such as the substrate.However,in most cases the activator:

A) acts as an uncompetitive inhibitor by binding to the product.
B) binds to the enzyme similar to the enzyme/substrate combination.
C) alters the enzyme's chemical properties to produce an altered product.
D) destroys enzyme activity by denaturing the protein.
Question
Immobilized enzymes are used analytically in various electrochemical techniques.The use of an ion-selective electrode that is coated with an enzyme that produces ions when placed in a substrate solution is a type of:

A) potentiometric measurement.
B) immunoassay.
C) equilibrium method.
D) consecutive enzymatic reaction.
Question
In regard to the expression of enzyme activity,a katal is:

A) a unit that describes the amount of substrate in moles converted to product in 1 minute.
B) a unit that describes the amount of enzyme that is consumed in 1 minute.
C) a unit that describes the amount of enzyme that will catalyze a mole of substrate in 1 second.
D) the substrate concentration at which the enzyme yields half the maximum velocity of the reaction.
Question
Statin drugs lower cholesterol by competitive inhibition of the cholesterol-synthesizing enzyme HMG-CoA reductase.A competitive inhibitor binds:

A) the enzyme at a site other than the active center,thereby decreasing the Vmax of the reaction.
B) to the active center of the enzyme,with no effect on the Vmax of the reaction.
C) to the entire enzyme-substrate complex,thereby decreasing the Km.
D) to the active center of the enzyme,thereby causing the Km to increase.
Question
Which one of the following is a correct statement describing a property of an enzyme?

A) Enzyme activity is not altered by heat denaturation.
B) Enzymes affect the rate of a chemical reaction by being altered to fit into the active site of a substrate.
C) Enzymes are protein catalysts that decrease the activation energy of a chemical reaction.
D) Enzymes contain a site to which the product binds during an enzymatic reaction.
Question
Varying different factors and studying their effects on an enzymatic reaction rate in the assessment of most favorable reaction conditions for an enzyme assay is referred to as:

A) optimization.
B) standardization.
C) quality control.
D) variable control.
Question
All enzymes are classified to one of six classes based on the reaction they catalyze.Based on this classification,creatine kinase is a member of which one of the following enzyme classes?

A) Hydrolase
B) Oxidoreductase
C) Ligase
D) Transferase
Question
The use of several enzymatic reactions linked together to provide a means of measuring the activity of the first enzyme or the concentration of the initial substrate is referred to as a(n):

A) equilibrium reaction.
B) consecutive enzymatic reaction.
C) self-indicating reaction.
D) enzyme immunoassay.
Question
The interaction of the amino acid side chains with the arrangement of the α\alpha -helices and β\beta -sheets to form a three-dimensional protein structure is called the _____ structure of the protein.

A) primary
B) secondary
C) tertiary
D) quaternary
Question
In an enzyme immunoassay such as ELISA,the specificity of the labeled enzyme is the most important aspect of the measurement.
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Deck 14: Enzyme and Rate Analyses
1
During embryonic and fetal development,changes in isoenzyme distribution patterns are common.These changes are thought to result from:

A) mutation-driven gene expression that reoccurs in adult malignancies.
B) altered production due to a genetic defect.
C) increased production and secretion from all undifferentiated proliferating cells.
D) differential expression and changes in the relative activities of gene loci within developing cells.
differential expression and changes in the relative activities of gene loci within developing cells.
2
Regarding enzyme kinetics,the Michaelis-Menten plot of the relationship between reaction velocity and substrate concentration is correctly expressed as which one of the following formulae?

A). v = Vmax[S]/Km + [S]
B). v = Km[S]/Vmax + [S]
C) .v = Vmax + [S]/Km[S]
D). v = Km + [S]/Vmax[S]
. v = Vmax[S]/Km + [S]
3
Regarding measurement of a property related to substrate concentration such as fluorescence production,the assay that,although more technically demanding,theoretically provides the most accurate measurement of enzyme activity is the:

A) fixed-time assay.
B) equilibrium method.
C) discontinuous-monitoring assay.
D) two-point kinetic method.
two-point kinetic method.
4
An example of a posttranslational modification of an enzyme that produces an enzyme isoform would be:

A) association of different types of subunits in various combinations in an oligomer.
B) modification of genes at different loci.
C) alteration of carbohydrate side chains.
D) the existence of different allelic genes.
Unlock Deck
Unlock for access to all 25 flashcards in this deck.
Unlock Deck
k this deck
5
True isoenzymes,which are multiple forms of an enzyme that possesses the ability to catalyze an enzyme's characteristic reaction,are formed by:

A) alteration of a carbohydrate side chain.
B) the existence of more than one gene locus coding for the structure of the enzyme protein.
C) association with other proteins and cofactors.
D) changes in the phosphorylation pattern of associated proteins.
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Unlock for access to all 25 flashcards in this deck.
Unlock Deck
k this deck
6
How does pH alter an enzymatic reaction rate?

A) By affecting key amino acids in the enzyme protein at the active center and other sites
B) By causing thermal inactivation through reconfiguration of the prosthetic group
C) By promoting the formation of the most active state of the enzyme
D) By decreasing the Km needed for maximum velocity to be reached
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Unlock for access to all 25 flashcards in this deck.
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k this deck
7
When a coenzyme binds to an enzyme,the enzyme portion of the resulting molecule is referred to as the:

A) activator.
B) holoenzyme.
C) apoenzyme.
D) prosthetic group.
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Unlock for access to all 25 flashcards in this deck.
Unlock Deck
k this deck
8
Regarding enzyme kinetics,the substrate concentration at which the reaction velocity is equal to 0.5 Vmax is referred to as:

A) Km.
B) Vmax association constant.
C) 1/v.
D) first order concentration.
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Unlock for access to all 25 flashcards in this deck.
Unlock Deck
k this deck
9
Zero-order kinetics occurs during the beginning of an enzyme-catalyzed reaction when a substrate concentration is high and the rate of the reaction is _____ on the _____ concentration.

A) dependent; substrate
B) dependent; coenzyme
C) independent; substrate
D) independent; enzyme
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Unlock for access to all 25 flashcards in this deck.
Unlock Deck
k this deck
10
In the reciprocal plot pictured below,the solid line indicates a normal enzyme reaction with no inhibition,and the dotted line indicates a decrease in Vmax and no change in Km.This plot is an example of which type of inhibition?

A) Competitive
B) Noncompetitive
C) Uncompetitive
D) The type of inhibition cannot be determined with this information.
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Unlock for access to all 25 flashcards in this deck.
Unlock Deck
k this deck
11
When determining the activity of an enzyme in serum as in a bisubstrate reaction,measurement of two different substances can be made.One measurement determines the decrease in substrate concentration acted upon by the enzyme and the other:

A) analyzes the disappearance of enzyme used in the reaction.
B) measures the increase in the concentration of a second substrate.
C) measures the increase in the concentration of the second product formed.
D) measures the amount of enzyme/substrate complex formed.
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Unlock for access to all 25 flashcards in this deck.
Unlock Deck
k this deck
12
In a continuous-monitoring assessment of an enzyme reaction rate,which one of the following is the preferable measurement?

A) Measurement of the decreasing concentration of substrate
B) Measurement of the increasing concentration of product
C) Direct measurement of enzyme protein
D) Calculation of Km and Vmax
Unlock Deck
Unlock for access to all 25 flashcards in this deck.
Unlock Deck
k this deck
13
The reciprocal plot pictured below indicates a decrease in Vmax and a decrease in Km.The solid line indicates a normal enzymatic reaction.What type of enzymatic inhibition is this?

A) Competitive
B) Noncompetitive
C) Uncompetitive
D) The type of inhibition cannot be determined with this information.
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Unlock for access to all 25 flashcards in this deck.
Unlock Deck
k this deck
14
Any condition,such as extreme temperature or extremes of pH,which changes the shape of the enzyme protein structure generally causes loss of enzymatic activity.This is referred to as:

A) activation.
B) inhibition.
C) denaturation.
D) optimization.
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Unlock for access to all 25 flashcards in this deck.
Unlock Deck
k this deck
15
In regard to factors that govern the rate of an enzymatic reaction,first-order reaction kinetics occur at that part of the reaction during which the rate of the reaction is:

A) directly proportional to the substrate concentration.
B) proportional to the concentration of the enzyme present.
C) independent of either the enzyme or substrate concentration.
D) dependent upon the pH and temperature of the system.
Unlock Deck
Unlock for access to all 25 flashcards in this deck.
Unlock Deck
k this deck
16
Activators increase the rates of enzyme-catalyzed reactions.In some cases,these activators interact with the nonenzymatic component of the reaction such as the substrate.However,in most cases the activator:

A) acts as an uncompetitive inhibitor by binding to the product.
B) binds to the enzyme similar to the enzyme/substrate combination.
C) alters the enzyme's chemical properties to produce an altered product.
D) destroys enzyme activity by denaturing the protein.
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Unlock for access to all 25 flashcards in this deck.
Unlock Deck
k this deck
17
Immobilized enzymes are used analytically in various electrochemical techniques.The use of an ion-selective electrode that is coated with an enzyme that produces ions when placed in a substrate solution is a type of:

A) potentiometric measurement.
B) immunoassay.
C) equilibrium method.
D) consecutive enzymatic reaction.
Unlock Deck
Unlock for access to all 25 flashcards in this deck.
Unlock Deck
k this deck
18
In regard to the expression of enzyme activity,a katal is:

A) a unit that describes the amount of substrate in moles converted to product in 1 minute.
B) a unit that describes the amount of enzyme that is consumed in 1 minute.
C) a unit that describes the amount of enzyme that will catalyze a mole of substrate in 1 second.
D) the substrate concentration at which the enzyme yields half the maximum velocity of the reaction.
Unlock Deck
Unlock for access to all 25 flashcards in this deck.
Unlock Deck
k this deck
19
Statin drugs lower cholesterol by competitive inhibition of the cholesterol-synthesizing enzyme HMG-CoA reductase.A competitive inhibitor binds:

A) the enzyme at a site other than the active center,thereby decreasing the Vmax of the reaction.
B) to the active center of the enzyme,with no effect on the Vmax of the reaction.
C) to the entire enzyme-substrate complex,thereby decreasing the Km.
D) to the active center of the enzyme,thereby causing the Km to increase.
Unlock Deck
Unlock for access to all 25 flashcards in this deck.
Unlock Deck
k this deck
20
Which one of the following is a correct statement describing a property of an enzyme?

A) Enzyme activity is not altered by heat denaturation.
B) Enzymes affect the rate of a chemical reaction by being altered to fit into the active site of a substrate.
C) Enzymes are protein catalysts that decrease the activation energy of a chemical reaction.
D) Enzymes contain a site to which the product binds during an enzymatic reaction.
Unlock Deck
Unlock for access to all 25 flashcards in this deck.
Unlock Deck
k this deck
21
Varying different factors and studying their effects on an enzymatic reaction rate in the assessment of most favorable reaction conditions for an enzyme assay is referred to as:

A) optimization.
B) standardization.
C) quality control.
D) variable control.
Unlock Deck
Unlock for access to all 25 flashcards in this deck.
Unlock Deck
k this deck
22
All enzymes are classified to one of six classes based on the reaction they catalyze.Based on this classification,creatine kinase is a member of which one of the following enzyme classes?

A) Hydrolase
B) Oxidoreductase
C) Ligase
D) Transferase
Unlock Deck
Unlock for access to all 25 flashcards in this deck.
Unlock Deck
k this deck
23
The use of several enzymatic reactions linked together to provide a means of measuring the activity of the first enzyme or the concentration of the initial substrate is referred to as a(n):

A) equilibrium reaction.
B) consecutive enzymatic reaction.
C) self-indicating reaction.
D) enzyme immunoassay.
Unlock Deck
Unlock for access to all 25 flashcards in this deck.
Unlock Deck
k this deck
24
The interaction of the amino acid side chains with the arrangement of the α\alpha -helices and β\beta -sheets to form a three-dimensional protein structure is called the _____ structure of the protein.

A) primary
B) secondary
C) tertiary
D) quaternary
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Unlock for access to all 25 flashcards in this deck.
Unlock Deck
k this deck
25
In an enzyme immunoassay such as ELISA,the specificity of the labeled enzyme is the most important aspect of the measurement.
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Unlock Deck
k this deck
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Unlock for access to all 25 flashcards in this deck.