Deck 20: Enzymes and Vitamins

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Question
In the induced-fit model of enzyme action, the enzyme active site

A)stays the same shape during substrate binding.
B)adjusts shape to adapt to the shape of the substrate.
C)stays the same shape while causing a change in the shape of the substrate.
D)uses an inhibitor to adjust its shape for the substrate.
E)uses a cofactor to change the shape of a substrate.
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Question
To what main class of enzymes does the enzyme that catalyzes the conversion of lactose to galactose and glucose belong?

A)oxidoreductase
B)transferase
C)hydrolase
D)lyase
E)isomerase
Question
The presence of enzymes to catalyze bioreactions in our bodies allows

A)us to eat non-nutritious substances without consequence.
B)the activation energy of a reaction to be raised.
C)the rate of a desired chemical reaction to slow down.
D)bioreactions to occur under extreme conditions of temperature and pH.
E)bioreactions to take place under mild conditions.
Question
When a substance bonds to an enzyme for reaction, its place of binding is the

A)allosteric site.
B)primary pocket.
C)end pocket.
D)primary site.
E)active site.
Question
In any reaction catalyzed by an enzyme, the reacting molecule is called the

A)substrate.
B)cofactor.
C)coenzyme.
D)isozyme.
E)allostere.
Question
To what main class of enzymes does the enzyme that catalyzes the following reaction belong? O OH <strong>To what main class of enzymes does the enzyme that catalyzes the following reaction belong? O OH   | CH₃ C COO- → CH₃ C HCOO-</strong> A)oxidoreductase B)transferase C)hydrolase D)lyase E)isomerase <div style=padding-top: 35px> | CH₃ C COO- → CH₃ C HCOO-

A)oxidoreductase
B)transferase
C)hydrolase
D)lyase
E)isomerase
Question
Compared to an uncatalyzed reaction, an enzyme-catalyzed reaction

A)uses less substrate.
B)produces different products.
C)occurs at a faster rate.
D)requires more energy.
E)requires a higher temperature.
Question
Most enzymes are

A)fluid-mosaic proteins.
B)induced proteins.
C)substrate proteins.
D)fibrous proteins.
E)globular proteins.
Question
Which of the following is NOT a step in the enzyme-catalyzed conversion of a substrate to product?

A)The substrate binds to the enzyme away from the active site.
B)The substrate binds in the active site to form the E-S complex.
C)The enzyme assists in the conversion of the substrate to product.
D)The product is released from the active site.
E)A new substrate molecule binds to the enzyme for a new cycle.
Question
An increase in concentration of the enzyme LDH in the blood can be used to detect

A)heart attack.
B)kidney damage.
C)anemia.
D)uremia.
E)bulimia.
Question
The active site of an enzyme

A)is remote from the site of substrate attachment.
B)is converted to a product.
C)catalyzes the reaction.
D)increases the energy of reaction.
E)includes the entire enzyme.
Question
The function of the enzyme-substrate complex is to provide an alternative reaction pathway that

A)lowers the energy of the products.
B)lowers the energy of the substrate.
C)changes the concentration of the substrate.
D) decreases the activation energy for the reaction.
E)changes the possible product formed.
Question
The general function of an enzyme in the body is to

A)catalyze chemical reactions.
B)maintain a neutral pH.
C)act as a reactant in carbohydrate storage.
D)maintain homeostasis.
E)eliminate waste products from the blood.
Question
Substances that react under the influence of an enzyme are usually held to the enzyme by

A)peptide bonds.
B)side chains of amino acids in the enzyme protein.
C)ester bonds.
D)pH changes.
E)competitive inhibition.
Question
The formation of an enzyme-substrate complex is the ________ step in enzyme action.

A)first
B)second
C)third
D)fourth
E)last
Question
Creatine kinase can be used in the diagnosis of

A)hepatitis.
B)rickets.
C)heart attack.
D)prostatitis.
E)cancer.
Question
Urease catalyzes only the hydrolysis of urea, and no other substrates. This limited activity is called

A)absolute specificity.
B)extreme specificity.
C)rigid specificity.
D)noncompetitive specificity.
E)hyperspecificity.
Question
Hexokinase catalyzes only the addition of phosphate to any hexose sugar. This type of activity is called

A)regional specificity.
B)collateral specificity.
C)group specificity.
D)noncompetitive specificity.
E)general specificity.
Question
How many generalized steps are there in the reaction of an enzyme (E) with a substrate (S) to form and release the product (P)?

A)one
B)two
C)three
D)four
E)five
Question
In the lock-and-key model of enzyme action, the enzyme active site is thought of as

A)a rigid, nonflexible shape that fits the substrate exactly.
B)an area of the enzyme that can adjust to fit the substrate shape.
C)a key-like shape that fits into a pocket of the substrate surface.
D)a hydrophilic area on the enzyme surface.
E)a lock that bars a noncompetitive inhibitor from reacting.
Question
In an enzyme-substrate reaction, when excess substrate is present, increasing the concentration of the enzyme will

A)increase the number of substrate molecules available.
B)inhibit the formation of products.
C)increase the decomposition rate of the enzyme-substrate complex.
D)decrease the turnover rate for the substrate.
E)increase the amount of reaction occurring.
Question
Urea is converted to ammonia and carbon dioxide by the action of urease. What will be the effect on the rate if the temperature of the reaction is lowered from 37 °C (the optimum temperature) to 27 °C? O <strong>Urea is converted to ammonia and carbon dioxide by the action of urease. What will be the effect on the rate if the temperature of the reaction is lowered from 37 °C (the optimum temperature) to 27 °C? O   NH2 - C - NH2 + H2O   2NH₃ + CO2</strong> A)There will be no effect. B)The rate will slow down. C)The rate will double. D)The rate will triple. E)The rate will slow down, then speed up again. <div style=padding-top: 35px> NH2 - C - NH2 + H2O <strong>Urea is converted to ammonia and carbon dioxide by the action of urease. What will be the effect on the rate if the temperature of the reaction is lowered from 37 °C (the optimum temperature) to 27 °C? O   NH2 - C - NH2 + H2O   2NH₃ + CO2</strong> A)There will be no effect. B)The rate will slow down. C)The rate will double. D)The rate will triple. E)The rate will slow down, then speed up again. <div style=padding-top: 35px> 2NH₃ + CO2

A)There will be no effect.
B)The rate will slow down.
C)The rate will double.
D)The rate will triple.
E)The rate will slow down, then speed up again.
Question
Allosteric enzymes can control their output of product by

A)binding the substrate at a site away from the active site.
B)binding an irreversible inhibitor at the active site.
C)binding a positive or negative regulator at a noncompetitive site.
D)changing the pH in the active site.
E)reversible inhibition using the product as the inhibitor.
Question
The hydrolysis of ester bonds in triglycerides is catalyzed by a(n)

A)lipase.
B)lyase.
C)isomerase.
D)hydrolase.
E)oxidoreductase.
Question
Some insecticides kill insects by inhibiting the enzyme

A)alcohol dehydrogenase.
B)acetylcholinesterase.
C)creatine kinase.
D)lipase.
E)penicillinase.
Question
"Physiological conditions" for reactions within the body are approximately

A)pH 3 and 37 °C.
B)pH 7 and 37 °C.
C)pH 7 and 37 °F.
D)pH 8 and 273 °C.
E)pH 7 and 273 K.
Question
The optimum temperature for sucrase activity is 37 °C. The hydrolysis of sucrose is slowest at which temperature in the choices below?

A)0 °C
B)10 °C
C)20 °C
D)25 °C
E)45 °C
Question
An irreversible inhibitor is one that

A)forms hydrogen bonds with the substrate.
B)binds to the enzyme with hydrophobic interactions.
C)reacts covalently with the substrate.
D)binds covalently to the enzyme active site.
E)reacts covalently with a cofactor.
Question
The surface of a freshly cut apple turns brown because of

A)inhibition of the surface enzymes by nitrogen.
B)interaction of the surface enzymes with oxygen.
C)a change in pH at the surface.
D)an increase in substrate concentration at the cut surface.
E)the presence of vitamin C in the apple.
Question
Most enzymes are deactivated permanently above a temperature of about

A)25 °C.
B)37 °F.
C)40 °C.
D)45 °F.
E)50 °C.
Question
Consider an enzymatic reaction in which the initial concentration of substrate is low. If the amount of enzyme is held constant, but the amount of substrate is increased, the rate of an enzyme catalyzed reaction will

A)increase in an exponential fashion.
B)decrease at first, then increase in a linear fashion.
C)increase at first in a linear fashion, then remain at a constant high rate.
D)stay the same.
E)be inhibited by the higher concentrations of substrate.
Question
A noncompetitive inhibitor has a structure that

A)does not resemble the substrate structure.
B)resembles the active site of the enzyme.
C)can bind to the active site of the enzyme.
D)does not interfere with the enzyme-substrate complex formation.
E)causes a change in the shape of the substrate.
Question
"Physiological pH", the pH for optimum activity for most enzymes, is a pH equal to

A)3.0.
B)5.4.
C)7.4.
D)8.6.
E)9.0.
Question
To what main class of enzymes does the enzyme that catalyzes the following reaction belong? Ser - Ala → Ser + Ala

A)oxidoreductase
B)transferase
C)hydrolase
D)lyase
E)isomerase
Question
A compound that binds to the surface of an enzyme, and changes its shape so that a substrate cannot enter the active site, is called a(n)

A)irreversible inhibitor.
B)proenzyme.
C)cofactor.
D)noncompetitive inhibitor.
E)competitive inhibitor.
Question
Pepsinogen is an example of a(n)

A)coenzyme.
B)cofactor.
C)isoenzyme.
D)allosteric enzyme.
E)zymogen.
Question
Penicillin functions as an antibiotic by

A)poisoning bacteria with toxins.
B)raising the temperature of a bacterium.
C)bonding to metal ions in bacterial electron transport systems.
D)inhibiting the enzymes for cell wall formation in bacteria.
E)acting as an acetylcholinesterase inhibitor.
Question
Penicillin-resistant bacteria can survive treatment with penicillin because they produce the enzyme

A)sucrase.
B)penicillin kinase.
C)penicillinase.
D)bacteriase.
E)phosphate lyase.
Question
A competitive inhibitor is one that

A)binds to the enzyme at a site far from the active site.
B)binds to the active site in place of the substrate.
C)destroys the substrate.
D)binds to the allosteric site on an enzyme.
E)forms a complex with the substrate.
Question
When an end product from an enzyme-mediated sequence is also an inhibitor for an earlier step in the reaction sequence, the process is referred to as

A)feedback control.
B)competitive inhibition.
C)irreversible inhibition.
D)negative catalysis.
E)concentration control.
Question
The names of many enzymes can be recognized by the suffix ________.

A)-ate
B)-ite
C)-ose
D)-ine
E)-ase
Question
The B vitamins are examples of

A)water-soluble vitamins.
B)essential amino acids.
C)essential minerals.
D)oil soluble vitamins.
E)vitamins that are stored in the liver.
Question
Enzymes that catalyze the same reactions but have slightly different structures are called ________.

A)coenzymes
B)cofactors
C)isoenzymes
D)competitive
E)noncompetitive
Question
A biological catalyst is called a(n) ________.

A)lipid
B)enzyme
C)cofactor
D)coenzyme
E)substrate
Question
The optimum pH for the activity of trypsin is about ________.

A)2.0
B)4.0
C)6.5
D)7.4
E)8.0
Question
When a cofactor is a small organic molecule, it is known as a(n)

A)isoenzyme.
B)vitamin.
C)zymogen.
D)coenzyme.
E)regulator.
Question
Allosteric enzymes can control their output of product by

A)binding the substrate at a site away from the active site.
B)binding an irreversible inhibitor at the active site.
C)binding a positive or negative regulator at a noncompetitive site.
D)changing the pH in the active site.
E)reversible inhibition using the product as the inhibitor.
Question
The optimum pH for the activity of pepsin is about ________.

A)2.0
B)4.0
C)6.5
D)7.4
E)7.6
Question
When an end product from an enzyme-mediated sequence is also an inhibitor for an earlier step in the reaction sequence, the process is referred to as

A)feedback control.
B)competitive inhibition.
C)irreversible inhibition.
D)negative catalysis.
E)concentration control.
Question
Iron(II) and iron(III) ions are used in the functioning of

A)urease.
B)alcohol dehydrogenase.
C)creatine kinase.
D)the cytochrome oxidase system.
E)pepsin.
Question
A noncompetitive inhibitor

A)binds at the active site of the enzyme.
B)alters the three-dimensional structure of the enzyme.
C)increases the rate of the enzyme-catalyzed reaction.
D)has a structure similar to the substrate.
E)has its effect reversed by adding more substrate.
Question
The water-soluble B and C vitamins supply

A)essential amino acids.
B)substrates necessary for most of the reactions in the body.
C)essential fatty acids.
D)coenzymes required by some enzymes.
E)competitive inhibitors needed to regulate enzyme activity.
Question
Metal ions such as Zn2+ and Fe3+ are often needed by enzymes as

A)isozymes.
B)allosteres.
C)inhibitors.
D)cofactors.
E)substrates.
Question
Pepsinogen is an example of a(n)

A)coenzyme.
B)cofactor.
C)isoenzyme.
D)allosteric enzyme.
E)zymogen.
Question
The full name of the enzyme LDH is ________.

A)lactate dehydrogenase
B)liver decompensation hexase
C)lactate dehydrase
D)liver dihydrogen kinase
E)lipase dehydrogenase
Question
Which of the following is NOT true for a competitive inhibitor?

A)It occupies the active site.
B)It cannot be converted to products.
C)It has a structure similar to the substrate.
D)Increasing the substrate concentration can reverse competitive inhibition.
E)It binds to the enzyme at a site remote from the active site.
Question
Another name for a zymogen is a(n) ________.

A)cofactor
B)coenzyme
C)prosthetic group
D)isozyme
E)proenzyme
Question
An enzyme that removes H from a substrate is classified as a(n) ________.

A)oxidoreductase
B)transferase
C)hydrolase
D)lyase
E)isomerase
Question
Coenzymes such as water-soluble vitamins are needed in only small amounts because

A)only small amounts of enzymes are present in each cell.
B)only small amounts of substrates are available at any one time.
C)they can be eliminated in the urine.
D)each vitamin molecule can be reused many times as a cofactor.
E)they can be stored in the liver for future use.
Question
An enzyme that converts a cis double bond to a trans double bond is classified as a(n) ________.

A)oxidoreductase
B)transferase
C)hydrolase
D)lyase
E)isomerase
Question
Indicate whether each of the following is fat soluble or water soluble.
pantothenic acid
Question
Indicate whether each of the following is fat soluble or water soluble.
vitamin D
Question
Indicate whether each of the following is fat soluble or water soluble.
vitamin E
Question
Alanine transaminase is an example of a transferase enzyme.
Question
Indicate whether each of the following is fat soluble or water soluble.
vitamin B6
Question
Indicate whether each of the following is fat soluble or water soluble.
vitamin K
Question
Indicate whether each of the following is fat soluble or water soluble.
ascorbic acid
Question
Indicate whether each of the following is fat soluble or water soluble.
vitamin A
Question
Pyruvate carboxylase is an example of a ligase enzyme.
Question
The optimum pH of most cellular enzymes is about 7.4.
Question
Phosphorylation is a common form of covalent modification.
Question
Indicate whether each of the following is fat soluble or water soluble.
riboflavin
Question
A diet very low in vitamin C can lead over time to the condition ________.

A)rickets
B)scurvy
C)cancer
D)carpal tunnel syndrome
E)anorexia nervosa
Question
Indicate whether each of the following is fat soluble or water soluble.
folic acid
Question
The active site is a large part of an enzyme.
Question
One deficiency disease that can be traced to insufficient intake of vitamin D is ________.

A)scurvy
B)rickets
C)beriberi
D)pellagra
E)pernicious anemia
Question
Indicate whether each of the following is fat soluble or water soluble.
niacin
Question
Insulin and digestive enzymes are produced as inactive forms called zymogens.
Question
Urease is an example of an oxidoreductase enzyme.
Question
In the induced fit model of enzyme activity, both the enzyme and the substrate change shape.
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Deck 20: Enzymes and Vitamins
1
In the induced-fit model of enzyme action, the enzyme active site

A)stays the same shape during substrate binding.
B)adjusts shape to adapt to the shape of the substrate.
C)stays the same shape while causing a change in the shape of the substrate.
D)uses an inhibitor to adjust its shape for the substrate.
E)uses a cofactor to change the shape of a substrate.
adjusts shape to adapt to the shape of the substrate.
2
To what main class of enzymes does the enzyme that catalyzes the conversion of lactose to galactose and glucose belong?

A)oxidoreductase
B)transferase
C)hydrolase
D)lyase
E)isomerase
hydrolase
3
The presence of enzymes to catalyze bioreactions in our bodies allows

A)us to eat non-nutritious substances without consequence.
B)the activation energy of a reaction to be raised.
C)the rate of a desired chemical reaction to slow down.
D)bioreactions to occur under extreme conditions of temperature and pH.
E)bioreactions to take place under mild conditions.
bioreactions to take place under mild conditions.
4
When a substance bonds to an enzyme for reaction, its place of binding is the

A)allosteric site.
B)primary pocket.
C)end pocket.
D)primary site.
E)active site.
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5
In any reaction catalyzed by an enzyme, the reacting molecule is called the

A)substrate.
B)cofactor.
C)coenzyme.
D)isozyme.
E)allostere.
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6
To what main class of enzymes does the enzyme that catalyzes the following reaction belong? O OH <strong>To what main class of enzymes does the enzyme that catalyzes the following reaction belong? O OH   | CH₃ C COO- → CH₃ C HCOO-</strong> A)oxidoreductase B)transferase C)hydrolase D)lyase E)isomerase | CH₃ C COO- → CH₃ C HCOO-

A)oxidoreductase
B)transferase
C)hydrolase
D)lyase
E)isomerase
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7
Compared to an uncatalyzed reaction, an enzyme-catalyzed reaction

A)uses less substrate.
B)produces different products.
C)occurs at a faster rate.
D)requires more energy.
E)requires a higher temperature.
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8
Most enzymes are

A)fluid-mosaic proteins.
B)induced proteins.
C)substrate proteins.
D)fibrous proteins.
E)globular proteins.
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9
Which of the following is NOT a step in the enzyme-catalyzed conversion of a substrate to product?

A)The substrate binds to the enzyme away from the active site.
B)The substrate binds in the active site to form the E-S complex.
C)The enzyme assists in the conversion of the substrate to product.
D)The product is released from the active site.
E)A new substrate molecule binds to the enzyme for a new cycle.
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10
An increase in concentration of the enzyme LDH in the blood can be used to detect

A)heart attack.
B)kidney damage.
C)anemia.
D)uremia.
E)bulimia.
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11
The active site of an enzyme

A)is remote from the site of substrate attachment.
B)is converted to a product.
C)catalyzes the reaction.
D)increases the energy of reaction.
E)includes the entire enzyme.
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12
The function of the enzyme-substrate complex is to provide an alternative reaction pathway that

A)lowers the energy of the products.
B)lowers the energy of the substrate.
C)changes the concentration of the substrate.
D) decreases the activation energy for the reaction.
E)changes the possible product formed.
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13
The general function of an enzyme in the body is to

A)catalyze chemical reactions.
B)maintain a neutral pH.
C)act as a reactant in carbohydrate storage.
D)maintain homeostasis.
E)eliminate waste products from the blood.
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14
Substances that react under the influence of an enzyme are usually held to the enzyme by

A)peptide bonds.
B)side chains of amino acids in the enzyme protein.
C)ester bonds.
D)pH changes.
E)competitive inhibition.
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15
The formation of an enzyme-substrate complex is the ________ step in enzyme action.

A)first
B)second
C)third
D)fourth
E)last
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16
Creatine kinase can be used in the diagnosis of

A)hepatitis.
B)rickets.
C)heart attack.
D)prostatitis.
E)cancer.
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k this deck
17
Urease catalyzes only the hydrolysis of urea, and no other substrates. This limited activity is called

A)absolute specificity.
B)extreme specificity.
C)rigid specificity.
D)noncompetitive specificity.
E)hyperspecificity.
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18
Hexokinase catalyzes only the addition of phosphate to any hexose sugar. This type of activity is called

A)regional specificity.
B)collateral specificity.
C)group specificity.
D)noncompetitive specificity.
E)general specificity.
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19
How many generalized steps are there in the reaction of an enzyme (E) with a substrate (S) to form and release the product (P)?

A)one
B)two
C)three
D)four
E)five
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20
In the lock-and-key model of enzyme action, the enzyme active site is thought of as

A)a rigid, nonflexible shape that fits the substrate exactly.
B)an area of the enzyme that can adjust to fit the substrate shape.
C)a key-like shape that fits into a pocket of the substrate surface.
D)a hydrophilic area on the enzyme surface.
E)a lock that bars a noncompetitive inhibitor from reacting.
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21
In an enzyme-substrate reaction, when excess substrate is present, increasing the concentration of the enzyme will

A)increase the number of substrate molecules available.
B)inhibit the formation of products.
C)increase the decomposition rate of the enzyme-substrate complex.
D)decrease the turnover rate for the substrate.
E)increase the amount of reaction occurring.
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22
Urea is converted to ammonia and carbon dioxide by the action of urease. What will be the effect on the rate if the temperature of the reaction is lowered from 37 °C (the optimum temperature) to 27 °C? O <strong>Urea is converted to ammonia and carbon dioxide by the action of urease. What will be the effect on the rate if the temperature of the reaction is lowered from 37 °C (the optimum temperature) to 27 °C? O   NH2 - C - NH2 + H2O   2NH₃ + CO2</strong> A)There will be no effect. B)The rate will slow down. C)The rate will double. D)The rate will triple. E)The rate will slow down, then speed up again. NH2 - C - NH2 + H2O <strong>Urea is converted to ammonia and carbon dioxide by the action of urease. What will be the effect on the rate if the temperature of the reaction is lowered from 37 °C (the optimum temperature) to 27 °C? O   NH2 - C - NH2 + H2O   2NH₃ + CO2</strong> A)There will be no effect. B)The rate will slow down. C)The rate will double. D)The rate will triple. E)The rate will slow down, then speed up again. 2NH₃ + CO2

A)There will be no effect.
B)The rate will slow down.
C)The rate will double.
D)The rate will triple.
E)The rate will slow down, then speed up again.
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23
Allosteric enzymes can control their output of product by

A)binding the substrate at a site away from the active site.
B)binding an irreversible inhibitor at the active site.
C)binding a positive or negative regulator at a noncompetitive site.
D)changing the pH in the active site.
E)reversible inhibition using the product as the inhibitor.
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24
The hydrolysis of ester bonds in triglycerides is catalyzed by a(n)

A)lipase.
B)lyase.
C)isomerase.
D)hydrolase.
E)oxidoreductase.
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25
Some insecticides kill insects by inhibiting the enzyme

A)alcohol dehydrogenase.
B)acetylcholinesterase.
C)creatine kinase.
D)lipase.
E)penicillinase.
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26
"Physiological conditions" for reactions within the body are approximately

A)pH 3 and 37 °C.
B)pH 7 and 37 °C.
C)pH 7 and 37 °F.
D)pH 8 and 273 °C.
E)pH 7 and 273 K.
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27
The optimum temperature for sucrase activity is 37 °C. The hydrolysis of sucrose is slowest at which temperature in the choices below?

A)0 °C
B)10 °C
C)20 °C
D)25 °C
E)45 °C
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28
An irreversible inhibitor is one that

A)forms hydrogen bonds with the substrate.
B)binds to the enzyme with hydrophobic interactions.
C)reacts covalently with the substrate.
D)binds covalently to the enzyme active site.
E)reacts covalently with a cofactor.
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29
The surface of a freshly cut apple turns brown because of

A)inhibition of the surface enzymes by nitrogen.
B)interaction of the surface enzymes with oxygen.
C)a change in pH at the surface.
D)an increase in substrate concentration at the cut surface.
E)the presence of vitamin C in the apple.
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30
Most enzymes are deactivated permanently above a temperature of about

A)25 °C.
B)37 °F.
C)40 °C.
D)45 °F.
E)50 °C.
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31
Consider an enzymatic reaction in which the initial concentration of substrate is low. If the amount of enzyme is held constant, but the amount of substrate is increased, the rate of an enzyme catalyzed reaction will

A)increase in an exponential fashion.
B)decrease at first, then increase in a linear fashion.
C)increase at first in a linear fashion, then remain at a constant high rate.
D)stay the same.
E)be inhibited by the higher concentrations of substrate.
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32
A noncompetitive inhibitor has a structure that

A)does not resemble the substrate structure.
B)resembles the active site of the enzyme.
C)can bind to the active site of the enzyme.
D)does not interfere with the enzyme-substrate complex formation.
E)causes a change in the shape of the substrate.
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33
"Physiological pH", the pH for optimum activity for most enzymes, is a pH equal to

A)3.0.
B)5.4.
C)7.4.
D)8.6.
E)9.0.
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34
To what main class of enzymes does the enzyme that catalyzes the following reaction belong? Ser - Ala → Ser + Ala

A)oxidoreductase
B)transferase
C)hydrolase
D)lyase
E)isomerase
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35
A compound that binds to the surface of an enzyme, and changes its shape so that a substrate cannot enter the active site, is called a(n)

A)irreversible inhibitor.
B)proenzyme.
C)cofactor.
D)noncompetitive inhibitor.
E)competitive inhibitor.
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36
Pepsinogen is an example of a(n)

A)coenzyme.
B)cofactor.
C)isoenzyme.
D)allosteric enzyme.
E)zymogen.
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37
Penicillin functions as an antibiotic by

A)poisoning bacteria with toxins.
B)raising the temperature of a bacterium.
C)bonding to metal ions in bacterial electron transport systems.
D)inhibiting the enzymes for cell wall formation in bacteria.
E)acting as an acetylcholinesterase inhibitor.
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38
Penicillin-resistant bacteria can survive treatment with penicillin because they produce the enzyme

A)sucrase.
B)penicillin kinase.
C)penicillinase.
D)bacteriase.
E)phosphate lyase.
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39
A competitive inhibitor is one that

A)binds to the enzyme at a site far from the active site.
B)binds to the active site in place of the substrate.
C)destroys the substrate.
D)binds to the allosteric site on an enzyme.
E)forms a complex with the substrate.
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40
When an end product from an enzyme-mediated sequence is also an inhibitor for an earlier step in the reaction sequence, the process is referred to as

A)feedback control.
B)competitive inhibition.
C)irreversible inhibition.
D)negative catalysis.
E)concentration control.
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41
The names of many enzymes can be recognized by the suffix ________.

A)-ate
B)-ite
C)-ose
D)-ine
E)-ase
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42
The B vitamins are examples of

A)water-soluble vitamins.
B)essential amino acids.
C)essential minerals.
D)oil soluble vitamins.
E)vitamins that are stored in the liver.
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43
Enzymes that catalyze the same reactions but have slightly different structures are called ________.

A)coenzymes
B)cofactors
C)isoenzymes
D)competitive
E)noncompetitive
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44
A biological catalyst is called a(n) ________.

A)lipid
B)enzyme
C)cofactor
D)coenzyme
E)substrate
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45
The optimum pH for the activity of trypsin is about ________.

A)2.0
B)4.0
C)6.5
D)7.4
E)8.0
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46
When a cofactor is a small organic molecule, it is known as a(n)

A)isoenzyme.
B)vitamin.
C)zymogen.
D)coenzyme.
E)regulator.
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47
Allosteric enzymes can control their output of product by

A)binding the substrate at a site away from the active site.
B)binding an irreversible inhibitor at the active site.
C)binding a positive or negative regulator at a noncompetitive site.
D)changing the pH in the active site.
E)reversible inhibition using the product as the inhibitor.
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48
The optimum pH for the activity of pepsin is about ________.

A)2.0
B)4.0
C)6.5
D)7.4
E)7.6
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49
When an end product from an enzyme-mediated sequence is also an inhibitor for an earlier step in the reaction sequence, the process is referred to as

A)feedback control.
B)competitive inhibition.
C)irreversible inhibition.
D)negative catalysis.
E)concentration control.
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50
Iron(II) and iron(III) ions are used in the functioning of

A)urease.
B)alcohol dehydrogenase.
C)creatine kinase.
D)the cytochrome oxidase system.
E)pepsin.
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51
A noncompetitive inhibitor

A)binds at the active site of the enzyme.
B)alters the three-dimensional structure of the enzyme.
C)increases the rate of the enzyme-catalyzed reaction.
D)has a structure similar to the substrate.
E)has its effect reversed by adding more substrate.
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52
The water-soluble B and C vitamins supply

A)essential amino acids.
B)substrates necessary for most of the reactions in the body.
C)essential fatty acids.
D)coenzymes required by some enzymes.
E)competitive inhibitors needed to regulate enzyme activity.
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53
Metal ions such as Zn2+ and Fe3+ are often needed by enzymes as

A)isozymes.
B)allosteres.
C)inhibitors.
D)cofactors.
E)substrates.
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54
Pepsinogen is an example of a(n)

A)coenzyme.
B)cofactor.
C)isoenzyme.
D)allosteric enzyme.
E)zymogen.
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55
The full name of the enzyme LDH is ________.

A)lactate dehydrogenase
B)liver decompensation hexase
C)lactate dehydrase
D)liver dihydrogen kinase
E)lipase dehydrogenase
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56
Which of the following is NOT true for a competitive inhibitor?

A)It occupies the active site.
B)It cannot be converted to products.
C)It has a structure similar to the substrate.
D)Increasing the substrate concentration can reverse competitive inhibition.
E)It binds to the enzyme at a site remote from the active site.
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57
Another name for a zymogen is a(n) ________.

A)cofactor
B)coenzyme
C)prosthetic group
D)isozyme
E)proenzyme
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58
An enzyme that removes H from a substrate is classified as a(n) ________.

A)oxidoreductase
B)transferase
C)hydrolase
D)lyase
E)isomerase
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59
Coenzymes such as water-soluble vitamins are needed in only small amounts because

A)only small amounts of enzymes are present in each cell.
B)only small amounts of substrates are available at any one time.
C)they can be eliminated in the urine.
D)each vitamin molecule can be reused many times as a cofactor.
E)they can be stored in the liver for future use.
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60
An enzyme that converts a cis double bond to a trans double bond is classified as a(n) ________.

A)oxidoreductase
B)transferase
C)hydrolase
D)lyase
E)isomerase
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61
Indicate whether each of the following is fat soluble or water soluble.
pantothenic acid
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62
Indicate whether each of the following is fat soluble or water soluble.
vitamin D
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63
Indicate whether each of the following is fat soluble or water soluble.
vitamin E
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64
Alanine transaminase is an example of a transferase enzyme.
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65
Indicate whether each of the following is fat soluble or water soluble.
vitamin B6
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66
Indicate whether each of the following is fat soluble or water soluble.
vitamin K
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67
Indicate whether each of the following is fat soluble or water soluble.
ascorbic acid
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68
Indicate whether each of the following is fat soluble or water soluble.
vitamin A
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69
Pyruvate carboxylase is an example of a ligase enzyme.
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70
The optimum pH of most cellular enzymes is about 7.4.
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71
Phosphorylation is a common form of covalent modification.
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72
Indicate whether each of the following is fat soluble or water soluble.
riboflavin
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73
A diet very low in vitamin C can lead over time to the condition ________.

A)rickets
B)scurvy
C)cancer
D)carpal tunnel syndrome
E)anorexia nervosa
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74
Indicate whether each of the following is fat soluble or water soluble.
folic acid
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75
The active site is a large part of an enzyme.
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76
One deficiency disease that can be traced to insufficient intake of vitamin D is ________.

A)scurvy
B)rickets
C)beriberi
D)pellagra
E)pernicious anemia
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77
Indicate whether each of the following is fat soluble or water soluble.
niacin
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78
Insulin and digestive enzymes are produced as inactive forms called zymogens.
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79
Urease is an example of an oxidoreductase enzyme.
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80
In the induced fit model of enzyme activity, both the enzyme and the substrate change shape.
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