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Module 1B > 8 Enzymes > Flashcards

8 Enzymes Flashcards

1
Q

Protein catalysts that increase the rate of chemical reactions

A

Enzymes

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2
Q

Are enzymes altered or consumed in chemical reactions?

A

No, enzymes are neither altered nor consumed in the reactions

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3
Q

A protein that provide a means for regulating metabolic pathways in the body

A

Enzymes

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4
Q

What is catalytic power in enzymes?

A

Enzyme’s ability to accelerate the rate of noncatalyzed reactions by as much as 10^26 times

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5
Q

What does enzyme specificity mean?

A

Extreme selectivity to the substances it interacts with (substrate), and the reaction it catalyzes

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6
Q

Why enzyme activity regulation is important?

A

Activity can be regulated (increased or decreased) so that the rate of product formation responds to cellular need

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7
Q

How many classes of reactions are recognized?

A

Six classes (oxidoreductases, transferases, hydrolases, lyases, isomerases, and ligases)

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8
Q

Which class of enzymes catalyzes oxidation-reduction reactions?

A

Oxidoreductase

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9
Q

Which class of enzymes catalyzes transfer of moieties such as glycosyl, methyl, or phosphoryl groups?

A

Transferase

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10
Q

Which class of enzymes catalyzes cleavage of bonds by addition of water?

A

Hydrolase

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11
Q

Which class of enzymes catalyzes cleavage of C–C, C–S, and certain C–N bonds?

A

Lyase

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12
Q

Which class of enzymes catalyzes rearrangement of optical or geometric isomers?

A

Isomerase

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13
Q

Which class of enzymes catalyzes formation of bonds between two molecules coupled to the hydrolysis of high-energy phosphates?

A

Ligase

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14
Q

What is the difference between synthase and synthetase?

A

Synthase catalyzes the formation of a compound without ATP, while synthetase requires ATP

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15
Q

What enzyme uses water to remove phosphate group?

A

Phosphatase

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16
Q

What enzyme adds phosphate from inorganic phosphate to organic molecule acceptor?

A

Phosphorylase

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17
Q

What is the role of oxidase enzyme?

A

Oxidase enzyme use oxygen as the acceptor, but oxygen atoms are not incorporated into the substrate

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18
Q

How does oxygenase function in reactions?

A

Oxygenase enzymes incorporate one or both oxygen atoms into the substrate

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19
Q

Special cleft that provides the environment wherein chemical transformation takes place.

A

Active Site

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20
Q

True or False. Substrate able to bind through weak forces such as hydrogen bonds.

A

TRUE

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21
Q

The specific site on the enzyme where the substrate binds and catalysis occurs

A

Active site

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22
Q

The substance by which an enzyme acts

A

Substrate

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23
Q

What do you call the metal ions that participate directly in substrate binding or catalysis and extend the mechanistic capabilities of an enzyme?

A

Cofactor

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24
Q

What enzymes require a metal ion cofactor?

A

Metal Activated Enzymes

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25
Q

What enzyme contains metal ions that serve as prosthetic group?

A

Metalloenzymes

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26
Q

What organic molecules participate directly in substrate binding (catalysis) and extend mechanistic capabilities of an enzyme?

A

Coenzyme

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27
Q

_____ is permanently associated with the enzyme

A

Prosthetic group

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28
Q

What is the non-protein component that is transiently associated with the enzyme?

A

Cosubstrate

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29
Q

What is an enzyme without its nonprotein moiety and catalytically inactive?

A

Apoenzyme

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30
Q

Some enzymes require non-proteins for enzymatic activity. What is the term for an enzyme with its nonprotein moiety that is catalytically active?

A

Holoenzyme

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31
Q

What are the two models for enzyme specifity?

A

Lock and Key model & Induced fit model

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32
Q

What model describes enzymes as resembling a lock while the particular substrate acts as the key?

A

Lock and Key model

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33
Q

What model is being described when the active site of an enzyme is modified or altered upon binding of the substrate?

A

Induced Fit Model

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34
Q

What are the Enzyme Catalysis Strategies?

A

Catalysis by Proximity and Orientation, Acid-Base Catalysis, Catalysis by Strain, Covalent Catalysis, and Ribozymes

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35
Q

An Enzyme Catalysis Strategy where substrate molecules must come within bond-forming distance in order to interact?

A

Catalysis by Proximity and Orientation

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36
Q

An Enzyme Catalysis Strategy where the enzyme allow subtrates to bind in a manner that places reactive groups in appropriate orientations to chemically interact?

A

Catalysis by Proximity and Orientation

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37
Q

An Enzyme Catalysis Strategy where the acceleration of the reaction is achieved by the catalytic transfer of a proton?

A

Acid-Base Catalysis

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38
Q

What are the two types of Acid-Base Catalysis?

A

Specific Acid/Base Catalysis and General Acid/Base Catalysis

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39
Q

What are the only participating acids or bases in specific acid/base catalysis?

A

Protons or Hydroxide ions

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40
Q

Enzymes bind substrates in a conformation that weakens the bond targeted for cleavage through physical distortion and electronic polarization.

A

Catalysis by Strain

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41
Q

Involves formation of a covalent bond between enzyme and one or more substrate.

A

Covalent Catalysis

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42
Q

Residues on the enzyme that participate in Covalent catalysis are?

A

Cysteine or Serine, Histidine(occasionally)

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43
Q

An Enzyme Catalysis Strategy that follows a ping-pong mechanism

A

Covalent Catalysis

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44
Q

Consisted of Catalytic RNAs and most act in RNA processing

A

Ribozymes

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45
Q

Ribozymes satisfy several enzymatic criteria, what are these?

A

Substrate specific, Enhance reaction rate, Emerge from reaction unchanged

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46
Q

Performs the vitally important and highly complex process of synthesizing long polypeptide chains following the instructions encoded in mRNA molecules

A

Ribosomes

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47
Q

Enzymes are proteins except for?

A

Ribozymes

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48
Q

What are the three distinctive features of enzymes?

A

Catalytic power, specificity, and regulation

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49
Q

What are the non protein components that are essential for the catalysis to occur?

A

Cofactors and coenzymes

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50
Q

____ is the systematic study of the rate of reactions

A

Kinetics

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51
Q

____ is a transient, high-energy intermediate condition where bonds in the substrate are maximally strainedA

A

Transition State

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52
Q

Where does the transition state appear in the energy diagram of a chemical reaction?

A

At the apex of the energy profile in the energy diagram

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53
Q

Describes the direction in which the reaction will tend to proceed. It describes in quantitative form the direction and the concentration of the reactant and products present at equilibrium.

A

Free Energy Change/ ΔG

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54
Q

The energy input required to initiate a reaction is referred to as the ____

A

energy of activation

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55
Q

Enzymes lower the ________ energy required for a reaction by providing an alternate energetically favorable pathway.

A

activation

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56
Q

TRUE OR FALSE. Higher energy of activation, the faster the reaction will proceed

A

FALSE, the slower the reaction will proceed

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57
Q

Enzymes lower the ________ energy required for a reaction by providing an alternate energetically favorable pathway.

A

activation

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58
Q

Regardless in the presence or absence of enzymes, the overall concentration of reactants and products remain constant, thus, the ____ is unaffected.

A

equilibrium constant

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59
Q

Temprature increases the rate of uncatalyzed and enzyme-catalyzed reactions by increasing ___ and ___ of the reacting molecules.

A

kinetic energy and collision frequency

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60
Q

What is the “collision theory of capital kinetics”?

A

“For two molecules to react, they must collide and that they must have sufficient kinetic energy to overcome energy barrier”

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61
Q

However, further increase in temperature does not increase activity any more because at temperatures too high, heat energy can disrupt noncovalent interaction that maintains the ____ of proteins.

A

3D structure

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62
Q

The rate of almost all enzyme-catalyzed reactions significantly depends on ________ concentration, also known as pH.

A

hydrogen ion

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63
Q

This affects active site ionization, and enzyme denaturation

A

hydrogen ion concentration

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64
Q

pH at which maximal enzyme activity is achieved is ____

A

variable

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65
Q

What is the pH at which maximal enzyme activity is achieved for most intracellular enzyme?

A

5-9

66
Q

What is the pH at which maximal enzyme activity is achieved for pepsin?

A

2

67
Q

As substrate concentration increases, rate ____ until it reaches a maximum value

A

increases

68
Q

What do you call the value where the enzyme is saturated and no further reaction can occur even as substrate concentration is increased?

A

Maximum Velocity (Vmax)

69
Q

What do you call the behavior where the reaction velocity does not increase despite increase in substrate concentration?

A

Saturation Effect

70
Q

____ kinetics is when the rate is independent of reactant (substrate) concentration

A

Zero-Order

71
Q

What shape does the curve in an enzyme-catalyzed reaction typically exhibit in a plot of reaction rate versus substrate concentration?

A

Hyperbolic

72
Q

Describes how reaction velocity varies with substrate concentration.

A

Michaelis-Menten Kinetics

73
Q

This reflects the affinity of an enzyme for a substrate. Numerically, it is equal to the substrate concentration at which vi is half the maximum velocity

A

Michaelis Constant Km

74
Q

TRUE OR FALSE. The lower the Km, the higher the affinity of an enzyme to a substrate.

A

TRUE

75
Q

What is the reaction order when the substrate concentration [𝑆] is much less than the Michaelis constant (𝐾𝑚)?

A

The reaction velocity is approximately proportional to substrate concentration, exhibiting first-order reaction kinetics.

76
Q

What is the reaction order when the substrate concentration [𝑆] is much greater than the Michaelis constant (𝐾𝑚)?

A

The reaction velocity is independent of substrate concentration, exhibiting zero-order reaction kinetics.

77
Q

What is the linear form of the Michaelis-Menten equation used to determine enzyme kinetics, with the y-intercept representing 1/Vi, the x-intercept representing -1/Km, and the slope representing Km/Vmax?

A

Lineweaver-Burk Plot

78
Q

What is the equation that is describing the enzymes with positive cooperativity, where the initial reaction velocity increases as the nth power of substrate concentration?

A

Hill Equation

79
Q

What is the, ability to determine the kinetic mechanism of an enzyme inhibitor and inhibition constants by producing a straight line graph?

A

Lineweaver-Burk Plot Virtue

80
Q

An empirical parameter denoted as ‘n’ in the Lineweaver-Burk Plot, representing the number, kind, and strength of interactions of multiple substrate-binding sites of an enzyme.

A

Hill Coefficient

81
Q

What is the type of reversible inhibition where the inhibitor binds to the enzyme at a site distinct from the substrate-binding site, competing with the substrate for binding.

A

Competitive Inhibition

82
Q

What is the sign when all binding sites of the hill coefficient behave independently?

A

n = 1

83
Q

What is the sign when the hill coefficient exhibits positive cooperativity?

A

n > 1

84
Q

What is the classification of inhibitor that interact with the enzyme through noncovalent association/dissociation reactions?

A

Reversible

85
Q

What is the type of reversible inhibition where the inhibitor binds to the enzyme at a site other than the active site, not competing with the substrate for binding?

A

Noncompetitive Inhibition

86
Q

What is the type of inhibition where inhibitors form covalent bonds with side chains or prosthetic groups in enzymes?

A

Irreversible Inhibition

87
Q

Substrates and inhibitors compete for the same binding site on the enzyme. Therefore, there will be _____

A

slowing down of reaction.

88
Q

Substrate shares a high degree of structural similarity to the inhibitor. Hence, it also follows that the inhibitor would bind to the substrate binding portion of the active site. However, the effect of competitive inhibitors can be overcome by _____

A

increasing the concentration of the substrate.

89
Q

What is an example of a competitive inhibitor, are a group of medicines that can help lower the level of low-density lipoprotein (LDL) cholesterol in the blood?

A

Statin

90
Q

Metabolite of Allopurinol, acts as a noncompetitive inhibitor of xanthine oxidase.

A

Oxypurinol

91
Q

Drug requiring metabolism to its active form; Allopurinol is a prodrug metabolized to Oxypurinol, a xanthine oxidase inhibitor.

A

Prodrug

92
Q

Form of arthritis causing joint pain and swelling due to high uric acid levels.

A

Gout

93
Q

This contains a beta lactam ring that binds to enzyme serine residue, blocking cell wall synthesis in bacteria. What do you call this?

A

Penicillin

94
Q

Sometimes irreversible enzymes are also termed as __ because even after removal of the remaining inhibitor, your enzymes are still inhibited

A

poison enzymes

95
Q

Penicillin is able to exert its effect by covalently reacting with an essential serine residue on the active site of the enzyme ___, an enzyme responsible for cross-linking peptidoglycan chains

A

glycopeptide transpeptidase

96
Q

Penicillin’s conformation resembles the transition state of glycopeptide transpeptidase’s normal substrate which is called

A

Transition State Analog

97
Q

What kind of single displacement is an addition of substrates in a specific order?

A

Ordered

98
Q

What kind of single displacement that either substrates may combine with the enzyme?

A

Random

99
Q

A bimolecular reaction where both substrates must combine with enzyme to form a ternary complex for catalysis to occur

A

Single Displacement/Sequential reaction

100
Q

A bimolecular reaction where one or more products released from enzyme before all substrates have been added. Ping-pong mechanism is the other term.

A

Double Displacement

101
Q

Enzymes increase the rate of chemical reactions by ___

A

lowering the energy of activation.

102
Q

3 factors that affect the rates of enzyme catalysis

A

Temperature, pH, and substrate concentration

103
Q

Substrate analogs generating reactive groups during enzyme catalysis, irreversibly inhibiting the enzyme.

A

Suicide Inhibitors

104
Q

This describes enzyme kinetics relating substrate concentration to reaction rate.

A

Michaelis-Menten Equation

105
Q

Protein catalysts that increase the rate of chemical reactions without being changed in the overall process

A

Enzymes

106
Q

T/F Almost all enzymes are proteins, except for ribozymes, which are ribosomal RNAs and a handful of other RNAs.

A

TRUE

107
Q

T/F Enzymes are neither altered nor consumed in a reaction. They may be modified during a reaction sequence but return to their original form in the end

A

TRUE

108
Q

How do enzymes regulate metabolic pathways?

A

By controlling the rate of product formation in response to cellular needs

109
Q

It refers to the ability of enzymes to accelerate the reaction rates of non-catalyzed reactions by up to 10²⁶ times.

A

Catalytic power

110
Q

T/F Enzyme activity cannot be regulated?

A

FALSE; Enzyme activity can be regulated, meaning it can be increased or decreased to ensure that the rate of product formation meets the cellular need.

111
Q

How are enzymes traditionally named?

A

By adding the suffix “-ase” to the name of the substrate they act upon or by the reaction they catalyze

112
Q

How many classes of reactions are recognized in the systemic naming of enzymes?

A

Six Classes

113
Q

What type of reactions do oxidoreductases catalyze?

A

Oxidation-reduction reactions (where an oxidized compound loses electrons.)

114
Q

Enzymes that catalyze the transfer of carbon, nitrogen, or phosphorus-containing groups.

A

Transferase

115
Q

What enzyme catalyzes the cleavage of bonds by the addition of water?

A

Hydrolase

116
Q

Which enzyme type catalyzes the cleavage of C–C, C–S, or certain C–N bonds without the use of water?

A

Lyase

117
Q

What is the main difference between a lyase and a ligase?

A

Lyase cleaves bonds; Ligase forms bonds

118
Q

What enzymes is responsible for rearranging optical or geometric isomers within a molecule?

A

Isomerase

119
Q

What enzyme requires ATP to function?

A

Synthetase

120
Q

What term describes an enzyme that is catalytically inactive because it lacks its non-protein moiety?

A

Apoenzyme

121
Q

Organic molecules that participate directly in the enzyme’s catalytic process and can either be permanently associated as a prosthetic group or transiently associated as a co-substrate

A

Coenzymes

122
Q

What enzyme catalyzes the removal of water from a molecule?

A

Dehydratase

123
Q

Isomerases are involved in which type of reaction?

A

Rearrangement of molecular structure

124
Q

Enzymes that are responsible for forming new covalent bonds between molecules, a process that is typically coupled with the hydrolysis of ATP to provide the necessary energy

A

Ligase

125
Q

What enzyme type adds a phosphate group to a substrate using inorganic phosphate?

A

Phosphorylase

126
Q

They are typically metal ions, such as zinc or iron, that help enzymes in binding substrates or catalyzing reactions. They can either be metal-activated enzymes or part of metalloenzymes.

A

Cofactors

127
Q

A non-protein coenzyme or metal ion that is permanently attached to the enzyme, forming a stable complex.

A

Prosthetic Group

128
Q

A coenzyme that binds transiently during the enzymatic reaction.

A

Co-substrate

129
Q

A fully active enzyme composed of its protein component (apoenzyme) and its non-protein moiety (cofactor or coenzyme).

A

Holoenzyme

130
Q

Specific site on the enzyme where substrate binds and catalysis occurs

A

Active Site

131
Q

An unstable high energy complex intermediate between the reactants and products formed by activated substrates and enzyme

A

Transition-state complex

132
Q

T/F Enzymes have extreme selectivity

A

TRUE

133
Q

Model by Emil Fischer that implied that enzymes are rigid

A

Lock and Key Model

134
Q

A more accepted model by Daniel Koshland that explains that the binding of a substrate to the enzyme induces a conformational change that is analogous to placing a hand to a glove

A

Induced Fit Model

135
Q

T/F Substrate molecules must come within bond-forming distance to interact

A

TRUE

136
Q

The ________ proximity of reactants, the higher the collision frequency, the faster the rate of reaction

A

Higher

137
Q

Type of Acid/Base Catalysis that only participating acids or bases are protons or hydroxide ions

A

Specific Acid/Base Catalysis

138
Q

Type of Acid/Base Catalysis that is responsive to all acids or bases present

A

General Acid/Base Catalysis

139
Q

Enzyme catalysis strategy where enzymes bind substrates in a conformation that weakens the bond targeted for cleavage through physical distortion and electronic polarization

A

Catalysis by Strain

140
Q

Enzyme catalysis strategy that involves formation of a covalent bond between enzyme and one or more substrate following a ping-pong mechanism

A

Covalent catalysis

141
Q

Ability to maintain a constant internal environment despite changes in external surroundings at the cellular level

A

Homeostasis

142
Q

2 Types of Mechanisms of Regulation

A

Passive & Active

143
Q

This allows intermediates to be directly transferred from one enzyme’s active site to another, minimizing the loss of energy and information

A

Compartmentalization

144
Q

Transfers electrons from NADPH to the next subunit

A

Cytochrome P450 Reductase

145
Q

Transfers the electrons to oxygen

A

Cytochrome P450

146
Q

In active regulation, one can increase or decrease the quantity of the enzyme via (2)

A

amount of enzyme being (1) synthesized and (2) degraded

147
Q

In active regulation, one can increase or decrease the catalytic activity of the enzyme via (2)

A

(1) allosteric regulation & (2) covalent modification

148
Q

Shutdown of enzyme synthesis through repressors

A

Repression

149
Q

Pathway for the control of enzyme degradation catalyzed by E3 ligases

A

ubiquitin-proteasome pathway

150
Q

2 prominent mechanisms of enzyme regulation to ensure a rapid response to meet the metabolic needs of cells

A

Allosteric Regulation & Covalent Modification

151
Q

Refers to the regulation of an enzyme through the binding of an activator or inhibitor molecule at a site other than the active site

A

Allosteric Regulation

152
Q

Allosteric effector that often bind to and either activate or inhibit one or more enzymes within their pathway

A

Feedback Effectors

153
Q

Metabolic end products or intermediates with a secondary role as allosteric effectors or enzyme

A

Indicator Metabolites

154
Q

Specialized allosteric ligands whose production or release is triggered in response to an external first messenger

A

Secondary Messengers

155
Q

Mechanism of enzyme regulation that introduces a new covalent bond or cleaving an existing covalent bond alters the identity of the affected enzyme

A

Covalent modification

156
Q

Type of Covalent modification where activated proteins retain their new form and properties until damaged, disposed, or degraded

A

Irreversible

157
Q

Example of irreversible covalent modification where proproteins transform into its active, functionally competent form

A

partial proteolysis

158
Q

Type of Covalent modification where one can restore modified protein to its modification-free precursor form

A

Reversible

159
Q

Most prominent form of covalent modification in cellular regulation accomplished by protein kinases and protein phosphatases working in opp directions

A

Phosphorylation

160
Q

Example of reversible covalent modification that involve histones, other nuclear proteins, and enzymes involved in core metabolic pathways

A

Acetylation

161
Q

enzymes that catalyze similar reactions, but differ slightly in their amino acid composition

A

Isozymes

Module 1B (7 decks)

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