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Jaspie - Biochemistry II > II - Enzymes and Bioenergetics > Flashcards

II - Enzymes and Bioenergetics Flashcards

1
Q

Protein catalysts that increase the velocity of a chemical reaction and are not consumed during the reaction they catalyze

A

Enzymes

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2
Q

Physically distinct enzymes which catalyze the same reaction

A

Isozymes

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3
Q

Catalyzes oxidations and reductions (transfers an electron from one molecule to another)

A

Dehydrogenase/Oxidoreductase

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4
Q

Catalyzes transfer of moieties such as glucosyl,methyl or phosphoryl groups

A

Transferase

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5
Q

Catalyzes hydrolytic cleavage of C-C, C-O, C-N and other bonds

A

Hydrolase

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6
Q

Catalyzes hydrolytic cleavage of C-C, C-O, C-N and other bonds by atom elimination, leaving double bonds

A

Lyase

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7
Q

Catalyzes geometric or structural changes within a molecule

A

Isomerase

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8
Q

Catalyzes the joining together of two molecules coupled to the hydroolysis of ATP

A

Ligase

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9
Q

Uses ATP to add high-energy phosphate onto a substrate

A

Kinase

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10
Q

Adds inorganic phosphate onto a substrate without using ATP

A

Phosphorylase

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11
Q

Removes a phosphate group from a substrate

A

Phosphatase

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12
Q

Adds a hydroxyl group (-OH) onto a substrate

A

Hydroxylase

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13
Q

Transfers CO2 groups with the help of biotin

A

Carboxylase

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14
Q

Relocates a functional group within a molecule

A

Mutase

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15
Q

Properties of Enzymes

A

contain an active site, efficient, specific, require cofactors, compartmentalized, regulated/inhibited

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16
Q

Substrate fits into the preformed active site

A

Lock & Key Model

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17
Q

Active site is slightly deformable to accomodate the shape of the substrate

A

Induced Fit Theory

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18
Q

Apoenzyme + Cofactor

A

Holoenzyme

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19
Q

Distinguished by their tight, stable incorporation into a protein’s structure by covalent or noncovalent forces

A

Prosthetic Groups

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20
Q

Binds in a transient, dissociable manner either to the enzyme or to a substrate

A

Cofactor

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21
Q

Serves as a recyclable shuttle (group transfer agent) that transports many substrates from their point of generation to teir point of utilization

A

Coenzyme

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22
Q

Why are enzymes compartmentalized?

A

To protect from inhibitors and to promote a favorable environment

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23
Q

Non-proteins required for enzyme function

A

Cofactors

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24
Q

Organic Cofactors

A

Coenzymes

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25
Q

Not required for enzyme function but can alter the rate of reaction

A

Effectors

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26
Q

Enzymes lower _____.

A

free energy of activation

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27
Q

Enzymes _____ the energy of the reactants and products , and the equilibrium of the reaction.

A

do not change

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28
Q

Describes how reaction velocity varies with substrate concentration

A

Michaelis-Menten Equation

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29
Q

Vi = (Vmax[S]) / (Km + [S])

A

Michaelis-Menten Equation

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30
Q

Enzymes that follow Michaelis-Menten kinetics have a _____ curve.

A

hyperbolic

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31
Q

Allosteric reactions have a _____ curve.

A

sigmoid

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32
Q

Tells you how fast the reaction is

A

Vi

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33
Q

The maximum velocity or the maximal number of substrate molecules converted to products per unit time

A

Vmax

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34
Q

The substrate concentration where Vi = Vmax/2

A

Km

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35
Q

High Km =

A

Low Substrate Affinity

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36
Q

Low Km =

A

High Substrate Affinity

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37
Q

Above Km - ___-order kinetics, rate ___ [S]

A

zero-order kinetics, rate not affected by [S]

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38
Q

Below Km - ___-order kinetics, rate ___ [S]

A

first-order kinetics, rate directly proportional to [S]

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39
Q

Reciprocal of Michaelis-Menten Equation

A

Lineweaver-Burk Plot

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40
Q

Used to calculate Km and Vmax

A

Lineweaver-Burk Plot

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41
Q

Determines the mechanism of action of enzyme inhibitors

A

Lineweaver-Burk Plot

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42
Q

Any substance that can diminish te velocity of an enzyme-catalyzed reaction

A

Enzyme Inhibitor

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43
Q

Similar to substrate, competes for the binding site and reversibly attaches to the enzyme

A

Competitive Inhibitor

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44
Q

Competitive Inhibitor: reversed by increased ___, Km - ___, Vmax - ___

A

reversed by increased [S], Km - increased, Vmax - not changed

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45
Q

Irreversibly binds to the allosteric site of the enzyme and changes the conformation of the binding site

A

Non-competitive Inhibitor

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46
Q

Non-competitive Inhibitor: reversed by increased ___, Km - ___, Vmax - ___

A

reversed by increased [E], Km - not changed, Vmax - lowered

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47
Q

Regulation of Enzyme Activity: change in substrate concentration

A

immediate

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48
Q

Regulation of Enzyme Activity: allosteric binding sites

A

immediate

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49
Q

Regulation of Enzyme Activity: covalent modification

A

immediate to minutes

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50
Q

Regulation of Enzyme Activity: induction/repression of enzyme synthesis

A

hours-days

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51
Q

The substrate itself serves as an effector

A

Homotropic Effector

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52
Q

The effector is different from the substrate

A

Heterotropic Effector

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53
Q

Fed State: Phosphorylated or Dephosphorylated?

A

Dephosphorylated

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54
Q

Fasting State: Phosphorylated or Dephosphorylated?

A

Phosphorylated

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55
Q

Transfer and utilization of energy in biologic systems

A

Bioenergetics

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56
Q

Measure of the heat content of the reactants and products

A

Enthalpy (ΔH)

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57
Q

Enthalpy (ΔH) is measured in ____.

A

joules (J)

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58
Q

Endothermic

A

(+) ΔH - needs heat

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59
Q

Exothermic

A

(-) ΔH - releases heat

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60
Q

Measure of the change in randomness or disorder of the reactants and products

A

Entropy (ΔS)

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61
Q

Entropy (ΔS) is measured in ____.

A

joules/Kelvin (J/K)

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62
Q

Change in Free Energy

A

ΔG = ΔH - TΔS

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63
Q

Standard Free Energy Change: ΔG under _____ conditions, reactants and products are _____ each, T is _____, pressure is _____

A

standard conditions, 1 mole, 25°C or 298K, 1 atm

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64
Q

The natural tendency for processes is to proceed from a state of ___ energy to a state of ___ energy.

A

high to low

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65
Q

Net loss of energy (exergonic), spontaneous - ΔG _ 0

A

ΔG < 0

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66
Q

Net gain of energy (endergonic), not spontaneous - ΔG _ 0

A

ΔG > 0

67
Q

Equilibrium, forward reactions = backwards reactions - ΔG _ 0

A

ΔG = 0

68
Q

(-) ΔH, (+) ΔS

A

spontaneous

69
Q

(+) ΔH, (-) ΔS

A

not spontaneous

70
Q

(+) ΔH, (+) ΔS

A

spontaneous at high T

71
Q

(-) ΔH, (-) ΔS

A

spontaneous at low T

72
Q

All ΔGs of a pathway are additive

A

Coupling Reactions

73
Q

“Energy Currency/Cash” of the cell, transfers free energy derived from substances of higher energy potential to those of lower energy potential

A

ATP - adenosine triphosphate

74
Q

ΔG of ATP → ADP + Pi

A

-7300 cal/mol or -7.3 kcal/mol

75
Q

ATP Production: Phosphoenolpyruvate

A

creates ATP

76
Q

ATP Production: Carbamoyl phosphate

A

creates ATP

77
Q

ATP Production: 1,3-bisphosphoglycerate to 3-phosphoglycerate

A

creates ATP

78
Q

ATP Production: Creatine phosphate

A

creates ATP

79
Q

ATP Production: ADP → AMP + Pi

A

requires ATP

80
Q

ATP Production: Pyrophosphate

A

made from ATP

81
Q

ATP Production: Glucose 1-phosphate

A

made from ATP

82
Q

ATP Production: Fructose 6-phosphate

A

made from ATP

83
Q

ATP Production: AMP

A

made from ATP

84
Q

ATP Production: Glucose 6-phosphate

A

made from ATP

85
Q

ATP Production: Glycerol 3-phosphate

A

made from ATP

86
Q

The greatest quantitative source of high energy phosphate in aerobic organisms

A

Oxidative Phosphorylation

87
Q

Free energy comes from successive oxidation of substances in the respiratory chain within mitochondria

A

Oxidative Phosphorylation

88
Q

The final substance to be reduced in oxidative phosphorylation

A

molecular oxygen

89
Q

Loss of Electrons

A

Oxidation

90
Q

Gain of Electrons

A

Reduction

91
Q

Done through coupling reactions where a phosphate group is transferred to ADP from another substance with a higher ΔG°

A

Substrate Level Phosphorylation

92
Q

“Bank” of the cell

A

ETC - Electron Transport Chain

93
Q

“Cheques” of the cell

A

NAD+, FAD

94
Q

Final common pathway by which electrons from different fuels of the body flow to oxygen

A

ETC - Electron Transport Chain

95
Q

Electron carrier which produces 3 ATP

A

NAD+ - Nicotinamide Adenine Dinucleotide

96
Q

Electron carrier which produces 2 ATP

A

FAD - Flavin Adenine Dinucleotide

97
Q

Electron carrier derived from B3 (niacin)

A

NAD+ - Nicotinamide Adenine Dinucleotide

98
Q

Electron carrier derived from B2 (riboflavin)

A

FAD - Flavin Adenine Dinucleotide

99
Q

NAD+ is derived from _____.

A

B3 (niacin)

100
Q

FAD is derived from _____.

A

B2 (riboflavin)

101
Q

Mitochondria: freely permeable to most molecules

A

outer membrane

102
Q

Mitochondria: impermeable to most molecules, selective

A

inner membrane

103
Q

Mitochondria: folds in the inner membrane

A

cristae

104
Q

Mitochondria: contains enzymes, mtDNA, mtRNA and mitchondrial enzymes

A

matrix

105
Q

“Tellers” of the ETC “Bank”

A

complexes

106
Q

Complex I

A

NADH Dehydrogenase

107
Q

Complex II

A

Succinate Dehydrogenase, accepts FADH2, part of the Kreb’s Cycle

108
Q

Coenzyme Q

A

Ubiquinone, lipid, only non-protein part of the ETC

109
Q

Complex III

A

Cytochrome b/c1 (Fe/heme protein)

110
Q

Cytochrome c

A

Fe/heme protein, mobile part of the ETC

111
Q

Complex IV

A

Cytochrome a/a3 (Cu/heme protein), where oxygen is reduced

112
Q

Complex V

A

ATP Synthase

113
Q

NADH Dehydrogenase

A

Complex I

114
Q

Succinate Dehydrogenase, accepts FADH2, part of the Kreb’s Cycle

A

Complex II

115
Q

Ubiquinone, lipid, only non-protein part of the ETC

A

Coenzyme Q

116
Q

Cytochrome b/c1 (Fe/heme protein)

A

Complex III

117
Q

Fe/heme protein, mobile part of the ETC

A

Cytochrome c

118
Q

Cytochrome a/a3 (Cu/heme protein), where oxygen is reduced

A

Complex IV

119
Q

ATP Synthase

A

Complex V

120
Q

Energy from oxidation of components in the respiratory chain is coupled to the translocation of hydrogen ions (H+/protons)

A

Mitchell’s Chemiosmotic Theory

121
Q

H= moves from inside to outside the inner mitochondrial membrane and accumulates in the intermembranous space

A

Mitchell’s Chemiosmotic Theory

122
Q

ETC generates an electrical gradient and a pH gradients across the inner mitochondrial membrane

A

Oxidative Phosphorylation

123
Q

Oxidative Phosphorylation: intermembranous space is more _____

A

positive

124
Q

Oxidative Phosphorylation: intermembranous space has ___ H+ ions

A

more

125
Q

Oxidative Phosphorylation: protons are driven ___ the mitochondrial matrix

A

towards

126
Q

Part of ATP Synthase that generates ATP from ADP and Pi

A

F1

127
Q

Part of ATP Synthase that acts as a channel where protons pass through

A

F0

128
Q

Anaerobic glycolysis is not enough for highly aerobic tissues like _____.

A

heart & nerves

129
Q

Stops electron flow from substrate to oxygen

A

ETC Inhibitor

130
Q

ETC Inhibitors: Barbiturate

A

Complex I

131
Q

ETC Inhibitors: Piericidin A

A

Complex I

132
Q

ETC Inhibitors: Amytal

A

Complex I

133
Q

ETC Inhibitors: Rotenone

A

Complex I

134
Q

ETC Inhibitors: Malonate

A

Complex II

135
Q

ETC Inhibitors: Carboxin

A

Complex II

136
Q

ETC Inhibitors: TTFA

A

Complex II

137
Q

ETC Inhibitors: Antimycin A

A

Complex III

138
Q

ETC Inhibitors: Dimercaprol

A

Complex III

139
Q

ETC Inhibitors: Cyanide

A

Complex IV

140
Q

ETC Inhibitors: Carbon monoxide (CO)

A

Complex IV

141
Q

ETC Inhibitors: Sodium Azide

A

Complex IV

142
Q

ETC Inhibitors: Hydrogen Sulfide

A

Complex IV

143
Q

Increase the permeability of the inner mitochondrial membrane so proton gradient is lost (ATP synthesis stops but ETC continues and produces heat)

A

Uncouplers

144
Q

Synthetic Uncouplers

A

2,4-dinitrophenol, aspirin

145
Q

Uncoupler Protein

A

thermogenin (brown fat)

146
Q

Directly inhibits Complex V so the proton gradient continues to rise but there is no escape valve for protons

A

ATP Synthase Inhibitors

147
Q

Example of ATP Synthase Inhibitor

A

Oligomycin

148
Q

Unstable products that are formed as byproducts of the ETC when molecular oxygen is partially reduced

A

Reactive Oxygen Species/Free Radicals: superoxide O2-, hydrogen peroxide H2O2, hydroxyl radical •HO

149
Q

Produced by neutrophils to kill phagocytosed bacteria

A

Reactive Oxygen Species/Free Radicals

150
Q

Increased during reperfusion injury due to the sudden burst of ETC activity with the introduction of oxygen

A

Reactive Oxygen Species/Free Radicals

151
Q

Denatures and precipitates proteins and other substrates

A

Reactive Oxygen Species/Free Radicals

152
Q

ROS Defense: Catalase

A

2H2O2 → 2H20 + O2

153
Q

ROS Defense: Peroxidase

A

H2O2 + AH2→ 2H2O + A

154
Q

ROS Defense: Superoxide Dismutase

A

2O2- + 2H+→ 2H2O + O2

155
Q

2H2O2 → 2H20 + O2

A

Catalase

156
Q

H2O2 + AH2→ 2H2O + A

A

Peroxidase

157
Q

2O2- + 2H+→ 2H2O + O2

A

Superoxide Dismutase

158
Q

Mitochondrial Diseases: Fatal Infantile Mitchondrial Myopathy

A

All Complexes

159
Q

Mitochondrial Diseases: MELAS (Mitochondrial Encephalopathy, Lactic Acidosis and Stroke-like episodes)

A

Complex I

160
Q

Mitochondrial Diseases: Kearns-Sayre Syndrome

A

Complex II

161
Q

Mitochondrial Diseases: Leber’s Hereditary Optic Neuropathy

A

Complex III

162
Q

Mitochondrial Diseases: Leigh’s Disease

A

Complex IV

163
Q

Mitochondrial Diseases: MERRF (Myoclonic Epilepsy with Ragged-Red Fibers)

A

Complex IV

Jaspie - Biochemistry II (15 decks)

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