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Biology 111 > Chapter 8 > Flashcards

Chapter 8 Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

Metabolism

A

Totality of an organism’s chemical reactions

An emergent property, involves several molecules

Never reaches equilibrium, defining feature of life

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2
Q

Activation Energy

A

amount of energy needed to start a chemical reaction

EA

Usually supplied in form of heat from surroundings

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3
Q

Substrates

A

Reactant that the enzyme acts on

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4
Q

Catabolic Pathways

A

break complex molecules into simpler ones by releasing energy

ex. cellular respiration

Release free energy in a series of reactions

Catabolic reactions in cell provide energy to phosphorylate ADP

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5
Q

Anabolic Pathways

A

build complex molecules from simper ones by absorbing energy

ex. photosynthesis, synthesis of macromolecules

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6
Q

Closed System

A

isolated from surroundings

ex. liquid in thermos

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7
Q

Open System

A

energy and matter can be exhanged between system and surroundings

ex. organisms

Reactions in open systems (living cells) are constantly trying to reach equilibrium, but never do

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8
Q

First Law of Thermodynamics

A

“Energy can be transferred and transformed, but it cannot be created nor destroyed”

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9
Q

Second Law of Thermodynamics

A

“Every energy transfer or transformation increases the entropy (disorder) of the universe”

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10
Q

Free energy

A

energy that can do work when temperature and pressure are uniform (homeostasis)

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11
Q

Change in free energy and how it’s related to everything else

A

change in free energy = delta G (difference in free energy between products and reactants)

delta G = delta H - T delta S (change in entropy)

Free energy decreases, stability increases

As free energy decreases, work increases

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12
Q

Equilibrium

A

state of maximum stability

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13
Q

Spontaneous processes

A

don’t require energy input and can happen quickly or slowly

A process is spontaneous and can perform work only if it is moving towards equilibrium

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14
Q

Exergonic reaction

A

spontaneous, releases energy

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15
Q

Endergonic reaction

A

nonspontaneous, absorbs free energy from surroundings

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16
Q

3 main kinds of work by a cell

A

chemical, transport, mechanical

Powered by hydrolysis of ATP

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17
Q

Energy coupling

A

use of exergonic process to drive an endergonic one

(it’s how cell manage energy resources)

(mediated by ATP)

In the cell, the energy from the exergonic reaction of ATP hydrolysis can be used to drive an endergonic reaction

Overall, coupled reactions are exergonic

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18
Q

Composition of ATP

A

Adenosine triphosphate

Ribose (sugar), adenine (a nitrogenous base), and 3 phosphate groups (nucleotide)

Bonds can be broken by hydrolysis (energy is released)

Release of energy comes from chemical change (to a lower state of energy), not phosphate bonds themselves.

ATP + H2O -> ADP + Pi + energy

ATP is a renewable resource (add P to ADP)

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19
Q

How does ATP drive endergonic reactions?

A

Phosphorylation (transferring a phosphate group to some other molecule, like a reactant) (recipient molecule is now phosphorylated)

ex. Transport work - ATP phosphorylates transport proteins

Mechanical work - ATP binds noncovalently to motor proteins, then is hydrolyzed

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20
Q

Chemical potential energy

A

temporarily stored in ATP, drives most cellular work

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21
Q

Catalyst

A

chemical agent that speeds up reaction without being consumed by reaction

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22
Q

Enzymes

A

Enzymes are catalytic proteins

-ase endings are enzymes

Speed up reactions by lowering activation energy (does not affect delta G)

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23
Q

Polymerase

A

synthesis of DNA or RNA

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24
Q

Nuclease

A

destroy DNA molecule

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25
Q

Exonuclease

A

outside DNA molecules, cut DNA into specific pieces

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26
Q

RNase

A

destroys RNA

a nuclease

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27
Q

DNase

A

Destroys DNA

a nuclease

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28
Q

Proteinase K

A

destroys proteins

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29
Q

Transition State

A

when reactants absorb energy, they become unstable

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30
Q

Enzyme-substrate complex

A

when an enzyme binds to the substrate

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31
Q

Active site

A

the region on the enzyme where the substrate can bind (lock and key relationship)

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32
Q

Induced fit of a substrate

A

brings chemical groups of the active site into positions that enhance their ability to catalyze the reaction

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33
Q

The active sity of an enzyme lowers activation energy by:

A
  • orienting substrates correctly
  • straining substrate bonds
  • providing a favorable microenvironment
  • covalently bonding to a substrate
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34
Q

Process of substrate binding to an enzyme

A
  1. substrates enter active site; enzyme changes shape to completely enfold substrate (induced fit)
  2. substrates held in active site by weak interactions (hydrogen and ionic bonds)
  3. Active site can lower EA and speek up reaction
  4. Substrates converted to products
  5. Products are released
  6. Enzyme is now available for 2 new substrate molecules
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35
Q

What is enzyme activity affected by?

A

General environmental factors (temp, pH, chemicals), ions (Mg+ (DNA polymerase), K+ (Sodium-Potassium Pump))

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36
Q

ideal pH of cell

A

6.8 - 7.2 (aqueous solution)

3 (stomach)

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37
Q

Thermophillic

A

heat-tolerant

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38
Q

Trypsin

A

intestinal enzyme

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39
Q

Taq DNA polymerase

A

specific to thermophillic bacteria

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40
Q

Cofactors

A

nonprotein enzyme helpers, can be organic (coenzymes ->vitamins) or inorganic (a metal in ionic form)

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41
Q

Competitive Inhibitors

A

bind to the active site of the enzyme, competing w/ substance

42
Q

Noncompetitive Inhibitors

A

binds to a different part of the enzyme, causing it to change shape (modifying it) (not reversible) (makes active site less effective)

43
Q

How does a cell regulate metabolic activities?

A

By turning on/off genes that encode specific enzymes or by regulating activity of enzymes

44
Q

Allosteric Regulation

A

Inhibits OR stimulates enzyme activity

Happens when a regulatory molecule binds to a protein at one site and affects the protein’s function at another

Made from polypeptide subunits

Binding of activator stabilizes active from

Binding of inhibitor stabilizes inactive form

45
Q

Cooperativity

A

amplifies enzyme activity. Binding of 1 substrate to active site stabilizes favorable conformational changes at all other subunits

46
Q

Allosteric regulators

A

are attracive drug candidates for enyme regulation

47
Q

Inhibition of proteolytic enzymes (one that simply acts on proteins) called caspases

A

may help management of inappropriate inflammatory responses

48
Q

Cysteine

A

amino acid that contains sulfur

49
Q

Feedback Inhibition

A

end product of a metabolic pathway shuts down the pathway

Prevents a cell from wasting chemical resourses by synthesizing more product than needed

(conserves energy within system)

50
Q

Some enzymes act as ?

A

structural componenets of membranes

Eukaryotic: some reside in specific organelles (enzymes for cellular respiration in mitochondria)

51
Q

Totality of an organism’s chemical reactions

An emergent property, involves several molecules

Never reaches equilibrium, defining feature of life

A

Metabolism

52
Q

amount of energy needed to start a chemical reaction

EsubA

Usually supplied in form of heat from surroundings

A

Activation Energy

53
Q

Reactant that the enzyme acts on

A

Substrates

54
Q

break complex molecules into simpler ones by releasing energy

ex. cellular respiration

Release free energy in a series of reactions

Catabolic reactions in cell provide energy to phosphorylate ADP

A

Catabolic Pathways

55
Q

build complex molecules from simper ones by absorbing energy

ex. photosynthesis, synthesis of macromolecules

A

Anabolic Pathways

56
Q

isolated from surroundings

ex. liquid in thermos

A

Closed System

57
Q

energy and matter can be exhanged between system and surroundings

ex. organisms

Reactions in open systems (living cells) are constantly trying to reach equilibrium, but never do

A

Open System

58
Q

“Energy can be transferred and transformed, but it cannot be created nor destroyed”

A

First Law of Thermodynamics

59
Q

“Every energy transfer or transformation increases the entropy (disorder) of the universe”

A

Second Law of Thermodynamics

60
Q

energy that can do work when temperature and pressure are uniform (homeostasis)

A

Free energy

61
Q

change in free energy = delta G (difference in free energy between products and reactants)

delta G = delta H - T delta S (change in entropy)

Free energy decreases, stability increases

As free energy decreases, work increases

A

Change in free energy and how it’s related to everything else

62
Q

state of maximum stability

A

Equilibrium

63
Q

don’t require energy input and can happen quickly or slowly

A process is spontaneous and can perform work only if it is moving towards equilibrium

A

Spontaneous processes

64
Q

spontaneous, releases energy

A

Exergonic reaction

65
Q

nonspontaneous, absorbs free energy from surroundings

A

Endergonic reaction

66
Q

chemical, transport, mechanical

Powered by hydrolysis of ATP

A

3 main kinds of work by a cell

67
Q

use of exergonic process to drive an endergonic one

(it’s how cell manage energy resources)

(mediated by ATP)

In the cell, the energy from the exergonic reaction of ATP hydrolysis can be used to drive an endergonic reaction

Overall, coupled reactions are exergonic

A

Energy coupling

68
Q

Adenosine triphosphate

Ribose (sugar), adenine (a nitrogenous base), and 3 phosphate groups (nucleotide)

Bonds can be broken by hydrolysis (energy is released)

Release of energy comes from chemical change (to a lower state of energy), not phosphate bonds themselves.

ATP + H2O -> ADP + Pi + energy

ATP is a renewable resource (add P to ADP)

A

Composition of ATP

69
Q

Phosphorylation (transferring a phosphate group to some other molecule, like a reactant) (recipient molecule is now phosphorylated)

ex. Transport work - ATP phosphorylates transport proteins

Mechanical work - ATP binds noncovalently to motor proteins, then is hydrolyzed

A

How does ATP drive endergonic reactions?

70
Q

temporarily stored in ATP, drives most cellular work

A

Chemical potential energy

71
Q

chemical agent that speeds up reaction without being consumed by reaction

A

Catalyst

72
Q

Enzymes are catalytic proteins

-ase endings are enzymes

Speed up reactions by lowering activation energy (does not affect delta G)

A

Enzymes

73
Q

synthesis of DNA or RNA

A

Polymerase

74
Q

destroy DNA molecule

A

Nuclease

75
Q

outside DNA molecules, cut DNA into specific pieces

A

Exonuclease

76
Q

destroys RNA

a nuclease

A

RNase

77
Q

Destroys DNA

a nuclease

A

DNase

78
Q

destroys proteins

A

Proteinase K

79
Q

when reactants absorb energy, they become unstable

A

Transition State

80
Q

when an enzyme binds to the substrate

A

Enzyme-substrate complex

81
Q

the region on the enzyme where the substrate can bind (lock and key relationship)

A

Active site

82
Q

brings chemical groups of the active site into positions that enhance their ability to catalyze the reaction

A

Induced fit of a substrate

83
Q
  • orienting substrates correctly
  • straining substrate bonds
  • providing a favorable microenvironment
  • covalently bonding to a substrate
A

The active sity of an enzyme lowers activation energy by:

84
Q
  1. substrates enter active site; enzyme changes shape to completely enfold substrate (induced fit)
  2. substrates held in active site by weak interactions (hydrogen and ionic bonds)
  3. Active site can lower EA and speek up reaction
  4. Substrates converted to products
  5. Products are released
  6. Enzyme is now available for 2 new substrate molecules
A

Process of substrate binding to an enzyme

85
Q

General environmental factors (temp, pH, chemicals), ions (Mg+ (DNA polymerase), K+ (Sodium-Potassium Pump))

A

What is enzyme activity affected by?

86
Q

6.8 - 7.2 (aqueous solution)

3 (stomach)

A

ideal pH of cell

87
Q

heat-tolerant

A

Thermophillic

88
Q

intestinal enzyme

A

Trypsin

89
Q

specific to thermophillic bacteria

A

Taq DNA polymerase

90
Q

nonprotein enzyme helpers, can be organic (coenzymes ->vitamins) or inorganic (a metal in ionic form)

A

Cofactors

91
Q

bind to the active site of the enzyme, competing w/ substance

A

Competitive Inhibitors

92
Q

binds to a different part of the enzyme, causing it to change shape (modifying it) (not reversible) (makes active site less effective)

A

Noncompetitive Inhibitors

93
Q

By turning on/off genes that encode specific enzymes or by regulating activity of enzymes

A

How does a cell regulate metabolic activities?

94
Q

Inhibits OR stimulates enzyme activity

Happens when a regulatory molecule binds to a protein at one site and affects the protein’s function at another

Made from polypeptide subunits

Binding of activator stabilizes active from

Binding of inhibitor stabilizes inactive form

A

Allosteric Regulation

95
Q

amplifies enzyme activity. Binding of 1 substrate to active site stabilizes favorable conformational changes at all other subunits

A

Cooperativity

96
Q

are attracive drug candidates for enyme regulation

A

Allosteric regulators

97
Q

may help management of inappropriate inflammatory responses

A

Inhibition of proteolytic enzymes (one that simply acts on proteins) called caspases

98
Q

amino acid that contains sulfur

A

Cysteine

99
Q

end product of a metabolic pathway shuts down the pathway

Prevents a cell from wasting chemical resourses by synthesizing more product than needed

(conserves energy within system)

A

Feedback Inhibition

100
Q

structural componenets of membranes

Eukaryotic: some reside in specific organelles (enzymes for cellular respiration in mitochondria)

A

Some enzymes act as ?

Biology 111 (9 decks)

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