Chapter 10 : Introduction to Metabolism Flashcards

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1
Q

Note from Christina: Hi! I just wanted to clarify that “(S#)” is my way of telling you what slide the flashcard was made from. For example, (S42) means that the flashcard was made from slide 42. (Flip card for another quick note!)

A

I use a lot of underscores to create “fill in the blank” questions, but the amount of lines I put and the amount of words that there really are for that answer don’t always match up. Happy studying! :D

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2
Q

What is energy? (S3)

A

Capacity to do work

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3
Q

What is metabolism? (S3)

A

All chemical reactions that occur in an organism to sustain life

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4
Q

What is anabolism? (S4)

A

Synthesis (build-up) of larger molecules from smaller ones

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5
Q

What are four examples of anabolism? (S4)

A

Carbohydrates, lipids, proteins, nucleic acids

(These are all large molecules that were “built-up” by smaller molecules. An example of anabolism) - Christina

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6
Q

Does anabolism require or release energy? (S4)

A

Requires energy

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7
Q

What is catabolism? (S5)

A

Degradation (breakdown) of larger molecules into smaller one

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8
Q

Does catabolism require or release energy? (S5)

A

Releases energy

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9
Q

What is chemical work? Does it require energy? (S6)

A

Synthesizing complex biomolecules (polymers) from smaller molecules (monomers)

Require energy

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10
Q

What is transport work? Does it require energy? (S6)

A

Take up nutrients, expel wastes, and
maintain ion balances

Require energy

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11
Q

What is mechanical work? Does it require energy? (S6)

A

Cell motility and movement of structures within the cell

Require energy

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12
Q

What is an exergonic reaction? Is it a spontaneous or nonspontaneous reaction? Is there molecule breakdown or molecule synthesis in this reaction? (S7)

A

Chemical reactions where there is a release of free energy

Spontaneous reactions (catabolic)

Molecule breakdown (cellular respiration)

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13
Q

What is an endergonic reaction? Is it a spontaneous or nonspontaneous reaction? Is there molecule breakdown or molecule synthesis in this reaction? (S8)

A

Chemical reaction that requires an input of free energy to occur

Nonspontaneous (anabolic)

Synthesis of larger molecules

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14
Q

For living organisms the most useful, practical form of energy is ________ (S10)

A

ATP
(adenosine 5’-triphosphate)

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15
Q

ATP consists of: (S10)

A
  • Adenine nitrogenous base
  • Ribose sugar
  • Three → phosphates
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16
Q

ATP ____ endergonic and exergonic reactions. Why is this (S11)

A

Links

Cells have to breakdown (“spend”) ATP in order to
make (“earn”) ATP

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17
Q

ATP is a high _______ molecule (S12)

A

High energy

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18
Q

During a hydrolysis reaction, terminal phosphate bond in ATP
is broken, releasing energy. ATP is almost completely hydrolyzed into ____________________ and an ______________. (S12)

A

Adenosine diphosphate (ADP)

Orthophosphate (Pi)

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19
Q

ATP, ADP, and Pi form an energy cycle. Fill in the blanks below to explain how this energy cycle works! (S13)

Energy released from an ______ ______ (glucose) is used
to form ___ from ___ and __

Energy released from ATP _____ powers
______ processes”

A

Energy source ; ATP ; ADP ; Pi

hydrolysis ; endergonic

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20
Q

Oxidation-reduction (redox) reaction (S15)

A

Electrons are moving from an electron donor (reducing agent) to an electron acceptor (oxidizing agent)

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21
Q

Reducing agent (S15)

A

Electron donor

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22
Q

Oxidizing agent (S15)

A

Electron acceptor

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23
Q

Oxidation (S16)

A

The loss of electrons of an atom inn a chemical compound

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24
Q

Reduction (S16)

A

the gain of electrons of an atom in a chemical compound

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25
Q

OILRIG is an acronym for what? (This isn’t on the slides, but she said it in class and it was very helpful)

A

Oxidation
Is
Loss (of electrons)
Reduction
Is
Gain (of electrons)

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26
Q

Electrons are moved through series of __________ _________ reactions, AKA _____ reactions (S17)

A

oxidation-reduction

redox

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27
Q

Redox reactions consist of two half reactions: (S18)

A

One half functions as the electron-donating half (oxidation).
The other as the electron-accepting half (reduction)

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28
Q

Nicotinamide adenine dinucleotide (NAD+) is an important
electron acceptor in (S19)

A

Catabolism

NAD+ is reduced to NADH

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29
Q

What is the cellular respiration redox equation? (S21)

A

LOOK IT UP!!!!

Just messing around, but you really do need to look up what the “cell respiration formula” looks like or look at slide 21 because this app won’t let me do it. - Christina

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30
Q

Electron transport chain (S22)

A

series of electron carriers, electrons flow through

(The next few slides sound like gibberish if you don’t have the picture of how the electron transport chain works. Highly recommend this video
https://www.youtube.com/watch?v=zJNx1DDqIVo)

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31
Q

Each electron transport carrier is _______ and then ______, ready to continue catabolism and accept more electrons (S22)

A

reduced ; reoxidized

Remember:
Reduced means it gained electrons
Oxidized means it lost electrons

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32
Q

Glucose is a common organic energy source, it is oxidized (broken down, catabolized) to release electrons.

Electrons from glucose are picked up by
_____, reducing NAD+ to ____, which is
transferred to the electron transport chain

The goal is to reduce oxygen (terminal electron acceptor) into ____ (S23)

A

NAD+ ; NADH

water

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33
Q

Electron _____ (NADH and FADH2) bring electrons to the electron transport chain (S24)

A

acceptors

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34
Q

What are two examples of electron acceptors that bring electrons to the electron transport chain? (S24)

“Electron electron electron electron electron! UGH!!!” -Christina

A

NADH and FADH2

It’s written in the slide before this one so if you got it wrong….. you’re dumb hahahah! JK! - Christina

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35
Q

Electrons are carried from one carrier to the next until the _____ _______ is reached (_____) (S25)

A

Terminal carrier ; oxygen

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36
Q

Using several carriers releases energy from an energy source
(glucose) in a __________ (S25)

A

controlled manner

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37
Q

In bacteria and archaeal cells, the ETC (electron transport chain) is found in the ____________ and _____________ (S26)

A

plasma membranes ; intracytoplasmic membranes

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38
Q

In eukaryotes, the ETC is found in the internal membranes of _______ and ______(S26)

A

mitochondria ; chloroplasts

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39
Q

Biochemical reactions are organized chemical
reactions that produce __________ (S28)

A

metabolites

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40
Q

Biochemical reactions can be linear pathways, branch pathways, and cyclic pathways. The steps of a biochemical reaction [starting product (substrate), intermediates, and end product] are different on each of these pathways listed above. What do the steps of each pathway consist of? (S28-29)

A

Linear
-Starting product (substrate)
-Intermediates
-End product

Branch
-Starting product (substrate
-Intermediates
-More than one end product

Cyclic
-All of the molecules in the pathway are intermediates

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41
Q

Cyclic biochemical pathways require inputs to ______ _______ (S29)

A

continue running

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42
Q

Are biochemical pathways isolated from one another? (S30)

A

No. They are connected and form a complex network

  • Molecules flow into and out of many pathways that function in
    cells
43
Q

Do exergonic reactions occur quickly or slowly without a catalyst? (S32)

A

They occur slowly and need the help of a biological catalyst to speed up chemical reactions

44
Q

Ribozymes (S32)

A

RNA catalysts

45
Q

Enzymes (S32)

A

protein catalysts

46
Q

Enzymes are protein catalysts specific for the: (S33)

A
  • reactions they catalyze,
  • molecules acted on,
  • product yielded
47
Q

Catalyst (S34)

A

substance that increases the rate of a chemical
reaction without being altered

48
Q

Substrates (S34)

A

reacting molecules

49
Q

Products (S34)

A

substances formed

50
Q

Apoenzyme (S36)

A

the protein component enzyme that needs a nonprotein → cofactor

51
Q

Cofactor (S36)

A

is a nonprotein component

  • Ex. Metal ions and organic
    molecules
52
Q

Holoenzyme (S37)

A

complete enzyme that consists of the apoenzyme and the cofactor

53
Q

Cofactor acts as a _______ when it is tightly or covalently bonded (S37)

A

prosthetic group

54
Q

Coenzyme (S37)

A

loosely attached cofactor

  • Carry products from one reaction to
    another or transfer chemical groups
    from one substrate to another
  • Ex. Vitamins (riboflavin forms
    FAD)
55
Q

Enzymes increase the rates of reactions, but do not ______ (S39)

A

alter the reaction

56
Q

Activation energy (S40)

A

the amount of energy required to bring reacting molecules together

  • A+B →AB++→ C+D
  • Transition-state complex – reacting molecules come
    together in the→ correct way (AB++)
  • A and B will not be converted into C and D if they do
    not have the energy equivalent to → activation
    energy
57
Q

Enzymes speed up reactions by ____ the activation
energy (S41)

A

lowering

More substrate molecules will have the energy to come together and form products

58
Q

Active site (catalytic site) (S42)

A

location on the enzyme where substrates come together

59
Q

What forms an enzyme-substrate complex? (S42)

A

A joined enzyme and substrate

60
Q

Induced fit model (S43)

A

the enzyme changes shape when it
binds a substrate

This ensures that the active site surrounds and perfectly
fits the substrate

61
Q

Substrate concentration can ___ enzyme activity in variable ways

A

alter

62
Q

Enzyme saturation (S44)

A

too much substrate can result in all active site being filled

  • Max rate of the reaction
63
Q

Every enzyme has an optimum ______ (S45-46)

A

pH and temperature

64
Q

When the pH changes too much this can ____ enzyme
activity or _____ the enzyme

A

slow ; damage

65
Q

If the temperature rises above the optimum temperature _________ will occur, the enzyme’s structure will be ______, and the active site won’t be able _____ to the substrate. (S46)

A

denaturation ; disrupted ; bind

66
Q

Competitive inhibitor (S47)

A

directly competes with a substrate
of an enzymes active site

67
Q

Competitive inhibitor prevents the enzyme from ________

A

forming the product

Ex. Regulatory molecules or poisons

68
Q

Sulfa drugs, like sulfonamide, act as _______________ (S48)

A

competitive inhibitors

69
Q

Sulfa drugs are competitive inhibitors and resemble ______ (S48)

A

p-aminobenzoate (PABA)

70
Q

What are p-aminobenzoate (PABA) used to form? (S48)

A

Folic acid

71
Q

Both sulfa drugs and PABA compete for the _____ on the enzyme

If the sulfa drug binds to the active site, what will this inhibit? (S48)

A

active site

Folic acid production is blocked, which inhibits the
growth of the organism

72
Q

Noncompetitive inhibitors (S49)

A

Inhibit enzyme activity by binding to a site on the enzyme other than the active site (allosteric site)

  • Ex. Heavy metals (mercury
73
Q

Noncompetitive inhibitors alter the active sites shape making it
_____ or _________ (S49)

A

inactive ; less active

74
Q

Does the inhibitor directly compete for the active site? (S49)

A

No

75
Q

True or false:
Metabolism must be regulated to maintain homeostasis (S50)

A

True

76
Q

Microorganisms have to regulate their metabolism to
conserve _____ and _____ to keep cellular components balanced (S51)

A

materials ; energy

77
Q

Microbes live in areas where nutrients, energy sources,
and physical conditions → S51)

A

change quickly

78
Q

Microbes constantly _____ their internal and
external conditions (S51)

A

monitor

79
Q

Microbes constantly monitor their internal and
external conditions (S51)

A

metabolic pathways are influence
by the localization of metabolites and enzymes into
different parts of the cell

80
Q

Metabolic channeling (S52)

A

metabolic pathways are influence
by the localization of metabolites and enzymes into
different parts of the cell

81
Q

Compartmentalization is the most common form of (S52)

A

Metabolic channeling

82
Q

Compartmentalization (S52)

A

Enzymes and metabolites are distributed to separate
cell structures or organelles

83
Q

Compartmentalization is important for eukaryotes
because of their

A

many membrane-bound organelles

84
Q

Fatty acids are broken down in _______ but are
synthesized in the ______(S53)

A

mitochondria ; cytosol

85
Q

Compartmentation occurs in the _____ and
__________ of __________ bacteria (S54)

A

periplasm ; microcompartments ; Gram-negative

86
Q

Compartmentation allows for ________ but ________ reactions to occur for regulation (S54)

A

simultaneous ; separate

87
Q

Compartmentation coordinates pathway activities by transporting _________ and _________ between compartments (S54)

A

metabolites ; coenzymes

88
Q

The rate of transcription and translation can be altered to
control what? (S55)

A

the amount of enzymes present in a cell

89
Q

An enzyme is not synthesized when it is (S55)

A

not needed

If it is needed more are synthesized
* Slow response, but saves the cell energy and → raw
materials

90
Q

Posttranslational regulation (S56)

A

the direct stimulation or
inhibition of critical enzyme activity to alter a pathway

  • Some are reversible and other irreversible
91
Q

Allosteric enzymes (S57)

A

regulator enzymes

92
Q

Allosteric enzyme’s activity is altered by (S57)

A

allosteric effectors

93
Q

Allosteric effectors (S57)

A

reversibly binds to a regulatory site
separate from the active site and
changes the enzymes shape

94
Q

Positive allosteric effectors _______ enzyme activity and negative effectors _____ enzyme activity (S57)

A

increase ; decrease

95
Q

Covalent Modification of Enzymes (S58)

A

Reversible on and off switch that regulates regulatory
enzymes

Addition or removal of a chemical group (phosphate,
methyl, or adenylyl)

96
Q

What are the advantages of covalent modifications of enzymes? (S59)

A

Respond to more stimuli in varied/sophisticated ways

Regulation of enzymes that catalyze covalent
modification adds a second level of regulation

97
Q

Inhibition of one or more critical enzymes in a pathway can
alter ______ (S60)

A

the entire pathway

98
Q

What does the pacemaker enzyme do? (S60)

A

catalyzes the slowest or rate-limiting reaction in the pathway

99
Q

Usually the ____ reaction is catalyzed by a pacemaker
enzyme (S60)

A

first

100
Q

Feedback inhibition (end product inhibition) (S61)

A

ensure that the end products are produced equally

101
Q

Feedback inhibition (end product inhibition) commonly occurs with ______ biochemical pathways. Use ______ enzymes at ______ points (S61)

A

branched ; regulatory ; branching

102
Q

If an end product is in excess, it will inhibit the _________
on the branch leading to its formation (S62)

A

first enzyme

103
Q

If an end product is in excess, it will inhibit the _________
on the branch leading to its formation. Formation is regulated without affecting the _______ of other products (S62)

A

first enzyme ; synthesis