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Chapter 10 : Introduction to Metabolism Flashcards

(103 cards)

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
OILRIG is an acronym for what? (This isn't on the slides, but she said it in class and it was very helpful)
Oxidation Is Loss (of electrons) Reduction Is Gain (of electrons)
26
Electrons are moved through series of __________ _________ reactions, AKA _____ reactions (S17)
oxidation-reduction redox
27
Redox reactions consist of two half reactions: (S18)
One half functions as the electron-donating half (oxidation). The other as the electron-accepting half (reduction)
28
Nicotinamide adenine dinucleotide (NAD+) is an important electron acceptor in (S19)
Catabolism NAD+ is reduced to NADH
29
What is the cellular respiration redox equation? (S21)
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
30
Electron transport chain (S22)
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)
31
Each electron transport carrier is _______ and then ______, ready to continue catabolism and accept more electrons (S22)
reduced ; reoxidized Remember: Reduced means it gained electrons Oxidized means it lost electrons
32
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)
NAD+ ; NADH water
33
Electron _____ (NADH and FADH2) bring electrons to the electron transport chain (S24)
acceptors
34
What are two examples of electron acceptors that bring electrons to the electron transport chain? (S24) "Electron electron electron electron electron! UGH!!!" -Christina
NADH and FADH2 It's written in the slide before this one so if you got it wrong..... you're dumb hahahah! JK! - Christina
35
Electrons are carried from one carrier to the next until the _____ _______ is reached (_____) (S25)
Terminal carrier ; oxygen
36
Using several carriers releases energy from an energy source (glucose) in a __________ (S25)
controlled manner
37
In bacteria and archaeal cells, the ETC (electron transport chain) is found in the ____________ and _____________ (S26)
plasma membranes ; intracytoplasmic membranes
38
In eukaryotes, the ETC is found in the internal membranes of _______ and ______(S26)
mitochondria ; chloroplasts
39
Biochemical reactions are organized chemical reactions that produce __________ (S28)
metabolites
40
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)
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
41
Cyclic biochemical pathways require inputs to ______ _______ (S29)
continue running
42
Are biochemical pathways isolated from one another? (S30)
No. They are connected and form a complex network * Molecules flow into and out of many pathways that function in cells
43
Do exergonic reactions occur quickly or slowly without a catalyst? (S32)
They occur slowly and need the help of a biological catalyst to speed up chemical reactions
44
Ribozymes (S32)
RNA catalysts
45
Enzymes (S32)
protein catalysts
46
Enzymes are protein catalysts specific for the: (S33)
* reactions they catalyze, * molecules acted on, * product yielded
47
Catalyst (S34)
substance that increases the rate of a chemical reaction without being altered
48
Substrates (S34)
reacting molecules
49
Products (S34)
substances formed
50
Apoenzyme (S36)
the protein component enzyme that needs a nonprotein → cofactor
51
Cofactor (S36)
is a nonprotein component * Ex. Metal ions and organic molecules
52
Holoenzyme (S37)
complete enzyme that consists of the apoenzyme and the cofactor
53
Cofactor acts as a _______ when it is tightly or covalently bonded (S37)
prosthetic group
54
Coenzyme (S37)
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
Enzymes increase the rates of reactions, but do not ______ (S39)
alter the reaction
56
Activation energy (S40)
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
Enzymes speed up reactions by ____ the activation energy (S41)
lowering More substrate molecules will have the energy to come together and form products
58
Active site (catalytic site) (S42)
location on the enzyme where substrates come together
59
What forms an enzyme-substrate complex? (S42)
A joined enzyme and substrate
60
Induced fit model (S43)
the enzyme changes shape when it binds a substrate This ensures that the active site surrounds and perfectly fits the substrate
61
Substrate concentration can ___ enzyme activity in variable ways
alter
62
Enzyme saturation (S44)
too much substrate can result in all active site being filled * Max rate of the reaction
63
Every enzyme has an optimum ______ (S45-46)
pH and temperature
64
When the pH changes too much this can ____ enzyme activity or _____ the enzyme
slow ; damage
65
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)
denaturation ; disrupted ; bind
66
Competitive inhibitor (S47)
directly competes with a substrate of an enzymes active site
67
Competitive inhibitor prevents the enzyme from ________
forming the product Ex. Regulatory molecules or poisons
68
Sulfa drugs, like sulfonamide, act as _______________ (S48)
competitive inhibitors
69
Sulfa drugs are competitive inhibitors and resemble ______ (S48)
p-aminobenzoate (PABA)
70
What are p-aminobenzoate (PABA) used to form? (S48)
Folic acid
71
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)
active site Folic acid production is blocked, which inhibits the growth of the organism
72
Noncompetitive inhibitors (S49)
Inhibit enzyme activity by binding to a site on the enzyme other than the active site (allosteric site) * Ex. Heavy metals (mercury
73
Noncompetitive inhibitors alter the active sites shape making it _____ or _________ (S49)
inactive ; less active
74
Does the inhibitor directly compete for the active site? (S49)
No
75
True or false: Metabolism must be regulated to maintain homeostasis (S50)
True
76
Microorganisms have to regulate their metabolism to conserve _____ and _____ to keep cellular components balanced (S51)
materials ; energy
77
Microbes live in areas where nutrients, energy sources, and physical conditions → S51)
change quickly
78
Microbes constantly _____ their internal and external conditions (S51)
monitor
79
Microbes constantly monitor their internal and external conditions (S51)
metabolic pathways are influence by the localization of metabolites and enzymes into different parts of the cell
80
Metabolic channeling (S52)
metabolic pathways are influence by the localization of metabolites and enzymes into different parts of the cell
81
Compartmentalization is the most common form of (S52)
Metabolic channeling
82
Compartmentalization (S52)
Enzymes and metabolites are distributed to separate cell structures or organelles
83
Compartmentalization is important for eukaryotes because of their
many membrane-bound organelles
84
Fatty acids are broken down in _______ but are synthesized in the ______(S53)
mitochondria ; cytosol
85
Compartmentation occurs in the _____ and __________ of __________ bacteria (S54)
periplasm ; microcompartments ; Gram-negative
86
Compartmentation allows for ________ but ________ reactions to occur for regulation (S54)
simultaneous ; separate
87
Compartmentation coordinates pathway activities by transporting _________ and _________ between compartments (S54)
metabolites ; coenzymes
88
The rate of transcription and translation can be altered to control what? (S55)
the amount of enzymes present in a cell
89
An enzyme is not synthesized when it is (S55)
not needed If it is needed more are synthesized * Slow response, but saves the cell energy and → raw materials
90
Posttranslational regulation (S56)
the direct stimulation or inhibition of critical enzyme activity to alter a pathway * Some are reversible and other irreversible
91
Allosteric enzymes (S57)
regulator enzymes
92
Allosteric enzyme's activity is altered by (S57)
allosteric effectors
93
Allosteric effectors (S57)
reversibly binds to a regulatory site separate from the active site and changes the enzymes shape
94
Positive allosteric effectors _______ enzyme activity and negative effectors _____ enzyme activity (S57)
increase ; decrease
95
Covalent Modification of Enzymes (S58)
Reversible on and off switch that regulates regulatory enzymes Addition or removal of a chemical group (phosphate, methyl, or adenylyl)
96
What are the advantages of covalent modifications of enzymes? (S59)
Respond to more stimuli in varied/sophisticated ways Regulation of enzymes that catalyze covalent modification adds a second level of regulation
97
Inhibition of one or more critical enzymes in a pathway can alter ______ (S60)
the entire pathway
98
What does the pacemaker enzyme do? (S60)
catalyzes the slowest or rate-limiting reaction in the pathway
99
Usually the ____ reaction is catalyzed by a pacemaker enzyme (S60)
first
100
Feedback inhibition (end product inhibition) (S61)
ensure that the end products are produced equally
101
Feedback inhibition (end product inhibition) commonly occurs with ______ biochemical pathways. Use ______ enzymes at ______ points (S61)
branched ; regulatory ; branching
102
If an end product is in excess, it will inhibit the _________ on the branch leading to its formation (S62)
first enzyme
103
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)
first enzyme ; synthesis