Ch. 8 Review Flashcards

(46 cards)

1
Q

What is metabolism?

A

all of the cells chemical reactions (biochemistry)

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2
Q

What are the metabolic pathways? What do they do?

A

anabolic- building of cells (growing)
catabolic- break down of nutrients

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3
Q

Need ______ to do ________

A

Catabolism, anabolism

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4
Q

What are the laws of thermodynamics? How do they relate to cells?

A
  1. Energy can only be TRANSFORMED
  2. disorder (S) of the universe increases

Cells must conform to BOTH

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5
Q

What is disorder (S)?

A

entropy, which is always increasing

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6
Q

what is the difference between enthalpy and entropy?

A

enthalpy- total heat content of a system

entropy- total disorderliness of a system

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7
Q

How much USABLE energy do we have?

A

Free energy which is the energy of the system that can do work (at uniform temp)

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8
Q

Define exergonic and endergonic reactions

A

exergonic- negative ΔG, ΔH decrease, ΔS increase
MORE stable, favorable rxn, SPONTANEOUS

endergonic- positive ΔG, ΔH increases, ΔS decreases
LESS stable, unfavorable rxn, NONSPONTANEOUS

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9
Q

In an endergonic reaction _______ are less stable than _______

A

products, reactants

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10
Q

If the system is at equilibrium? How does this relate to cells?

A
  1. ΔG=0
  2. system has MAX stability
  3. does no work

Cells are NEVER at equilibrium, they are dynamic, equilibrium= cell death

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11
Q

Hydrolysis is an _______ rxn

A

exergonic

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12
Q

Dehydration synthesis is an ________ rxn

A

endergonic

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13
Q

Catabolism is _______, anabolism is ______

A

exergonic, endergonic

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14
Q

What is ATP?

A

Adenosine Triphosphate
1. nucleotide used to make RNA
2. BASE is adenine
3. three phosphates
4. Ribose
ENERGY RICH

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15
Q

Where does the energy from ATP come from?

A

By releasing a terminal phosphate making ADP

*remember phosphate groups are negatively charged, the 3 phosphates are covalently bonded, when the break apart a lot of energy is released

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16
Q

ATP is broken by

A

Hydrolysis

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17
Q

What is the ATP breaking equation

A

ATP + H2O –> ADP + Pi + Energy
= -7.3kcal/mol

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18
Q

ATP hydrolysis is _____ in endergonic reactions

A

COUPLED

ex. glutamic acid and ammonia anabolism

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19
Q

What in the cells are endergonic?

A

chemical work (anabolism)
transport work (vesicles)
mechanical work (flagella, cilia, pseudopodia, muscle contraction, cell division)

20
Q

What in the cells are exergonic?

A

cellular respiration
fermentation

21
Q

Breaking bonds ________, forming bonds ________

A

requires, releases

22
Q

All reactions require _______ even exergonic ones

A

bond breaking and forming

23
Q

Is ATP enough to break bonds?

A

NO, breaking bonds TAKES energy

24
Q

All reactions have a _______

A

Energy barrier which makes reactions SLOW

25
How can we speed up life reactions?
Catalysts in the form of ENZYMES
26
Why can't heat be a catalyst for cells?
1. causes denaturing proteins 2. no specificity
27
Why do we use enzymes?
1. they do not damage the cells 2. they are SPECIFIC
28
Catalysts effect the _______ of reaction, and they are ______ consumed
rate, not
29
How does an enzyme overcome Ea without adding heat?
Enzymes reduce Ea
30
Is ∆G affected by enzymes?
NO
31
Enzymes cannot make an _______ reaction _________
unfavorable, favorable
32
Enzymes are also (4)
1. reusable 2. work in both directions 3. can be regulated (turned on/off) 4. are typically PROTEINS
33
True/False Enzymes create endergonic reactions to exergonic reactions?
FALSE
34
What are the ways enzymes reduce Ea (3)?
1. orients two substrates 2. puts stress on bonds 3. creates a microenvironment
35
What are the things that affect the RATE of an enzyme-catalyzed reaction (6)?
1. [substrate]= greater concentration of substrate means greater reaction rate 2. [enzyme]= greater concentration of enzyme increases reaction rate 3. temperature = higher temperature, faster reaction -every enzyme has an optimal temperature 4. pH= varies depending on enzyme - every enzyme has optimal pH 5. binding of regulatory molecules 6. localizing (proximity of enzyme to a pathway) ex. organelles localize
36
Of the things that effect enzyme rate, which change concentrations and which alter shape?
Concentration- enzyme and substrate concentrations 3-D shape- temperature, pH, binding of regulatory molecules
37
Localizing in enzymes (3)
1. in organelles 2. as membrane proteins 3. in multi-enzyme complexes
38
Enzymes can be stronger due to what type of covalent bonds?
disulfide bonds
39
If you denature an enzyme with heat, once it cooled can it be reused?
Yes, only if it refolds perfectly without sticking to other molecules
40
What helps refold enzymes
chaperones
41
What are the types of regulatory molecules?
Competitive inhibitors- binds to the active site Noncompetitive inhibitors- binds to the allosteric site
42
Competitive inhibitors
- inhibitor blocks the substrate - inhibitor vs. substrate concentration determines who binds
43
Noncompetitive inhibitors
- [inhibitor] does not matter - changes shape of the active site - allosteric regulation can turn the enzyme on/off
44
Competitive inhibitors ________ by concentration, noncompetitive inhibitors ________ by concentration
can be countered, cannot be countered
45
Do all enzymes have an active site? Do all enzymes have an allosteric site?
Yes, No relatively few enzymes are needed to turn on/off
46
Feedback inhibition involves
Turning off the enzyme with the product of the reaction ex. threonine and isoleucine production