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Biology 1 > Ch. 8 Review > Flashcards

Ch. 8 Review Flashcards

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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
Q

How can we speed up life reactions?

A

Catalysts in the form of ENZYMES

26
Q

Why can’t heat be a catalyst for cells?

A
  1. causes denaturing proteins
  2. no specificity
27
Q

Why do we use enzymes?

A
  1. they do not damage the cells
  2. they are SPECIFIC
28
Q

Catalysts effect the _______ of reaction, and they are ______ consumed

A

rate, not

29
Q

How does an enzyme overcome Ea without adding heat?

A

Enzymes reduce Ea

30
Q

Is ∆G affected by enzymes?

A

NO

31
Q

Enzymes cannot make an _______ reaction _________

A

unfavorable, favorable

32
Q

Enzymes are also (4)

A
  1. reusable
  2. work in both directions
  3. can be regulated (turned on/off)
  4. are typically PROTEINS
33
Q

True/False
Enzymes create endergonic reactions to exergonic reactions?

A

FALSE

34
Q

What are the ways enzymes reduce Ea (3)?

A
  1. orients two substrates
  2. puts stress on bonds
  3. creates a microenvironment
35
Q

What are the things that affect the RATE of an enzyme-catalyzed reaction (6)?

A
  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
Q

Of the things that effect enzyme rate, which change concentrations and which alter shape?

A

Concentration- enzyme and substrate concentrations

3-D shape- temperature, pH, binding of regulatory molecules

37
Q

Localizing in enzymes (3)

A
  1. in organelles
  2. as membrane proteins
  3. in multi-enzyme complexes
38
Q

Enzymes can be stronger due to what type of covalent bonds?

A

disulfide bonds

39
Q

If you denature an enzyme with heat, once it cooled can it be reused?

A

Yes, only if it refolds perfectly without sticking to other molecules

40
Q

What helps refold enzymes

A

chaperones

41
Q

What are the types of regulatory molecules?

A

Competitive inhibitors- binds to the active site

Noncompetitive inhibitors- binds to the allosteric site

42
Q

Competitive inhibitors

A
  • inhibitor blocks the substrate
  • inhibitor vs. substrate concentration determines who binds
43
Q

Noncompetitive inhibitors

A
  • [inhibitor] does not matter
  • changes shape of the active site
  • allosteric regulation can turn the enzyme on/off
44
Q

Competitive inhibitors ________ by concentration, noncompetitive inhibitors ________ by concentration

A

can be countered, cannot be countered

45
Q

Do all enzymes have an active site? Do all enzymes have an allosteric site?

A

Yes, No relatively few enzymes are needed to turn on/off

46
Q

Feedback inhibition involves

A

Turning off the enzyme with the product of the reaction

ex. threonine and isoleucine production

Biology 1 (9 decks)

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