Chapter 15 Flashcards

(34 cards)

1
Q

First Stage of the Generation of Energy from Food

A

large molecules in food are broken down into smaller molecules in the process of digestion

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2
Q

Second Stage of the Generation of Energy from Food

A

the many small molecules are processed into key molecules of metabolism, most notably acetyl CoA

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3
Q

Third Stage of the Generation of Energy from Food

A

ATP is produced from the complete oxidation of acetyl CoA

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4
Q

Energy is needed for:

A
  • Movement: muscle contraction, cells
  • Active transport: molecules and ions
  • Biosynthesis: building complex molecules
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5
Q

Ultimate energy source

A

phototrophs: capture and transform sunlight energy
chemotrophs: get energy from oxidizing carbon fuel

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6
Q

Energy currency

A
  • all “LIFE” uses ATP to link energy release and energy use
  • carbon fuel oxidation generates ATP
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7
Q

Metabolic Pathways

A
  • Stepwise reactions breaking down or synthesizing molecules
    • Reaction types actually limited
      - Often common intermediates
  • Typically defined by a specific substrate getting converted to a specific end point
    Example: glucose into: pyruvate or acetyl-CoA or CO2, water and ATP
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8
Q

Intermediary Metabolism

A
  • Pathways interact with other pathways
    - All reactions within a cell considered “Intermediary Metabolism”
  • Traditionally studied as isolated pathways
    - Then linked by defining key interaction points
    - “Systems biology” is an emerging field that attempts
    to study the pathways all at once
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9
Q

Catabolic

A

metabolic pathway: converts energy from fuel to ATP
ex: glycolysis

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10
Q

Anabolic

A

metabolic pathway: requires energy for synthesis
ex: gluconeogenesis

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11
Q

Catabolic and anabolic pathways

A
  • share reactions (enzymes)
  • but there will be key, regulated, irreversible reactions for distinct pathways
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12
Q

Amphibolic Pathways

A
  • Pathways that can be catabolic or anabolic
    depending on situation
    - TCA Cycle convert Acetyl-CoA to energy
    - TCA cycle providing carbon backbones for
    synthesis
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13
Q

Thermodynamics of Pathways

A
  1. Each reaction must be specific in the pathway
  2. Overall pathway must be thermodynamically favourable
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14
Q

ATP: High-Energy Phosphates

A
  • Phosphoryl groups in cellular compounds
  • The hydrolysis of ATP is exergonic because the triphosphate
    unit contains two phosphoanhydride bonds that are unstable
  • The energy released on ATP hydrolysis is used to power a host of cellular functions
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15
Q

ATP: Energy yield

A

Phosphoanhydrides have more energy than phosphoesters
- High phosphoryl-transfer potential

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16
Q

Four Factors that contribute to phosphoryl transfer potential

A
  1. Electrostatic repulsion
  2. Resonance stabilization
  3. Increase in entropy
  4. Stabilization due to hydration
17
Q

Electrostatic Repulsion

A
  • At pH 7.4, phosphates have negative charges
    - Triphosphate of ATP carries 4 negative charges
    - Negative charges repel each other
    - Anhydride (ADP and ATP) have more repulsion
    - Ester (AMP) bond has less repulsion
18
Q

Resonance stabilization

A
  • Ability to share electrons across the molecule
    - More sharing = Lower energy state
  • Orthophosphate (Pi): Individual phosphate allows more sharing of electrons
  • ATP: When phosphates have anhydride bond, the electron sharing is
    reduced compared with individual phosphates
    - One oxygen not able to form O=O
19
Q

Increase in Entropy

A
  • Hydrolysis of ATP generates 2 molecules instead of one molecule, which increases entropy
  • A water molecule is lost?
    - But the system already has a high concentration of water (55.5M)
    - Losing one water molecule has essentially no effect
20
Q

Stabilization due to Hydration

A
  • Ability of water to hydrogen bond to molecule
  • More hydrogen bonds possible with ADP and Pi versus ATP
    • More stabilization
    • Inhibits reverse reaction to form ATP
21
Q

ATP: Energy yield

A

High phosphoryl-transfer potential
- Ability to transfer phosphate groups
- ATP has phosphoryl-transfer potential that is intermediate
- Act as a carrier of phosphoryl groups

22
Q

Clinical Insight: Exercise and Energy

A

Resting muscle [ATP] = 4mM
[Creatine phosphate] = 25mM
- Amount of muscle ATP used rapidly
- Higher amount of creatine phosphate
- Creatine phosphate has high phosphoryl-transfer potential
- Buffers (regenerates) ATP; eventually creatine phosphate depleted
- Anaerobic support
- Followed by increasing need for aerobic support

23
Q

Carbon Oxidation is Paired with

A
  • Oxidation reactions involve loss of electrons; must be paired with reactions that gain electrons, reduction reactions
  • carbon atoms in fuels are oxidized to yield CO2, and the electrons are ultimately
    accepted by oxygen to form H2O.
  • more reduced a carbon atom is, the more free energy is released upon oxidation.
24
Q

What is a more efficient food source

A
  • Fats are a more efficient food source than glucose because fats are more reduced
25
Reduced compounds
- can oxidize to release electrons - Electrons power the electron transport chain to make energy
26
Oxidized compounds
- have already lost electrons - Limited ability to power the electron transport chain
27
Two characteristics are common to activated carriers
1. The carriers are kinetically stable in the absence of specific catalysts 2. The metabolism of activated groups is accomplished with a small number of carriers
28
Activated carriers
- NADH and FADH2 → activated electron carriers for fuel oxidation - NADPH → Activated electron carriers for synthesis - Coenzyme A → Activated 2-carbon carrier
29
Activated Carriers: NADP+
* NADP+: Differs from NAD+ by a phosphoryl group * NADPH * supplies electrons for reduction power during biosynthesis * making fatty acids requires reducing methylene groups as acetyl groups are added
30
Other Carriers
- The B vitamins function as coenzymes. - Vitamins A, C, D, E, and K play a variety of roles but do not serve as coenzymes.
31
Metabolic Processes Are Regulated
1. Amount of enzyme 2. Regulate enzyme activity 3. Substrate accessibility
32
Amount of enzyme
- Change gene expression to make more/less enzyme - Enzyme degradation (proteases)
33
Regulate enzyme activity
- Allosteric regulation - Covalent modification ie. phosphorylation - Tied to ATP (energy status) - Second messenger regulation
34
Substrate accessibility
- Compartmentalization of reactions in different locations - Flux between compartments controlled