Energy and Enzymes Flashcards

1
Q

Energy (what it is and forms)

A
  • a force that can accomplish work
  • 2 major forms
    • potential
    • kinetic
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2
Q

Potential energy (what it is and examples)

A
  • energy of position (stored energy)

- ex: chemical energy (in bonds)

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3
Q

Kinetic energy (what it is and example)

A
  • energy of motion

- ex: mechanical energy

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4
Q

Metabolism (what it is and types)

A
  • sum of all chemical reaction in a living organism
  • includes
    • anabolism
    • catabolism
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5
Q

Anabolism

A
  • Biosynthesis reactions: building

- Endergonic: requires energy

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6
Q

Catabolism

A
  • degrative reactions: breaking down

- exergonic: energy releasing

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7
Q

Chemical reactions (components and directions)

A
Components:
  -Substrate: what goes in (reactant)
  -product: what comes out
Directions:
  -Forward
  -reverse
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8
Q

Factors affecting chemical reactions

A
  1. law of mass action
  2. activation energy
  3. enzymes
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9
Q

Law of mass action

A
  • forward reactions
  • higher reactants= higher products
  • high product= slow down making of product
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10
Q

Activation energy

A
  • minimum energy required for reactants to overcome activation energy barrier –> transition state –> product
  • Sources:
    • collision from other molecules
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11
Q

Enzymes (structure, function)

A
Structure:
  -protein based molecules
  -substrate specific 
Function:
  -reduce activation energy
  -biological catalysts:
      -speed up reactions
      -does not get used up or changed
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12
Q

Models for Enzyme Binding

A
  1. lock and key mechanism

2. induced fit model

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13
Q

Lock and key mechanism

A
  • substrate fits an enzyme like a key to a lock

- problem: doesn’t explain reversible reactions

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14
Q

Induced fit model

A
  • substrates approximately fit enzyme

- after binding –> conformational change for a better fit

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15
Q

How enzymes work (steps)

A

-enzyme binds with a substrate converting them to products

  1. substrate contacts active site of the enzyme
  2. enzyme- substrate complex forms
  3. substrate is transformed, broken down, or compounded with other substrates
  4. transformed substrate (products) released
  5. unchanged enzyme free to interact with other substrates
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16
Q

Enzyme sites

A
  1. active site: where substrate binds

2. allosteric site: where molecules other than the substrate bind

17
Q

Types of enzymes

A
  1. simple enzymes: proteins with catalytic activity

2. holoenzymes: conjugated enzymes

18
Q

Holoenzymes (protein and nonprotein portion)

A

Protein portion: apoenzyme
nonprotein portion:
-cofactor: inorganic ions (zinc, iron, magnesium, calcium)
-coenzyme: organic molecules (vitamins/minerals) ex: NAD+, NADP+, FAD, coenzyme A

19
Q

Factors influencing enzymatic rate (6)

A
  1. enzyme concentration
  2. substrate concentration
  3. temperature
  4. pH
  5. enzyme catalytic rate
  6. affinity
20
Q

Enzyme catalytic rate

A

inherent speed of an enzyme

21
Q

Substrate concentration

A

increasing substrate, increasing activity until saturation

-saturation: enzymes active sites are filled with substrate

22
Q

Enzyme concentration

A

increase in enzymes= increase in maximum rate

23
Q

Affinity

A

How tightly a substrate binds to an active site

high affinity –> increase reaction rates

24
Q

Temperature

A
  • enzymes have an optimal temperature
  • increases rate of collision and reaction
  • too much –> denature enzyme
25
Q

pH

A
  • enzymes have an optimal pH

- extreme pH (acidic or basic) –> denature enzyme

26
Q

Enzyme regulation

A
  1. allosteric regulation

2. inhibitors

27
Q

Allosteric regulation (what it is and examples)

A

-modulators weakly bind to allosteric site

  1. activator: increase catalytic rate, increase affinity to substrate
  2. inhibitor: decreases enzymatic activity
28
Q

Inhibitors

A
  1. competitive: chemicals that bind to the active site
    ex: penicillin, sulfanilamide
  2. non-competitive: chemicals that bind to the allosteric site or cofactors
    ex: cyanine, fluoride