C3: Enzymes Flashcards

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1
Q

What are intracellular and extracellular enzymes?

A

Intracellular -> works inside cells
Extracellular -> works outside cells

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2
Q

How do enzymes speed up reactions?

A

by lowering activation energy

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3
Q

What is activation energy?

A

the energy needed to start a chemical reaction

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4
Q

What are the 3 ways in which enzymes lower activation energy?

A
  1. binding and orienting substrates
  2. rearranging electrons in a substrate
  3. straining substrate and forcing it to a transition state
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5
Q

What are endergonic and exergonic reactions?

A

Endergonic -> products contain more free energy than reactants
Exergonic -> products contain less free energy than reactants (releases energy in the form of heat)

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6
Q

What are anabolic and catabolic reactions?

A

Anabolic -> enzymes bring the substrate molecules together
Catabolic -> enzymes break substrates

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7
Q

What are the two hypotheses of enzymes’ mode of action?

A

Lock-and-key hypothesis: the substrate has to perfectly fit the active site
Induced-fit hypothesis: the enzyme/substrate can change shape to ensure a perfect fit (more efficient)

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8
Q

What type of proteins are enzymes?

A

globular proteins

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9
Q

What is a turnover number?

A

the number of substrate molecules transformed per second by one enzyme

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10
Q

Why are enzymes present in small amounts?

A

They have high molecular activity.

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11
Q

What factors affect reaction rates?

A

temperature, pH, enzyme concentration, and substrate concentration

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12
Q

How does temperature affect reaction rates?

A

At low temperatures, enzymes have low kinetic energy and do not react with substrates a lot. At high temperatures, enzymes denature. Enzymes have an optimum temperature where their reaction rate is the greatest.

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13
Q

What is the optimum temperature for most human enzymes?

A

40º C

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14
Q

How does pH affect reaction rates?

A

Each enzyme has its own optimum pH, and extremes of pH can denature them.

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15
Q

How do you measure the effect of an enzyme?

A

compare the non-catalyzed rate with the catalyzed rate

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16
Q

Why do we measure the initial rate of reaction?

A

to measure before factors like substrate concentration had time to change; reflects the graph

17
Q

What is affinity?

A

The attraction of enzyme to substrate

18
Q

What are the two types of reversible inhibitors, and how do they affect the rate of reaction?

A

Competitive inhibitors compete with substrates for the active site. Non-competitive inhibitors bind to an enzyme’s allosteric site, which alters the shape of the active site.

19
Q

What are free and immobilized enzymes?

A

Free enzymes are not bound and are free to add to solutions. Immobilized enzymes are bound to a stationary and insoluble material.

20
Q

What are the three advantages of using immobilized enzymes?

A
  1. There are no enzymes in the product
  2. They can be reused multiple times
  3. They have a greater tolerance of temperature and pH changes.