Overview of Enzymes Flashcards

1
Q

What is the main function of enzymes?

A

Lower the activation energy (EA) for a reaction.

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2
Q

Enzymes are biological catalysts. What is the significance of this?

A

Enzymes increase reaction rates which increases the amount of product formed per unit of time.

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3
Q

What are substrates?

A

Reactants acted upon by enzymes.

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4
Q

What is the active site of an enzyme?

A

Location where the substrate binds.

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5
Q

What is enzyme specificity?

A

The active site of an enzyme only binds a specific substrate.

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6
Q

What is an enzyme-substrate complex?

A

A complex formed when an enzyme and substrate bind tightly together.

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7
Q

What is activation energy?

A

The minimum amount of energy needed to start a chemical reaction.

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8
Q

Why is it so important for enzymes to lower activation energy (EA)?

A

Because it decreases the barrier for starting a reaction.

(If the energy barrier is lower, then the enzyme can catalyze the reaction much faster, thus increasing reaction rate.)

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9
Q

What does the induced fit model state?

A

A substrate binds to an enzyme and induces a conformational change in its active site, so that they are a complementary fit.

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10
Q

What are cofactors?

A

Inorganic molecules (or metal ions)

Example: minerals

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11
Q

What are coenzymes?

A

Organic molecules

Example: vitamins or vitamin derivatives

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12
Q

What is the main function of both cofactors and coenzymes?

A

Activate enzymes by inducing conformational changes.

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13
Q

What is a holoenzyme? Apoenzyme?

A

holoenzyme: An enzyme WITH its cofactor

apoenzyme: An enzyme WITHOUT its cofactor

(completely nonfunctional)

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14
Q

What is a zymogen?

A

An inactive form of an enzyme.

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15
Q

What is Vmax?

A

How fast an enzyme can catalyze a reaction.

(the rate of reaction when the enzyme is saturated with substrate)

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16
Q

What is Km (or Michaelis constant)?

A

Substrate concentration at which the reaction rate is equal to 1/2Vmax.

(Km = 1/2Vmax)

17
Q

When does saturation kinetics occur?

A

When Vmax has been reached.

Adding more substrate will NOT increase reaction rate, once Vmax has been reached.

18
Q

A low Km, has what kind of substrate affinity?

A

low Km = high substrate affinity

19
Q

A high Km, has what kind of substrate affinity?

A

high Km = low substrate affinity

20
Q

What is Km inversely proportional to?

A

Enzyme-substrate affinity

21
Q

What are the three main factors that affect the rates of enzymes?

A
  1. temperature
  2. pH
  3. salinity (increasing levels of salt can disrupt hydrogen and ionic bonds)
22
Q

What is the optimal temperature for enzymes in the human body?

A

37° C

[37°C = 98.6°F = 310 K]

23
Q

When does an enzyme or protein exhibit cooperativity?

A

When there are multiple binding sites or subunits.

Cooperativity results in a sigmoidal shape curve (s-shape).

24
Q

What is the Hill coefficient (nH)?

A

A measure of the cooperativity of substrate binding to an enzyme.

25
Q

For the Hill coefficient (nH), what does it mean if:

  • nH = 0
  • nH > 1
  • nH < 1
A
  • nH = 0 NO cooperativity
    • The enzyme follows normal M-M kinetics​.
  • nH > 1 positive cooperativity
    • ​i.e. hemoglobin binding with oxygen
  • nH < 1 negative cooperativity
    • If it’s essentially one ( such as 1.1, or 1.2) it is still considered negative cooperativity.
26
Q

What is an endergonic (or nonspontaneous) reaction?

A

A reaction that requires energy input.

ΔG > 0

27
Q

What is an exergonic (or spontaneous) reaction?

A

A reaction that releases energy.

ΔG < 0

28
Q

What occurs when a homogenous catalyst is not separated from products at the end of a reaction?

A

The products will be contaminated.

29
Q

How will the rate of a catalyzed reaction be affected if the solid catalyst is finely ground before being added to the reaction mixture?

A

The rate will be faster because a greater surface area of catalyst will be exposed.