Enzymes Flashcards

1
Q

What is the function of enzymes?

A

Do not alter the equilibrium yet speed up the time that equilibrium is reached at.

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2
Q

Name the 2 enzyme mechanisms.

A

Induced fit.

Lock and key.

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3
Q

Explain the lock and key mechanism.

A

The active site is complementary to the substrate.

Each active site is shaped to hold a specific substrate.

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4
Q

Explain the induced fit mechanism.

A

The active site and the substrate don’t fit perfectly.

Once the substrate binds the active site shape alters and becomes complementary.

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5
Q

Most enzymes are what?

A

Proteins

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6
Q

What is the exception to most enzymes being proteins?

A

Ribozymes (catalytic RNA molecules)

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7
Q

Define free energy change.

A

The difference in energy from the reactants at the initial stage and the products at the final stage.

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8
Q

Define activation energy.

A

Amount of energy required to activate a reaction.

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9
Q

Define thermodynamic activation.

A

Increase in free energy.

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10
Q

Define thermodynamic inactivation.

A

When proteins become denatured.

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11
Q

Define Vmax.

A

Maximum reaction rate. Where all enzymes are saturated with substrate.

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12
Q

Define Km.

A

The concentration of substrate where the reaction rate is half its maximum.
Vmax divided 2 = Km.

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13
Q

Km is the …

A

Inverse measurement of affinity

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14
Q

Describe a low Km.

A

Enzyme is fully saturated with substrate. Happens quickly.

Remains at a fairly constant rate.

Lower the Km, higher the affinity for the substrate.

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15
Q

Describe a high Km.

A

Enzyme not fully saturated, relies on the concentration of he substrate.

Activity varies.

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16
Q

What is a competitive inhibitor?

A

A molecule that is structurally similar to the substrate and competes with it for the active site.

17
Q

How do competitive inhibitors affect Km and Vmax?

A

Vmax: Unaltered
Km: Lowered

18
Q

How can the effects of completive inhibitors be reversed?

A

Increasing the concentration of substrate.

19
Q

What is a non-competitive inhibitor?

A

A molecule that binds to an allosteric site on the enzyme,

20
Q

How do non-competitive inhibitors affect Km and Vmax?

A

Km: Unaltered.
Vmax: Decreased.

21
Q

What happens when modulators bind to enzymes?

A

Conformation changes occur.

22
Q

What is the effect of a positive modulator?

A

Increases the affinity for the active site. (Negative has the reversed effect)