Chapter 14- Enzyme Inhibition Flashcards

(41 cards)

1
Q

Inhibitors are substances that interfere with ______ by _______ enzymatic reactions

A

catalysis
slowing or halting

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2
Q

Two classes of inhibitors:

A
  • Reversible
  • Irreversible
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3
Q

Reversible inhibitors use _____ bonds that form ____ but break _____

A

weak
rapidly
easily

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4
Q

Which type of inhibitor does not permanently disable the enzyme?

A

reversible inhibitors

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5
Q

Reversible inhibitors come to an equilibrium with the enzyme to form ____

A

enzyme inhibitor complex (EI)

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5
Q

Irreversible inhibitors are known as:

A

enzyme inactivators

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5
Q

Irreversible inhibitors combine with enzymes through _____

A

strong (usually) covalent bond

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5
Q

An enzyme is ___ when paired with an irreversible inhibitor

A

permanently disabled

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6
Q

irreversible inhibitors are ______ dependent

A

time

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7
Q

for irreversible inhibitors, you cannot apply____

A

Michaelis-Menton kinetics

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8
Q

Depending on their nature, reversible inhibitors will effect____ or _____

A

Km
Vmax

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9
Q

Km and Vmax are measured in _______ which gives the ____

A

presence of inhibitor
apparent Km or Vmax

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10
Q

Competitive inhibitors _____ with substrate binding

A

compete

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11
Q

The substrate and competitive inhibitor are typically ____

A

mutually exclusive

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12
Q

Competitive inhibitors typically binds ____- to the enzyme

A

reversibly

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13
Q

The winner of the competition between competitive inhibitors and substrates depends on the ______

A

the concentration of each.

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14
Q

Competitive inhibitors bind to _____ but not to _____

A

free enzyme
ES complex

15
Q

Competitive inhibitors will _____ Km, because ____

A

increase
because there is no affinity for S when EI has been made which reduces affinity and increases Km

16
Q

Competitive inhibitors will ___ Vmax, because ____

A

not change
Vmax is the velocity of very high [S] which means inhibitor will not inhibit the enzyme bc it is out competed and doesn’t slow down the rxn

17
Q

Uncompetitive inhibitor is ____ of binding to free E

18
Q

Uncompetitive inhibitors only bind to the _____

19
Q

How do uncompetitive inhibitors inactivate the enzyme?

A

causes structural distortion of the active site

20
Q

Effect of low [S] on uncompetitive inhibitors

A

inhibitor cannot bind bc most enzyme are free, making the inhibitor ineffective

21
Q

Effect of high [S] on uncompetitive inhibitors

A

Inhibitor can bind bc most E is in ES complex, making the inhibitor effective.

22
Effect of high [Inhibitor] on competitive inhibitors
able to bind because [S] is out-competed which reduces [free Enzyme]
23
Effect of high [S] on competitive inhibitor
S out-competes inhibitor which makes it ineffective
24
Uncompetitive inhibitor effect on Km, why??
Decreases Km effectively reduces [ES] which pulls the equilibrium towards [ES]. This increases the amount of S that binds to E which increases the affinity
25
uncompetitive inhibitor effect on Vmax. Why?
Decrease Vmax inhibitor effective at high [S], effectively reduces [ES] and [E]. Vmax= K2[E]
26
Competitive inhibition effect on Lineweaver Burke plot:
- No incr in Km - No change in Vmax
27
Uncompetitive inhibition effect on Lineweaver Burke plot:
Both Km and Vmax are decreased leading to parallel lines
28
Noncompetitive inhibitors can bind to ___
either E or ES
29
Noncompetitive inhibitors will bind to _____
a site remote from the active site
30
Noncompetitive inhibitors prevent E from ___
turning substrate into product
31
With noncompetitive inhibitors, EI and ESI are ____
un reactive
32
Two classes of mixed inhibitors
1. pure noncompetitive 2. Mixed noncompetitive
33
Pure noncompetitive inhibitors
binding of I does not affect S binding (rare case)
34
Mixed noncompetitive inhibitors
binding of inhibitor reduces affinity of S for E (or ES)
35
How does pure noncompetitive inhibition affect Km and Vmax?
- Km is unchanged - Vmax is decreased
36
Why do pure noncompetitive inhbitors decrease Vmax?
reduces [ES] and [E] which reduces the total amount of enzyme, slowing the reaction
37
How does mixed noncompetitive inhibitors affect Km?
when K1K1' then Km decreases
38
How do mixed noncompetitive inhibitors affect Vmax?
Vmax is decreased in both cases of K1 and K1'