1.9- ENZYME INHIBITION Flashcards

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1
Q

What are enzyme inhibitors?

A

substances that directly or indirectly interfere with functioning of active site of enzyme

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2
Q

What do enzyme inhibitors do?

A

reduce enzyme activity

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3
Q

What are two types of enzyme inhibitors?

A

competitive inhibitors

non-competitive inhibitors

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4
Q

What do competitive inhibitors do?

A

bind to active site of enzyme

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5
Q

What do non-competitive inhibitors do?

A

bind to enzyme at position other than active site

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6
Q

What shape do competitive inhibitors have?

A

molecular shape similar to that of the substrate

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7
Q

What does competitive inhibitors having a similar shape to the substrate allow them to do?

A

allow them to occupy the active site of an enzyme

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8
Q

Why do competitive inhibitors compete with the substrate?

A

as they can occupy the active site so compete for with substrate for available active sites

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9
Q

What determines the effect of the inhibitors on the enzyme activity?

A

difference between concentration of inhibitor and concentration of substrate

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10
Q

What happens when if the substrate concentration is increased?

A

effect of the inhibitor is reduced

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11
Q

Is the competitive inhibitor permanently bound to the active site?

A

no

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12
Q

What happens when the competitive inhibitor leaves?

A

another molecule can take its place

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13
Q

What could be the molecule that takes the place of the competitive inhibitor once it leaves?

A

a substrate or inhibitor molecule, depending on how much of each type is present

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14
Q

sooner or later what will happen?

A

all the substrate molecules will occupy an active site

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15
Q

What will make it longer for all the substrate molecules to occupy an active site?

A

greater the concentration of inhibitor

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16
Q

What enzyme and substrate does an example of a competitive inhibitor occur with?

A

a respiratory enzyme that acts on succinate

17
Q

What is another compound that can inhibit the respiratory enzyme?

A

malonate

18
Q

How can malonate inhibit the respiratory enzyme?

A

has a very similar molecular shape to succinate

19
Q

As the malonate has a very similar molecular shape to the succinate what is it able to do?

A

easily combines with the enzyme and blocks succinate from combining with the enzyme’s active site

20
Q

What is another example of an inhibitor and of what enzyme?

A

inhibition of enzyme transpeptidase by penicillin

21
Q

What do non-competitive inhibtors do?

A

attach themselves to the enzyme at binding site which is not the active site

22
Q

Upon attaching to the enzyme, what does the non-competitive do?

A

alters shape of enzyme

23
Q

What happens as the shape of the enzyme is altered due to the non-competitive inhibitor?

A

active site of shape changes

24
Q

What happens as the shape of the active site is changed?

A

substrate molecule can no longer occupy active site so enzyme cannot function

25
Q

Why does increasing the substrate concentration not decrease the effect of the inhibitor ?

A

substrate and inhibitor not competing for same site