Module 2 Section 4 - Cofactors and Enzyme Inhibition Flashcards

1
Q

What are cofactors

A

Substances that are non protein that are bound to enzymes to allow them to work

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2
Q

Some cofactors are

A

Inorganic molecules or ions

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3
Q

How do cofactors work

A

They work by helping the enzyme and substrate to bind together

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4
Q

Do cofactors participate in the reaction

A

No, so they aren’t used up or changed in any way by the reaction

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5
Q

What are coenzymes

A

Cofactors that are organic molecules

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6
Q

Do coenzymes participate in reactions

A

Yes, they participate in reactions and are changed by it

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7
Q

Coenzymes often act as….

A

Carriers, moving chemical groups between different enzymes.

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8
Q

Are coenzymes recycled

A

Yes, they are continually recycled during this process - vitamins are often sources of coenzymes

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9
Q

What is a prosthetic group

A

A cofactor that is tightly bound to the enzyme

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10
Q

How can enzyme activity be prevented

A

By enzyme inhibitors

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11
Q

What are enzyme inhibitors

A

Molecules that bind to the enzyme that they inhibit

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12
Q

Enzyme inhibition can be either

A

Competitive
Non competitive

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13
Q

What is a competitive inhibitor

A

Molecules that have similar shape to that of the substrate molecule

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14
Q

Why is it called competitive

A

Because they compete with the substrate molecules to bind to the active site, but no reaction takes place. They block the active site so the substrate doesn’t fit in

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15
Q

How much the enzyme is inhibited depends …

A

On the relative concentrations of the inhibitor and the substrate

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16
Q

If there’s high concentration of the inhibitor…

A

It’ll take up nearly all the active sites and hardly any of the substrate will get to the enzyme - decreasing rate of reaction

17
Q

If there’s a higher concentration of substrate….

A

Then the substrates chances of getting to an active site before the inhibitor increase meaning increasing substrate will increase rate of reaction

18
Q

Where do non competitive inhibitor molecules bind to

A

The allosteric site (away from the active site)

19
Q

Why does the non competitive inhibitor binding to the allosteric site cause

A

Causes the active site to change shape - so the substrate molecule no longer fits

20
Q

Why are non competitive inhibitors called non competitive

A

Because they don’t compete with the substrate molecules to bind to the active site because they are a different shape

21
Q

What difference will Increasing the substrate make to the rate of reaction on non competitive inhibition

A

Enzyme activity will still be inhibited

22
Q

Inhibitors can be ….

A

Reversible
Non-Reversible

23
Q

What does the reversibility of inhibitors depend on

A

The strength of the bonds between the enzyme and the inhibitor

24
Q

What is the reversibility if the bonds between the enzyme and inhibitor is strong covalent bonds

A

Non reversible, because the inhibitor can’t be removed easily

25
Q

What is the reversibility if the bonds between enzyme and inhibitor is weak hydrogen or ionic bonds

A

Reversible, the inhibitor can be removed

26
Q

Some drugs and metabolic poisons are….

A

Enzyme inhibitors

27
Q

Some medical drugs are enzyme inhibitors e.g.

A

Some Antiviral drugs - reverse transcriptase inhibitors
Some antibiotics - penicillin

28
Q

Metabolic poisons are often enzyme inhibitors e.g.

A

Cyanide
Malonate
Arsenic

29
Q

What are metabolic pathways regulated by

A

End-product inhibition

30
Q

What is a metabolic pathway

A

A series of connected metabolic reactions. The product of the first reaction takes part in the second and so on. Each reaction is catalysed by a different enzyme

31
Q

What is product inhibition

A

Enzymes that are inhibited by the product of the reaction they catalyse

32
Q

What is end-product inhibition

A

When the final product in a metabolic pathway inhibits an enzyme that acts earlier on in the pathway

33
Q

What is the reversibility of product and end-product inhibition

A

Reversible, so when the level of the product starts to drop, the level of inhibition will start to fall and the enzyme can start to function again - this means more product can be made

34
Q

Enzymes are sometimes synthesised as

A

Inactive precursors in metabolic pathways to prevent causing damage to cells e.g. proteases.

35
Q

Part of the precursor molecules…

A

Inhibits it’s action as an enzyme, once it is removed the enzyme becomes active