Enzymes Flashcards

(42 cards)

1
Q

What do enzymes do to reactions

A

Catalyse them

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2
Q

Are enzymes globular or fibrous proteins

A

Globular

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3
Q

What is meant by the specificity of enzymes

A

Which biochemical reaction is catalysed by the enzyme

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4
Q

What are anabolic reactions

A

Where smaller molecules are joined together to make a larger one

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5
Q

What are catabolic reactions

A

Where larger molecules are broken down to form smaller ones

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6
Q

Which out of anabolic and catabolic reactions are catalysed by enzymes

A

Both

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7
Q

What is metabolism

A

Metabolism is the sum of all of the different reactions and reaction pathways happening in a cell or an organism, and it can only happen as a result of the control and order imposed by enzymes

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8
Q

What factors affect reaction rate

A

Temperature
Pressure
pH

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9
Q

What is Vmax of a reaction

A

The maximum rate of reaction

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10
Q

What is activation energy

A

The minimum amount of energy required for a reaction to occur

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11
Q

What are the 2 ways that enzymes reduce the required activation energy

A

Lock and key hypothesis
Induced-fit hypothesis

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12
Q

What is formed when enzymes and substrates join together

A

An enzyme-substrate complex

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13
Q

What do intracellular enzymes do

A

aid metabolic processes inside of both prokaryotes and eukaryotes

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14
Q

An example of an intracellular enzyme and what it does

A

Catalase ensures that hydrogen peroxide is broken down into oxygen and water, therefore preventing its accumulation

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15
Q

What do extracellular enzymes do

A

Break down larger nutrient molecules into smaller molecules in the process of digestion

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16
Q

An example of an extracellular enzyme and what it does

A

Amylase begins the digestion of starch in the mouth

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17
Q

What does trypsin do

A

An enzyme that catalyses the digestion of proteins into smaller peptides which can then be broken down further by other proteases

18
Q

What factors affect enzyme activity

A

Temperature
pH
Enzyme and substrate concentration

19
Q

What is temperature coefficient (Q10)

A

A measure of how much the rate of reaction increases with a 10 degree rise in temperature

20
Q

What is Q10 usually for an enzyme-controlled reaction

A

Usually around 2

21
Q

How are enzymes working at colder temperatures adapted

A

They are more flexible, especially at the active site. However it makes them more vulnerable to smaller temperature changes

22
Q

How are enzymes working at warmer temperatures adapted

A

The enzymes are more stable due to an increased number of bonds, particularly hydrogen and disulphide bonds

23
Q

Why does pH affect the shape of enzymes

A

A change in the concentration of H+ ions and OH- ions interfere with the shape of the tertiary structure

24
Q

Why is it important to control metabolic activity within cells

A

Important to regulate the rate and quantity of product formation

25
What effects does a competitive inhibitor have
Slows down the rate of reaction however does not impact the Vmax of a reaction
26
How can the effects of a competitive inhibitor be reduced
Add more substrate
27
What site does non-competitive inhibitors bind to
Allosteric site
28
How does a non-competitive inhibitor work
Binds to the allosteric site which causes the tertiary shape of the enzyme to change, therefore the shape of the active site changes
29
Example of irreversible non-competitive inhibitors
Proton pump inhibitors (PPIs) are used to treat long term indigestion. They irreversibly block an enzyme system responsible for secreting hydrogen ions into the stomach
30
What is end-product inhibition
When the product at the end of an enzyme-controlled reaction acts as an inhibitor to the enzyme that produces it
31
What kind of a feedback cycle is end-product inhibition
Negative feedback
32
What is an example of a reversible non-competitive inhibition
End-product inhibition
33
What is a cofactor
A cofactor is a substance that has to be present to ensure that an enzyme-catalysed reaction that takes place at the appropriate rate
34
What is a prosthetic group
Cofactors that are permanently bound to the protein
35
Example of a prosthetic group
Zn2+ ion in carbonic anhydrase, which is an enzyme necessary for the metabolism of carbon dioxide
36
Why can't the inhibitor be removed easily in a non-competitive inhibition
Strong covalent bonds are formed
37
Why can the inhibitor be removed more easily in a competitive inhibition
Weaker hydrogen or ionic bonds are formed
37
What are inactive precursor enzymes
Enzymes that are produced in an inactive form
38
What often needs to change shape in precursor enzymes for them to be activated
Active site
39
How do precursor enzymes become activated
By the addition of a cofactor
40
What is a precursor enzyme called before a cofactor is added
Apoenzyme
41
What is a precursor enzyme called after a cofactor is added
Holoenzyme