FACTORS AFFECTING ENZYME ACTION Flashcards

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1
Q

What 2 things have to occur for an enzyme to work

A

1) come into physical contact with its substrate

2) have an active site that fits the substrate

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2
Q

What do we usually measure to see the progress of an enzyme-catalysed reaction

A

its time-course

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3
Q

What is a reactions time-course

A

how long it takes for a particular event to run its course

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4
Q

What are the 2 time-course changes are measured most frequently

A

1) formation of the products of the reaction

2) the disappearance of a substance

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5
Q

Explain the shape of the graph of enyme: substrate (as substrate decreases so does the amount of product formed, decreasing rate) using

A

1) at first=lots of substrate and no product
2) lots of substrate & lots of empty active sites
3) all substrates filled and substrate rapidly broken into product
4) as substrate breaks down = less substrate and more product
5) becomes more difficult for substrate to find empty active site (less substrate, more active site filled) so disappearance of substrate decreases & formation of product also decreases
6) at the end = no substrate left, so no product made

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6
Q

How do you find the rate of change of a graph

A

measuring the gradient at that point

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7
Q

How do you measure the gradient at that point

A

draw a tangent

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8
Q

What are the 5 factors that affect enzyme action

A

1) temperature
2) pH
3) enzyme concentration
4) substrate concentration
5) enzyme inhibition

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9
Q

In what way does temperature affect enzyme action

A

higher temperature = rate of reaction increases

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10
Q

Which 2 ways does temperature have this affect

A

1) Higher temperature = higher kinetic energy of molecules, meaning the molecules move around faster and are more likely to collide with each more often (enzyme & substrate).
2) Higher temperature = higher energy in collisions, so more likely to lead to a successful collision and therefore a reaction

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11
Q

What does temperature increase look like on a graph

A

rising curve up to a point

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12
Q

Draw a graph of the effect of a rise in temperature

A

rising curve (up to a point)

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13
Q

What happens if the temperature becomes too high

A

the enzyme action slows down as some hydrogen bonds are broken, far too high = denature

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14
Q

Why do enzymes denature

A

the heat breaks the hydrogen bonds in the tertiary structure of the enzyme meaning that the active site changes shape so the substrate no longer fits

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15
Q

Can denaturation be un-done

A

no

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16
Q

What is the optimum temperature

A

temperature that enzymes work best at

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17
Q

What is the optimum temperature for human enzymes

A

40 degrees C

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18
Q

Is the optimum temperature the same for all enzymes

A

no

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19
Q

For what 3 reasons might the human body be colder than the optimum temp for enzymes

A

1) more food would be required that would cancel out the benefits of higher metabolic rate
2) other proteins may be denatured at higher temperatures
3) an increased temperature during things such as illness might mean the enzymes are denatured

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20
Q

Why do birds have a higher body temperature than humans

A

they require more energy from metabolic reactions for flight

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21
Q

How does pH effect enzymes

A

at optimum pH = highest rate of enzyme-controlled reactions, extreme higher/ lower = enzymes denatured

22
Q

What is the pH of a solution

A

a measure of its hydrogen ion content

23
Q

How do you calculate pH

A

-log10(H+)

24
Q

Which 2 ways does pH alter enzyme action

A

1) changes the charges on the amino acids that make up the active site, so the substrate can no longer become attached to the active site
2) the H+ and OH- ions in acid & alkalis can break the ionic and hydrogen bonds that maintains the enzymes tertiary structure

25
Q

Is it common for pH changes to denature enzymes and why

A

no, because the fluctuations inside organisms are usually small

26
Q

What is the effect of enzyme concentration on the rate of reaction ( with limited amount of substrate throughout)

A

1) low enzyme con = too few active sites for substrate to bind so some wasted & less likely to collide = slower rate of reaction
2) intermediate enzyme conc = all substrate molecule can occupy active site & more likely to collide = higher rate of reaction
3) high enzyme conc = no further affect as all substrates have binded to active site

27
Q

When does the higher the concentration of enzyme always mean a higher rate of reaction

A

when the substrate concentration is not limited

28
Q

What does the graph of enzyme conc:rate of reaction look like (limited/ unlimited)

A
limited = straight line that levels off
un-limited = straight line
29
Q

What is the effect of substrate concentration on the rate of reaction (with limited conc. of enzyme)

A

1) low substrate conc = too few substrate to occupy all available active sites = rate is only half maximum possibility
2) intermediate substrate conc = all active sites occupied and more likely to collide = rate of reaction higher
3) high substrate conc = no effect, all active sites filled so active sites are ‘saturated’

30
Q

When is the highest rate of reaction of enzymes : substrate and why

A

initial rate (at the start) , because substrate is used up over time so rate decreases

31
Q

What are heat-loving bacteria

A

thermophilic

32
Q

What are thermophilic bacteria

A

heat-loving

33
Q

What are enzyme inhibitors

A

substances that directly/indirectly interfere with the functioning of the active site of an enzyme

34
Q

What do enzyme inhibitors do

A

decrease the enzyme activity

35
Q

How many types of enzyme inhibitors are there

A

2

36
Q

What are the types of enzyme inhibitors

A

1) competitive

2) non-competitive

37
Q

What are competitive inhibitors

A

molecules that have a similar shape to the substrate molecule

38
Q

What does the shape of the competitive inhibitor allow them to do

A

bind to the active site

39
Q

What do competitive inhibitors compete with

A

the substrate

40
Q

What do competitive inhibitors bind with

A

the active site

41
Q

What determines the effect of competitive inhibitors effectiveness and how

A

the concentration of substrate
higher conc of substrate = effect of inhibitor reduced
lower conc of substrate = effect of inhibitor increased

42
Q

Does the competitive inhibitor stay binded to the active site or does it leave, and what does this mean (refer to conc)

A

It leaves, meaning another molecule takes its place (high conc of substrate = more likely to be substrate)

43
Q

What is an example of a competitive inhibitor

A

respiratory enzyme that acts on succinate (substrate) - malonate (inhibitor) can inhibit the enzyme by binding to its active site because it has a similar shape to succinate

44
Q

What is a non- competitive inhibitor

A

molecule with a different shape to the substrate

45
Q

What does a non-competitive inhibitor do

A

attach themselves to the enzyme at a binding site (NOT active site) that causes the shape of the active site to change = substrate can no longer fit to form an enzyme-substrate complex

46
Q

Does increasing the substrate concentration effect the rate of reaction when a non-competitive inhibitor is present, & why

A

no, because they are not competing for the active site

47
Q

What is a metabolic pathway

A

series of reactions in which each step is catalysed by an enzyme

48
Q

What feedbacks can metabolic pathways have

A

negative & positive

49
Q

What do feedbacks in metabolic pathways result in & what is it known as

A

the concentration of any chemical being maintained realtively constant, known as end-product inhibition

50
Q

What type of inhibition is end-product inhibition usually

A

non-competitive