Enzymes, inhibitors, pH Flashcards

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1
Q

What are enzymes?

A

biological catalysts that speed up the rate of metabolic reactions

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2
Q

What are enzymes made of?

A

made up of amino acids

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3
Q

What type of structure do enzymes have?

A

globular proteins with tertiary structure

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4
Q

What is the active site?

A

the part of the molecule where the substrate fits during a reaction

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5
Q

How does an active site lose it’s shape?

A

the bonds that hold the tertiary structure together (hydrogen bonds/disulphide bridges/ionic bonds) are broken so the shape changes

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6
Q

What does an enzyme’s 3D shape depend on?

A

the unique sequence of amino acids in the primary structure

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7
Q

What is activation energy?

A

the minimum amount of energy required for a reaction to take place

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8
Q

Why can the activation energy NOT be provided through heating in the body?

A

because the human body has a temperature of 37C, so enzymes lower the activation energy required

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9
Q

What are the two different types of models of enzyme action?

A

lock and key
induced fit

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10
Q

What is the lock and key model?

A

the active site and the enzyme are exactly complementary- fit together perfectly

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11
Q

What is the induced fit model?

A

the complementary substrate binds to the active site of the enzyme to form an enzyme-substrate complex. as the substrate binds the active site moulds around the substrate- it is not a perfect fit initially

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12
Q

What has to happen for enzymes to have an effect?

A

it has to come into contact with the substrate
it has to have a complementary active site to the substrate

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13
Q

What are the four factors impacting enzymes?

A

temperature
pH
substrate concentration
enzyme concentration

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14
Q

How does temperature impact the enzyme?

A

as temperature increases, so does the rate of enzyme activity (until the temperature surpasses the optimum temperature)

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15
Q

Why does the temperature impact the enzyme in this way?

A

the temperature increase means that the molecules have more kinetic energy, so move around faster, making the substrate more likely to collide with the active sites

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16
Q

Why does the enzyme denature after the temperature increases past the optimum temperature?

A

due to the fact that the molecules are vibrating so much that some of the bonds (like the ionic bonding) break, causing the active site to change shape so the enzyme-substrate complexes can no longer form

17
Q

How does pH impact the enzyme?

A

each enzyme has it’s own optimum pH, and the enzyme rates are the most efficient at the correct pH

18
Q

Why does the pH impact the enzyme in this way?

A

if the pH is too high or too low, then the H+ and OH- ions found in acid and alkalis can disrupt the ionic/hydrogen bonds that holds the tertiary structure in place, if this changes shape then enzyme-substrate complexes can no longer form

19
Q

How does substrate concentration impact the enzyme?

A

as the substrate concentration increases, so does the rate of enzyme activity, up to the saturation point

20
Q

Why does substrate concentration impact the enzyme in this way?

A

more substrate means more chance of collision between substrate and enzyme

21
Q

What is the saturation point and why does it stop the rate of reaction?

A

the saturation point is where all of the enzymes’ active sites are filled up by substrate, so no more enzyme-substrate complexes can be formed

22
Q

How does enzyme concentration impact the enzyme?

A

as the enzyme concentration increases, so does the rate of enzyme activity

23
Q

Why does the rate of enzyme activity slow down/stop despite the increase of enzyme concentration?

A

because as soon as all of the substrate is used, the amount of enzymes will not increase the rate of reaction anymore as there is no more substrate to form enzyme-substrate complexes

24
Q

Why is the body 37C?

A

any further increase (due to fever etc) would denature the enzyme

other proteins may be denatured at a higher temperature

additional food/energy required to sustain the body at a higher temperature would be too great

25
Q

What are enzyme inhibitors?

A

they slow down or stop enzyme reactions

26
Q

What are the two types of enzyme inhibitors?

A

competitive and non-competitive

27
Q

What is a competitive inhibitor and how does it stop the enzyme?

A

the competitive inhibitor is a similar shape to the substrate and so is able to ‘compete’ for the active site and hence block the substrate

28
Q

How do we reduce the effect of competitive inhibitors?

A

by increasing the substrate concentration

29
Q

What happens to the amount of product produced when competitive inhibitors are involved?

A

all of the product will still be produced but the time it takes to produce it slower

30
Q

What is a non-competitive inhibitor and how does it stop the enzyme?

A

the non-competitive inhibitor attaches to a site away from the active site and so this alters the shape of the active site, so the substrate is unable to bind and form enzyme-substrate complexes

31
Q

How do we reduce the effect of non-competitive inhibitors?

A

we cannot reduce the effect of non-competitive inhibitors by increasing the concentration of substrate as they are not competing for the same site

32
Q

What is largely controlled by non-competitive inhibitors?

A

metabolism

33
Q

How can the non-competitive inhibitors control reactions?

A

they can temporarily deactivate the enzyme when the product is not needed

34
Q

How do you calculate the pH of a solution?

A

-log(H+ concentration)

EXAMPLE=
H+ concentration is 3.28x10^-4 = -log(3.28x10^-4)
so the pH is 3.48

35
Q

How do you calculate the H+ ion concentration of a solution?

A

1x10^(-pH)

EXAMPLE=
pH is 3.6 =
1x10^(-3.6) = 2.51x10^4
so the H+ ion concentration is 2.51x10^4