Enzymes Flashcards

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1
Q

Enzymes

A
  • Globular proteins that act as catalysts
  • Lower the activation energy level (allows reactions to occur at lower temperatures)
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2
Q

Catalysts

A

Alter the rate of a chemical reaction without undergoing permanent change themselves

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3
Q

Why are enzymes effective in small amounts

A

Can be reused repeatedly

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4
Q

Activation energy

A

An energy barrier that must be overcome for the reaction to take place

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5
Q

Enzyme structure

A
  • Have a specific 3D shape that is due to its primary structure
  • Active site
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6
Q

Active site

A
  • A specific region of the enzyme that is functional
  • Made up of a relatively small number of amino acids
  • Forms a small depression within the much larger enzyme molecule
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7
Q

Substrate

A

Fits neatly into the active site to form an enzyme-substrate complex

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8
Q

Enzyme-substrate complex

A

The substrate molecule is held within the active site by bonds that temporarily form

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9
Q

Induced fit model of enzyme action

A
  • The enzyme and substrate interact
  • The proximity of the substrate (a change in the environment of the enzyme) leads to a change in the enzyme that forms the functional active site
  • The enzyme is flexible + can mould itself to the shape of the substrate
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10
Q

How does the presence of a substrate change the shape of the active site in the induced fit model?

A

Puts a strain on the substrate molecule which distorts a particular bond in the substrate + consequently lowers the activation energy needed to break the bond

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11
Q

What happens to the active site after the products are released

A

The active site reverts to its original shape

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12
Q

Limitation of the lock + key model

A

It is considered as a rigid structure

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13
Q

What has to occur for an enzyme to work?

A
  • Come into physical contact with its substrate
  • Have an active site which fits the substrate

Factors that influence the rate of enzyme activity, affect these 2 things

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14
Q

How to measure an enzyme-catalysed reaction

A
  • Measure its time-course (how long it takes for a particular event to run its course)
  • Measure the formation of the products of the reaction (amount)
  • Measure the disappearance of the substrate (concentration)
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15
Q

Graph: x-axis = time, y-axis = volume of gas produced

A

Upwards curve

  1. At first there is a lot of substrate and no product
  2. It is very easy for substrate molecules to come into contact with empty active sites on the enzyme molecule
  3. Amount of substrate starts to decrease as its broken down -> increases amount of product
  4. More difficult for substrate to come into contact with enzyme due to product getting in the way
  5. Takes longer for substrate to be broken down so graph becomes plateued
  6. All substrate has been used up and no new product can be produced
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16
Q

How to measure the rate of change on a graph

A

Gradient of tangent at a given point

17
Q

What do you have to do when investigating the effect of a certain variable

A

Keep all other variables constant

18
Q

Factors that effect enzyme action

A
  • Temperature
  • pH
  • Enzyme concentration
  • Substrate concentration
19
Q

Effect of temperature on enzyme action

A
  • increases K.E. of molecules -> move around more rapidly + more frequent collisions = more successful collisions
  • increasing temp. causes bonds in enzyme structure to break -> enzyme starts to change shape -> substrate fits less easily into the changed active site
  • After a certain temperature, enzyme becomes denatured
20
Q

Denaturation

A

Permanent change of the enzyme that stops it from functioning altogether

21
Q

Why is human body temperature slightly lower than optimum temperature of enzymes

A
  • More energy would be needed to maintain a high temp.
  • Any further rise in temp. (e.g. during illness) would denature the enzymes
22
Q

What does body temperature of an organism depend on

A

Its activity

  • More active organisms have a higher metabolic rate so higher temp.
23
Q

Effect of pH on enzyme action

A
  • Change in pH alters the charges on the amino acids that make up the active site
  • Depending on the significance of the change in pH, the bonds of the tertiary structure may break
24
Q

Effect of enzyme concentration on the rate of reaction

A
  • Low enzyme concentration: Too few enzymes to allow all substrate molecules to have an active site

Intermediate enzyme concentration: All substrate molecules can occupy an active site

High enzyme concentration: The addition of further enzymes has no effect on rate of reaction (graph is plateued)

25
Q

Graph of effect of enzyme concentration on the rate of reaction

A

x-axis: enzyme conc.
y-axis: rate of reaction

26
Q

Effect of substrate concentration on the rate of enzyme concentration

A

Low substrate concentration: There are too few substrates to fill all active sites

Intermediate substrate concentration: all active sites are occupied at one time. Maximum

High substrate concentration: The addition of more substrate has no effect as all active sites are occupied at one time

27
Q

Graph of effect of substrate concentration on the rate of enzyme concentration

A

x-axis: substrate concentration
y-axis: rate of reaction

28
Q

Enzyme inhibitors

A

Directly or indirectly interfere with the functioning of the active site

29
Q

Types of enzyme inhibitors

A
  • Competitive inhibitors
  • Non-competitive inhibitors
30
Q

Competitive inhibitors

A
  • Have a molecular shape similar to that of a substrate
  • So compete with the substrate for the available active sites
  • Not permanently bound
31
Q

How can the effect of a competitive inhibitor be reduced?

A

Increase substrate concentration

32
Q

Non-competitive inhibitors

A
  • Attach to the enzyme on a binding site which is not the active site -> alters the shape of the enzyme and so its active site as well
  • Permanently stops the enzyme from functioning