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Biology - biological molecules + cells > 3.1.4.2 Many Proteins are Enzymes > Flashcards

3.1.4.2 Many Proteins are Enzymes Flashcards

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1
Q

What do enzymes do in living cells

A

Control reactions

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2
Q

What do enzymes do

So what are they

A

Speed up reactions

Biological catalysts

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3
Q

What do enzymes not do to reactions

A

Cause then

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4
Q

2 advantages of enzymes

A

Can be used over + over

Effective in small amounts

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5
Q

What were enzymes discovered in in 1900

What type of enzyme

A

In yeast

Extracellular

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6
Q

What does the word ‘enzyme’ mean

A

‘In yeast’

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7
Q

How many different enzymes are there in human cells

A

40,000

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8
Q

What is each enzyme like to different chemical reactions

A

Specific

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9
Q

What do enzymes do to rate of reactions

A

Increase by up to 10(12) times

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10
Q

What would the speed of reactions not do without enzymes

A

Support life

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11
Q

What type of protein structure do enzymes have

A

Tertiary

Globular proteins

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12
Q

What’s an enzymes function determined by

A

It’s complex structure

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13
Q

Wheee does the reaction in an enzyme take place

A

In the active site

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14
Q

Only a few of what are involved in enzyme reactions

What type

A

Amino acids

Catalytic amino acids

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15
Q

What do catabolic reactions do

A

Break down

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16
Q

What do anabolic reactions do

A

Build up

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17
Q

What does the tertiary structure do in enzyme reactions

A

Brings them together

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18
Q

What binds in the active site

What does the rest of the protein do

A

The substrate

Acts as support

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19
Q

What do enzymes only bind with and control as they’re specific

A

Only bind with 1 substrate

Control only 1 reaction

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20
Q

What are the substrate and active site to each other

A

Complementary

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21
Q

What do enzymes ALWAYS form when they combine with their substrate

A

enzyme-substrate complexes

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22
Q

Why are enzyme-substrate complexes released as products

A

Due to their change in shape (after they bond)

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23
Q

Why can enzymes be re-used

A

As they aren’t altered or used up by reactions

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24
Q

Enzymes are energy efficient but what do they not do

What

A

Don’t last forever

As can be denatured/digested by protease

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25
Q

What do many enzymes also need to function

A

Other chemicals - coenzymes

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26
Q

What can slow down/stop enzyme function

A

Inhibitors

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27
Q

What inhibitor slows down enzyme function

A

Competitive

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28
Q

What inhibitor stops enzyme function

A

Permanent

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29
Q

Formula for enzyme function

A

Enzyme + substrate -> enzyme-substrate complex -> enzyme + products

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30
Q

How long does the enzyme-substrate complex last

A

Only temporarily while the substrate is sat in the active site

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31
Q

What are the 2 enzyme hypothesis’ s

A

Lock + key hypothesis

Induced fit hypothesis

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32
Q

What type of model is the lock + key hypothesis

What’s the active site like towards the substrate

A

Rigid

Active site is the inverse shape of the substrate - its complementary

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33
Q

How does the substrate form the enzyme-substrate complex in the lock + key hypothesis

A

The substrate fits into the precise shape (active site)

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34
Q

What does the lock+ key hypothesis not fully explain

A

The stabilisation of the enzyme - substrate complex

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35
Q

What’s the most generally accepted mechanism of action theory

A

Induced fit hypothesis

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36
Q

What is the active site not in the induced fit hypothesis

A

Active site is not a rigid shape

37
Q

What does the active site do in the induced fit hypothesis when the substrate is attracted to it

A

Active site changes shape and modules around the substrate

38
Q

Whats formed in the induced fit when the active site ,oilers around the substrate
What does the enzyme carry out

A

The enzyme-substrate complex

Enzyme carries out its catalytic function

39
Q

How do the products differ in the 2 hypothesis’

A

In the induced fit hypothesis they have a different shape so are no longer complementary to the active site

Lock + key are ^

40
Q

What do the products do at the end of the induced fit hypothesis as they’re not complementary anymore

A

Detach and leave the enzyme completely

41
Q

What does the enzyme do at the end of the induced fit hypothesis until another enzyme arrives

A

Reverts back to its original state

42
Q

Why does the shape of the active site change in the induced fit hypothesis

A

To accommodate the substrate

43
Q

What happens to bonds in chemical reactions

A

Old bonds are broken

New bonds form

44
Q

What’s the energy required to break bonds in chemical reactions

A

Activation energy

45
Q

What does the substrate require energy from to react in any chemical reaction

A

Heat

46
Q

What do enzymes do to the activation energy

What does this allow

A

Lower it

Allows reactions to take place at lower temperature

47
Q

What do enzymes do to reactions as they all them to take place at lower temperatures

A

Make them more energy efficient

48
Q

What 2 things does enzymes lowering activation energy cause to increase

A

Likelihood of correct reaction taking place (correct enzyme-substrate complexes form)
Rate of reaction

49
Q

3 factors affecting rate of reaction

A

Temperature
PH
Substrate concentration

50
Q

What’s the optimum temperature in humans at which enzymes work fastest

A

37*c

51
Q

What are Molecules that may have optimum at very different temperatures called

E.g

A

Extremophiles

E.f bacteria in volcanoes/Arctic

52
Q

What does increasing temperature do to kinetic energy

How does this increase rate of reaction

A

It increases kinetic energy
So are more collisions forming enzyme-substrate complexes
Increasing rate of reaction

53
Q

What do collisions form

A

enzyme-substrate complexes

54
Q

How can enzymes become denatured due to increasing temperature

A

Increasing temperature vibrates molecules violently
Breaks hydrogen bonds and other forces within enzyme (ionic bonds)
Altering tertiary 3D shape
So active site no longer fits substrate to form enzyme-substrate complexes

55
Q

What’s the temperature for denaturing approximately in humans

A

60*C

56
Q

What’s rate of reaction basically all about

A

The probability of enzyme colliding with substrate to form an enzyme-substrate complex

57
Q

What’s normally the best pH for enzymes to work at

A

7

58
Q

What pH to protease enzymes work best at in the stomach

Why

A

ph 1-2

Hydrochloric acid

59
Q

What does PH affect at the active site

What does this affect and cause

A

pH affects charge of amino acids at active site
Affecting ionic bonds
So substrate can no longer bind to form enzyme-substrate complex

60
Q

What can change in pH do to enzymes

A

Denature enzymes

61
Q

Sum up denaturing

A

Change of charge

Unravel of shape

62
Q

How does substrate concentration increase rate of reaction

A

As the substrate concentration increases

63
Q

What’s all filled as the enzyme is working at fully capacity (large substrate concentration )

A

All active sites filled

64
Q

How can more active sites be filled

A

Due to more collisions between enzyme and substrate

65
Q

What isn’t all being used in low substrate concentrations

A

Not all enzyme molecules are being used

66
Q

More of what is formed as substrate concentration increases

A

More enzyme-substrate complexes

67
Q

What does not affect rate when all active sites are in use (saturated)

A

Substrate concentration

68
Q

What is the part of a graph called that isn’t stopped but is just at a steady state

A

Plateau

69
Q

What can inhibitors do to enzymes catalytic activity

A

Slow it down or stop it

70
Q

What type of process is inhibitions

What’s it for

A

Natural

To switch enzymes on/off when needed

71
Q

What is inhibition mostly
What’s exceptions
E.g

A

Reversible

But some poisons are permanently inhibiting e.g heavy metal like mercury

72
Q

What happens to the enzyme when the inhibitor is removed if it’s reversible

A

Returns to Normal

73
Q

2 types of reversible inhibitors

A

Competitive

Non-competitive

74
Q

What do competitive inhibitors do and why

A

Compete with substrate molecules to occupy the active site

75
Q

What can competitive inhibitors not be converted to even though they have similar structure to substrate

A

Products

76
Q

What do competitive inhibitors reduce

A

Number of enzyme-substrate complexes being formed

77
Q

What do competitive inhibitors do to the final amount of product formed

A

Nothing it’s the same

But just takes longer

78
Q

What happens to rate if there’s an equal amount of substrate and competitive inhibitors

A

Rate is halved

79
Q

What reduces the effect of competitive inhibitor

A

Increase in substrate concentration

80
Q

What does the competitor not cause

A

Damage

81
Q

Where do non-competitive inhibitors bind to the enzyme

A

Away from the active site (allosteric site)

82
Q

What topic do we see non-compatible inhibitors in

A

Homeostasis

83
Q

What do non competitive inhibitors change

A

The overall shape of the molecules including the active site indirectly

84
Q

What’s there no competition for with non-competitive inhibitors

A

The active site

85
Q

What molecules do non-competitive inhibitors reduce the amount of

A

Active enzyme molecules (more are inactive)

86
Q

What do non-competitive inhibitors do to rate of reaction

How

A

Decrease it by decreasing number of enzyme-substrate complexes

87
Q

What doesn’t reduce the affect of non-competitive inhibitors

A

Increase if substrate concentration

88
Q

How do non-competitive inhibitors change active site shape

A

Pull out of shape

Biology - biological molecules + cells (16 decks)

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