Enzymes Flashcards

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1
Q

Define metabolic reactions.

A

‘The complex of physical and chemical processes
occurring within a living cell or organism that are
necessary for the maintenance of life’.

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2
Q

Describe the process of catabolism.

A

The process were complex molecules are broken down into simpler ones is known as catabolism – i.e. proteins
to amino acids.

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3
Q

Describe the process of anabolism.

A

The process were complex molecules are synthesised
from simpler ones is known as anabolism – i.e. amino
acids to proteins – these can then be utilised in the body.

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4
Q

describe the function of digestion

A

This is the function of digestion. To break down complex insoluble molecules (catabolism) into
simpler soluble molecules so they can be absorbed and assimilated (synthesised – anabolism)

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5
Q

What are reactions called when they release energy and give an example?

A

Some of these reactions release energy and are exergonic – i.e. cellular respiration. .

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6
Q

What are reactions called that require energy?

A

Some reactions require energy and are endergonic.

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7
Q

What are enzymes?

A

Enzymes are globular proteins that act as biological catalysts.

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8
Q

What is a catalyst and what do catalysts do?

A

A catalyst increases the rate at which chemical reactions occur but remain unchanged or are unaffected by the reaction.

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9
Q

State the equation for a chemical reaction.

A

Reactants————————- Products

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10
Q

Define the activation energy?

A

Activation energy is the minimum energy required

for a successful chemical reaction.

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11
Q

why do enzymes speed up the rate of reactions?

A

Enzymes speed up the rate of reaction by lowering the activation energy needed for a
chemical reaction.

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12
Q

How do enzymes speed up the rate of reactions and decrease the amount of activation energy needed?

A

Enzymes do this by helping to align the reactants through the formation of enzyme substrate
complexes and stress the bonds (bending bonds) within the substrate, so they require less
energy to break them. Collisions will occur between specific parts of the molecules involved
in the reaction, so bonds can break and reform more efficiently, therefore less activation
energy is required.

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13
Q

Describe the structure of enzymes.

A

Enzymes are proteins which have a specific 3D/tertiary shape. They have a specifically
complementary active site to their substrate/s (reactant/s). This then allows the substrate
to bind to the enzyme active site forming an enzyme–substrate complex (ES). It is this that
aligns the reactant and lowers the activation energy.

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14
Q

what does the lock and key theory state?

A

The lock and key theory states that the active site is specifically complementary to its substrate, fitting
it like a key in a lock. This model is useful as it helps to describe the specificity demonstrated by enzymes.

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15
Q

describe the stages of the lock and key theory?

A
  1. The substrate enters the enzymes active site
  2. The substrate fits exactly into the active site – they are complementary
  3. Products are formed and no longer fit into the active site – not complementary
  4. The enzyme is free to take part in another reaction
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16
Q

what does the lock and key model not take into consideration?

A

The lock and key model does not take into account that enzyme’s active sites are not rigid
structures and can be changed when substrates bind.

17
Q

Describe what the induced fit model states.

A

The induced fit theory states that the active site is not fully fixed and the substrate ‘induces’ a change in the shape of the active site making it
complimentary.

18
Q

Describe the stages of the induced fit model

A
  1. The substrate enters the enzymes active site
  2. The binding of the substrate molecule/s induces the change in the shape of the active
    site.
  3. When the substrate leaves the active site it then returns to its previous shape.
19
Q

why does only one enzyme only catalyse one reaction?

A

This is due to the lock and key theory.

20
Q

As enzymes are proteins they are affected by temperature and pH. what are enzymes also affected by?

A
  • Inhibitors

* Substrate concentration

21
Q

How does temperature affect enzymes?

A

Every enzyme has a temperature at which it works best (optimum). As the temperature increases up to its optimum the enzyme and substrate molecules have more kinetic energy and are more likely to collide and form more enzyme substrate complexes per unit time (the collisions are more successful). The rate of the reaction increases.

22
Q

Define the term ‘optimum temperature’

A

Optimum Temperature – The maximum heat energy that can be supplied to the enzyme
molecules before hydrogen and ionic bonds start to break

23
Q

Describe what would happen when temperature is above the optimum temperature.

A

Above the optimum temperature:
• further increase in kinetic energy
• causes amino acids in polypeptide chain to
vibrate
• breaks hydrogen and ionic bonds between the R
groups
• the tertiary structure is lost
• Active site shape is no longer specific to
substrate
• No enzyme substrate complexes can be formed.
• Enzyme is denatured and can no longer catalyse
any chemical reactions.

24
Q

Define the term pH

A

pH is a measure of hydrogen ion concentration.

25
Q

What occurs when the pH alters from the optimum level?

A

If the pH alters from the optimum then the charge on the R groups of the amino acids are altered and ionic bonds in the tertiary structure are broken.
Therefore the active site changes shape and the substrate can no longer fit (not specifically
complementary). No enzyme substrate complexes can be formed and the rate of the reaction
decreases either side of the optimum. The enzyme is denatured.

26
Q

Describe the effect of substrate concentration

A

As the substrate concentration increases the rate
of reaction increases and then levels off. The rate of reaction is low at low substrate concentrations as not all of the active sites of the enzymes are saturated (filled). The substrate is a limiting factor.

27
Q

What happens when the substrate concentration increases?

A

As the substrate concentration increases, the active sites are filled and the rate of reaction increases, due to more successful collisions between enzyme active sites and substrate. The substrate is no longer a limiting factor.
HOWEVER At high levels of substrate, there is no further rise in rate of reaction since the enzymes
cannot formed any more enzyme substrate complexes as all active sites are filled. The number of enzymes is now the limiting factor.

28
Q

describe competitive inhibitors

A

Competitive inhibitors have a similar structure to
substrates. They fit into the active site but do not react.
They prevent the normal substrate from binding and hence slow the rate of reaction as fewer enzyme substrates can be formed.

29
Q

Describe non competitive inhibitors

A

These bind to a site on the enzyme which is distant from the active site. They alter the shape of the active site so that substrate/s cannot fit. Fewer enzyme substrates can be formed and the rate
of reaction is decreased.