Metabolic Pathways Flashcards

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1
Q

What do we call integrated and controlled pathways of enzyme-catalysed reactions in a cell?

A

Metabolic pathways

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2
Q

What is metabolism?

A

All the chemical reactions that take place within an organism

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3
Q

Tell me 2 things about anabolic reactions.

A
  1. build up larger molecules from smaller molecules

2. Require energy

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4
Q

If a step within a metabolic pathway is one-way is is described as…

A

irreversible

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5
Q

If a product can be converted back into a substrate within a pathway, it is described as…?

A

reversible

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6
Q

With the induced fit model, what is it that changes shape?

A

The active site of the enzyme

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7
Q

There isn’t always one way to get to the same end product. If there is a different pathway, what do we call it?

A

An alternative route

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8
Q

Tell me 2 things about a catabolic reaction.

A
  1. Breaks down larger molecules into smaller molecules

2. Releases energy

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9
Q

‘Lock and Key’ in Nat 5 was a lie!!! What is a better model for how an enzyme works?

A

induced fit model

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10
Q

State 3 functions of proteins embedded within the cell membrane.

A
  1. Protein pores (diffusion)
  2. Protein pumps (active transport)
  3. Enzymes
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11
Q

If there is a mutation to a gene that controls the production of an enzyme, how would that affect the concentration of substrate and product?

A

Substrate would probably increase

Product would probably decrease (enzyme not present to carry out the reaction)

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12
Q

What does the term affinity mean?

A

an attraction

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13
Q

What is the affinity between an enzyme and its substrate.

A

High

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14
Q

What is the affinity between an enzyme and its product.

A

Low

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15
Q

What do we call the energy required to initiate a reaction?

A

Activation energy

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16
Q

How does an enzyme affect the activation energy for a reaction?

A

It lowers the activation energy

17
Q

State the 3 roles of the active site.

A
  1. It orientates reactants and is a binding site for reactants (high affinity for substrates)
  2. It decreases the activation energy
  3. It releases products with low affinity
18
Q

State 5 factors that can affect enzyme activity.

A
  1. temperature
  2. pH
  3. Enzyme concentration
  4. substrate concentration
  5. end product inhibition
19
Q

Describe how increasing substrate concentration affects the rate of a reaction (2)

A

As the substrate concentration increases initially the rate of reaction increases and then rate of reaction levels out and remains the same.

20
Q

Explain why continually increasing the substrate concentration does not continually increase the rate of reaction.

A

The enzymes reach saturation point - all the enzyme active sites are occupied.

21
Q

In end product inhibition, what does the end product inhibit?

A

An enzyme at the start of the metabolic pathway

22
Q

What is end product inhibition also known as?

A

Feedback inhibition

23
Q

When does feedback inhibition take place?

A

When the end product reaches a critical concentration.

24
Q

It the concentration of the end product decreases to below the critical concentration, what happens?

A

The enzyme at the start of the metabolic pathway is no longer inhibited.

25
Q

What do we call substances that prevent enzyme activity?

A

inhibitors

26
Q

Where does a competitive inhibitor join onto an enzyme?

A

active site

27
Q

Why is a competitive inhibitor able to join to the active site of an enzyme?

A

It has a similar shape to the substrate

28
Q

What is the result of the competitive inhibitor attaching to the active site?

A

It blocks the active site so no enzyme-substrate complex can be produced so the reaction rate is reduced

29
Q

Why is a competitive inhibitor described an a reversible reaction?

A

When the inhibitor is released from the active site, the substrate can once again interact with the enzyme

30
Q

How can you reduce the effect of a competitive inhibitor?

A

Increase the concentration of substrate, there is more chance of the substrate winning the competition and combining with the active site

31
Q

Where does a non-competitive inhibitor join to an enzyme?

A

The allosteric site, somewhere else on the enzyme

NOT the active site

32
Q

Why does a non-competitive inhibitor joining to the allosteric site affect the rate of a reaction?

A

It causes the active site of the enzyme to alter its shape, no longer complementary to the substrate

33
Q

How does increasing the concentration of substrate affect a non-competitive inhibitor?

A

It doesn’t

34
Q

Why is a non-competitive inhibitor described as reversible?

A

Once the inhibitor is released, the active site is restored to its original shape