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Chapter 4 Enzyme regulation in biochemical

pathways Total marks 14

Chapter test

Name: ______________________ Class: ______ Date: ______

Section A: Multiple choice (8 marks)

Use the following graph to answer questions 1 and 2.


The graph below shows the energy levels of a reaction in the presence or absence of an
enzyme.

1 What is the best explanation of the different energy levels labelled P, Q and R?

P Q R

A Absence of an enzyme Presence of an enzyme Endergonic reaction

B Presence of an enzyme Absence of an enzyme Exergonic reaction

C Absence of an enzyme Presence of an enzyme Exergonic reaction

D Presence of an enzyme Absence of an enzyme Endergonic reaction

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2 Which of the following represents the activation energy of the enzyme-catalysed
reaction?
A P
B Q
C P+R
D Q+R

3 What is an active site?


A the part of an enzyme that binds only to the product molecules
B the part of an enzyme that binds to a substrate
C the sequence of amino acids responsible for the structure of an enzyme
D the specific area responsible for the activity of all proteins

4 According to the induced fit model of enzyme function, which of the following
statements is correct?
A There is an exact fit between a specific substrate and a specific enzyme.
B The enzyme can change shape to accommodate the substrate.
C The substrate can change its shape to fit a number of enzymes.
D Competitive inhibitors can change the shape of enzymes.

5 The following graph shows the effect of temperature on enzyme activity. What is
happening at point P?

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A The enzyme is being denatured.
B The concentration of the product is decreasing.
C The concentration of the substrate remains constant.
D The reaction is increasing in speed.

6 The following graph shows the effect of changing substrate concentration on the
amount of product formed.

Which of the following is a suitable conclusion from these results?


A The rate of reaction increases exponentially with an increase in substrate
concentration.
B The rate of reaction decreases exponentially with an increase in substrate
concentration.
C The rate of reaction increases greatly up to a point as the substrate concentration
increases, and then the rate of increase starts to slow down.
D The rate of reaction is not affected by any change in the substrate concentration.

7 What can reduce the effect of a competitive inhibitor of an enzyme?


A Increase the temperature at which the reaction takes place.
B Increase the pH at which the reaction takes place.
C Increase the substrate concentration.
D Add a non-competitive inhibitor.

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8 Which of the following options describes how non-competitive inhibition works?

Binding to the Inhibitor binds Enzyme will be activated


enzyme is to active site of and/or inhibited
reversible enzyme

A No Yes Activated

B Yes No Can be activated or inhibited

C Yes Yes Inhibited

D No No Can be activated or inhibited

Section B: Short answer (6 marks)

1 Enzymes are used to catalyse cellular reactions.

a What enzyme activation model does the diagram above represent?

b If heated above its critical temperature, an enzyme denatures. Define the term
‘denature’.

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c What implications does denaturing have for the enzyme’s activity?

2 a Using the lock-and-key model, explain enzyme substrate specificity.

b Identify at least three other characteristics of enzymes.

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3 a Define the term ‘metabolic pathway’.

b Explain why each step in a metabolic pathway often requires a separate enzyme.

c Explain how feedback inhibition controls metabolic pathways.

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4 The graph below shows the effect of pH on the activity of three enzymes: pepsin,
salivary amylase and trypsin.

a Describe the relationship between the activity of each enzyme and the pH.

b Outline the effect of pH values above and below the optimum on enzyme structure
and activity.

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5 a What are coenzymes?

b Distinguish between loaded and unloaded forms of coenzymes, and give an


example.

Multipart question

1 Glycolysis is an important metabolic pathway that occurs in the cytoplasm. A section of


the pathway showing the various substrates, products and enzymes is illustrated
below.

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Scientists measured the effect of different concentrations of fructose 6-phosphate on
phosphofructokinase activity. Phosphofructokinase activity was also measured with low
and high concentration of ATP in the reaction mixture. The graph below shows the
results.

a Outline the effect of increasing fructose 6-phosphate.

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b Explain how increasing the concentration of fructose 6-phosphate affects the
activity of phosphofructokinase.

c Outline the effect of increasing ATP concentration on the activity of


phosphofructokinase.

d Given that one of the functions of glycolysis is to produce ATP, explain how the
effect of ATP on phosphofructokinase is advantageous.

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