Altrincham Grammar School For Girls

Extra Enzymes Qs 2017

Q1.(a)     Describe the induced-fit model of enzyme action.

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(2)

(b)     A scientist investigated the hydrolysis of starch.He added amylase to a suspension

of starch and measured the concentration of maltose in the reaction mixture at
regular intervals.

His results are shown in the graph below.

Determine the rate of the reaction at 10 minutes.

Show how you obtained your answer.

Rate of reaction ............................................. mg dm−3 min−1

(2)

(c)     Explain the results shown in the graph.

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(2)

(Total 6 marks)

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Q2.Read the following passage.

Alzheimer’s disease leads to dementia. This involves small β-amyloid

proteins binding together to form structures called plaques in the brain.

Nerve cells in the brain produce a large protein called amyloid-precursor

protein that has a complex shape. This protein is the substrate of two
different enzymes, α-secretase and β-secretase. These enzymes are                    5
normally produced in the brain. One product of the reaction catalysed by
β-secretase is a smaller protein that can lead to β-amyloid protein formation.
Many people with Alzheimer’s disease have mutations that decrease
α-secretase production, or increase β-secretase production.

One possible type of drug for treating Alzheimer’s disease is a competitive           10
inhibitor of β-secretase. When some of these types of drugs were trialled on
patients, the trials had to be stopped because some patients developed
serious side effects.

Use information from the passage and your own knowledge to answer the following
questions.

(a)     Suggest how amyloid-precursor protein can be the substrate of two different
enzymes, α-secretase and β-secretase (lines 3–5).

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(2)

(b)     One product of the reaction catalysed by β-secretase is a smaller protein (lines 6–
7).

Describe what happens in the hydrolysis reaction that produces the smaller protein
from amyloid-precursor protein.

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(2)

(c)     Many people with Alzheimer’s disease have mutations that decrease α-secretase
production, or increase β-secretase production (lines 8–9).

Use the information provided to explain how these mutations can lead to
Alzheimer’s disease.

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 Altrincham Grammar School For Girls
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(3)

(d)     One possible type of drug for treating Alzheimer’s disease is a competitive inhibitor
of β-secretase (lines 10–11).

Explain how this type of drug could prevent Alzheimer’s disease becoming worse.

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(2)

(e)     When some of these types of drugs were trialled on patients, the trials were stopped
because some patients developed serious side effects (lines 11–13).

Using the information provided, suggest why some patients developed serious side
effects.

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(1)
(Total 10 marks)

Q3.Lipase is an enzyme that hydrolyses triglycerides.

A student investigated the hydrolysis of triglycerides in milk by human lipase at 20 °C.

He recorded the pH of a sample of milk before and after adding lipase. He used a pH
meter to record pH.

His results are shown in the graph.

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(a)     Suggest one advantage of using a pH meter rather than a pH indicator in this
experiment.

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(b)     Explain why the pH decreases when the lipase is added to the milk.

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(c)     Suggest why the pH remained constant after 2 minutes.

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(d)     The student carried out his experiment at 20 °C. He then repeated the experiment at
15 °C.
Draw a line on the graph to show the results you would expect at 15 °C.
(2)
(Total 6 marks)

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 Altrincham Grammar School For Girls

M1.(a)     1.      (before reaction) active site not complementary to/does

not fit substrate;
2.      Shape of active site changes as substrate binds/as
enzyme-substrate complex forms;
Note. Points 1 and 2 may be made in one statement and
‘complementary’ introduced at any point.
Points 1&2 – active site mentioned once applies for both
points
Point 2 – Ignore references to how shape change is caused
3.      Stressing/distorting/bending bonds (in substrate leading to reaction);
2 max

(b)     1.      Tangent to curve drawn;

Tangent drawn at about 10 minutes
2.      Value in range of 8 to 11;
1 mark only for correct answer
2

(c)     1.      (Rate of) increase in concentration of maltose slows as

substrate/starch is used up
OR
High initial rate as plenty of starch/substrate/more E-S complexes;
Reject ref. to amylase being used up

2.      No increase after 25 minutes/at end/levels off because no substrate/starch left;

Accept ‘little’
Ignore references to substrate a limiting factor
2

(d)     1.      Make/use maltose solutions of known/different concentrations

(and carry out quantitative Benedict’s test on each);
2.      (Use colorimeter to) measure colour/colorimeter value of each
solution and plot calibration curve/graph described;
Axes must be correct if axes mentioned, concentration on x-
axis and colorimeter reading on y-axis
3.      Find concentration of sample from calibration curve;
3
[9]

M2.(a)     1.      Different parts/areas/amino acid sequences (of amyloid-precursor) protein;

Accept APP
2.      Each enzyme is specific/fits/binds/complementary to a different part of the
APP;
Point 2 subsumes point 1 and is worth 2 marks total.
2

(b)     1.      Peptide bond broken;

2.      Using water;
Hydrolysis in stem
2

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(c)     1.      Mutations prevent production of enzyme(s)/functional enzyme;

2.      (Increase in β-secretase) leads to faster/more β-amyloid production
OR
(Decrease in α-secretase) leads to more substrate for β-secretase;
‘This’ must refer to α-secretase
3.      (Leads to) more/greater plaque formation;
3

(d)     1.      (Inhibitor) binds to/blocks active site of β-secretase/enzyme;

2.      Stops/reduces production of β-amyloid/plaque;
2

(e)     1.      Some β-amyloid required/needed (to prevent side effects)

OR
(Some) β-secretase needed;
Accept ‘Both enzymes needed’
2.      Leads to build-up of amyloid-precursor protein (that causes harm)
OR
Too much product of α-secretase (causes harm);
Accept build-up of substrate (leads to harm)
1 max
[10]

M3.(a)     Any one from:

1.      Numerical readings / not subjective / colour change

subjective / gives quantitative data / not qualitative / gives
continuous data;
2.      Greater accuracy;
Accept greater precision
1 max

(b)     Fatty acids produced;

1

(c)     1.       No more (fatty) acids produced;

2.       All triglycerides/fat//lipids/substrate used up / enzyme
denatured;
2

(d)     1.       Line starting at same point and falling above original
line;
2.       Levels off at same pH, but later;
Accept the line still falling at 4 minutes
Do not credit if levels off at higher pH
2
[6]

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