Questions................................................................................................................2 HKALE 1995 Biology Paper I...............................................................................2 HKALE 1996 Biology Paper I...............................................................................

3 HKALE 1997 Biology Paper I...............................................................................5 HKALE 1998 Biology Paper I...............................................................................6 HKALE 1999 Biology Paper I B2.........................................................................6 HKALE 1995 Biology Paper I...............................................................................9 Temperature /C............................................................................................................10 HKALE 1996 Biology Paper I.............................................................................11 HKALE 1997 Biology Paper I.............................................................................13 HKALE 1998 Biology Paper I.............................................................................13

Questions HKALE 1995 Biology Paper I

8. (a) An experiment was conducted to investigate the effect of temperature on the activities of amylases I and II. These enzymes were obtained from the same type of tissue of vertebrate animals I and II respectively. Similar pH, enzyme concentration and substrate concentration were used. The experimental data obtained are recorded in the following table : Time for complete digestion of 1 unit of substrate / minute Amylase I 10 15 20 25 30 35 40 (i) 2.0 1.6 1.5 1.6 2.0 4.0 10.0 Amylase II 5.0 3.5 2.5 2.0 1.6 1.4 1.5

Temperature/

Plot a graph to demonstrate the effect of temperature on the activities of (5 marks)

amylases I and II.

(ii) (iii)

Explain the results for amylase I.

(2 marks)

What are the optimum temperatures for amylase I and amylase II ? What thermoregulatory ability would the data for amylase I suggest for vertebrate animal I ? (2 marks)

(b)

The graph below shows the effects of two chemicals, A and B, on the activity of amylase I. Similar pH, temperature, enzyme concentration and chemical concentration were used in the experiment.

Amylase I Enzyme activity (arbitrary unit) Amylase I + Chemical A Amylase I + Chemical B

Substrate concentration (arbitrary unit)

(i)

Compare and contrast the effects of chemical A and chemical B on the (3 marks)

activity of amylase I.

(ii)

Explain how each chemical, A and B, exerts its effect on amylase I. (3 marks) (Total : 15 marks)

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HKALE 1996 Biology Paper I

10. (a) A student performed an experiment to monitor the progress of a simple enzymecatalysed reaction involving one substrate and one product. He prepared replicate reaction tubes. In each tube, the concentration of only one reaction component, either the substrate or product, was measured. The results of three selected tubes are shown as curves A, B and C below :

(i)

Identify which measured component, substrate or product, is represented by each curve. (1 marks)

(ii)

It was realized that the reaction mixture in one of the three tubes had been wrongly prepared. This resulted in a different reaction condition. (1) State which curve represents the result of an error in the preparation. Give a reason for your choice. Suggest two possible mistakes in the student's preparation of this reaction mixture. (2) (3 marks)

What evidence shows that the other two curves represent identical reaction conditions ? (2 marks)

(iii)

With reference to curve C,

(1)

calculate the rate of enzyme reaction at the 3rd minute, given that 100% concentration is equivalent to 100 mmoles of the measured component (Show the readings you take from the graph in your calculation.) ; marks) (2

(2)

compare and explain the difference in enzyme reaction rate at the 3rd and 15th minute. (2 marks)

(iv) Curve A will finally level off and will not reach 100 %. Explain this phenomenon. (b) (11 marks) (1 marks) Total : 15 marks

Explain what is meant by the 'active site' of an enzyme.

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HKALE 1997 Biology Paper I

2. Compare and contrast the characteristics of competitive and non-competitive inhibitors on enzyme activity. (4 marks)

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HKALE 1998 Biology Paper I

6. Give one application of enzyme and explain its effect. (2 marks)

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HKALE 1999 Biology Paper I B2

12. The following reaction is catalysed by the enzyme succinate dehydrogenase :

(a)

State three parameters that can be used to determine the rate of this reaction.

(3 marks)

.................................................................................................................................................. .................................................................................................................................................. .................................................................................................................................................. ..................................................................................................................................................

(b)

The graph below shows the effect of succinate concentration on the rate of reaction under optimum pH and temperature :

The curve flattens out at X. Give two explanations for this observation based on the mechanism of enzymatic reaction. (2 marks)

.................................................................................................................................................. .................................................................................................................................................. .................................................................................................................................................. .................................................................................................................................................. (c) Malate and succinate are metabolic intermediates in the Krebs cycle. They have the following structural formulae :

(i)

Suggest what effect malate might have on the rate of reaction catalysed by succinate dehydrogenase. (1 mark)

......................................................................................................................................... (ii) The positions of malate, succinate and fumarate in the Krebs cycle are shown in the following flowchart :

Malate can play a role in regulating the rate of reactions in the Krebs cycle. Explain the possible mechanism by which malate can achieve such a control. (4 marks)

.................................................................................................................................................. .................................................................................................................................................. .................................................................................................................................................. .................................................................................................................................................. .................................................................................................................................................. .................................................................................................................................................. Total : 10 marks

HKALE 1995 Biology Paper I

8. (a) (i) properly scaled and fully labelled X and Y axes with correct units 1 1 curve labelled or keyed
correctly plotted points (correct conversion for 1/t) for the 2 curves (1 marks for each curve) (if students plot time VS temp : title () properly scaled and fully labelled axis with correct unit ().)

Refer to the graph shown below title of graph

Deduct mark if 1-2 points are plotted wrongly, and if extra points are shown. No mark if > 2 points are plotted wrongly. (Bonus : mark if student can distinguish 'reaction rate' and 'enzyme activity'. Activities of enzyme can be expressed as arbitrary unit- of substrate over time, to be indicated on Y axis.) Effect of temperature on the activities of amylase I and II

5
Reaction Rate / min
-1

4 Amylase I 3 Amylase II

10

15

20

25 temperature

30

35

40

(correct conversion for 1/t. For marker's reference in checking accuracy of

points) Rate of react on 1/t / min-1 Amylase I Amylase II 10 0.5 0.2 15 0.625 0.29 20 0.67 0.4 25 0.625 0.5 30 0.5 0.625 35 0.25 0.71 40 0.1 0.67 (Possible Max. 5) (ii) As temperature increases from 10C to 20C, the kinetic energy () of the molecules increases and there is increased collision () between enzyme and 1 substrate molecules (to form the enzyme substrate complex which subsequently breaks down to form the products). As temperature increases further, the active site of the enzyme is progressively destroyed / the enzyme undergoes thermal denaturation (1), and the reaction rate declines. 1 (2) (iii) The optimum temperature for amylase I is around 20C () while that for amylase II is the value shown on the candidates graph (). 1 It is possible that vertebrate animal I is poikilothermic / cold blooded animal. 1 (2) OR The thermoregulatory ability cannot be deduced owing to insufficient data.
Temperature /C

Deduct mark for spelling mistake. (b) (i) 1 Both chemicals A and B inhibit the activity of amylase I.

The inhibitory activity of A is competitive / can be overcome by increasing the substrate concentration but the inhibitory activity of B is non-competitive / cannot be overcome by increasing substrate concentration. 2 (3) OR
Contrast the effect at high substrate concentration (1) and at low substrate concentration (1).

(ii) Chemical A competes with the substrate for the active site () on amylase I and produced inhibitory effect at low substrate concentration (). Chemical A is structurally similar to the substrate (). max. 1 However, when substrate concentration increases, more substrate molecules are available to compete for the active site on amylase I. 1 Thus inhibitory effect is overcome at high substrate concentration. 1 Chemical B binds with enzyme in such a way that it reduces the catalytic properties of the enzyme. (Total : 15 marks) (Possible max. 15 marks) back to top

HKALE 1996 Biology Paper I

10. (a) (i) Curve A = product () Curve B = product () Curve C = substrate () (1) (ii) (1) Curve B () because it indicates a slower rate of reaction () when compared to the reaction rates indicated by curves A and C () Possible errors are : (any two, 1mark each)

(1) was added was added possible contaminant(s) / inhibitor(s) was introduced into the reaction mixture (any other acceptable answer, do not accept temperature difference as an answer) (2) (3) (2) The remaining two curves / curves A and C show a corresponding conversion to the product from the substrate (1) according to (with respect to) their % concentration (2) OR Rate of formation of the product as shown in curve A is the same as the rate of disappearance of the substrate as shown in curve C (2) (iii) (1) throughout the time points (). changes (1) at various time points (). lower substrate concentration was used / less substrate lower enzyme concentration was used / less enzyme

8 mmoles min -1(1) N.B. No mark for no unit Y2 Y1 (1) X 2 X1

Readings (2) (2)

At 3rd minute : faster rate of enzyme reaction (1) / or at 15th minute : slower rate of enzyme reaction (1) At 3rd minute, substrate concentration is higher () / at 15th minute, substrate concentration is lower, at 3rd minute chance of collision between enzyme and substrate molecules is higher () / at 15th minute chance of collision between enzyme and substrate molecules is less, at 15th minute rate is limited by product inhibition (). (1) (2)

(iv) The reaction is reversible (). End product effect pushes the reaction backwards and equilibrium is reached (1)

(1) (b) It is a special region on the enzyme molecule with a specific configuration () that can bind with the substrate to form an enzyme substrate complex (). Reaction occurs at the active site () (1) (Total : 15 marks)

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HKALE 1997 Biology Paper I

2. Both lower the activity of enzymes () and their actions are reversible () / no permanent damage to the enzyme. 1 Competitive inhibitor inhibitor molecules have similar structure as the substrate molecule (), compete with the substrate for the active sites on the enzyme molecule (), inhibition effect overcome by increased substrate concentration (). 1 Non-competitive inhibitor molecules attack the enzyme molecule not at the active site (), but changes the conformation of the enzyme () prevents the active site from catalyzing reactions, inhibition effect not overcome by increased substrate concentration (). 1 Q2 = 4 marks

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HKALE 1998 Biology Paper I

6. meat tenderizer (1) ( accept correct alternatives) contains protease () which breaks down protein in the meat(), renders the meat more tender() (2)

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