cape biology unit one

Please try to keep the answers brief, clear and accurate.

1. What are enzymes? (3 mks)

2. State five properties of enzymes. (5 mks)
3. What don’t enzymes affect? (2 mks)
4. Complete the following description of enzymes by adding the most appropriate word or
words in the gaps:

Enzymes are biological catalysts which increase the rate of a reaction by reducing the
_________________energy needed for the reaction to take place. Enzymes are globular
________________ which possess a region on their surface where binding to a substrate
occurs. This region is called the ____________. The bonds which maintain the tertiary
structure of the
enzyme can be disrupted by factors such as __________________ and
___________________, reducing the catalytic action of the enzyme. Ions of heavy
metals such as mercury cause ________________inhibition of enzymes. Other inhibitors
reduce enzyme activity because they are a similar shape to the enzyme’s substrate. These
are called __________________ inhibitors. (7 mks)

5. What is meant by enzyme ‘cofactor’? Explain how a vitamin deficiency may affect
enzyme activity. (3 mks)
6. Describe the three main categories of chemical reactions. (3 mks)
7. State what activation energy is and describe how enzymes work to lower the activation
energy of a reaction? Be sure to include a graphical representation (6 mks)
8. Explain the two models for how substrates bind the active site of an enzyme. (4 mks)
9. What is meant by (a) active site (3 mks); (b) enzyme specificity (2 mks); (c) denaturing
(3 mks) and (d) enzyme turnover number (2 mks)?
10. Using a named example, explain the key stages in the mode of action of enzymes. (8
mks)

Enzyme 1 Enzyme 2 Enzyme 3 Enzyme 4

11. A B C D
E

If a cell was unable to make enzyme 3, what would happen in the cell to the level of: (a)
compound D; (b) compound C. (2 mks)

12. Explain the effects of temperature, pH, enzyme concentration and substrate concentration
on enzyme action. Be sure to include expected graphs. (12 mks)
 cape biology unit one

13. Using named examples, distinguish between reversible and irreversible inhibition. (6
mks)
14. Using succinic dehydrogenase as an example, explain how competitive inhibition affects
enzyme activity. (5 mks)
15. Using a named example, explain how non-competitive inhibition affects enzyme activity.
(5 mks)
16. Read this account of an enzyme experiment and answer the questions which follow:
Powdered mild contains the protein casein. When powdered milk is mixed with water, it
forms an opaque white suspension. If a proteolytic enzyme such as trypsin is added to
this suspension, it will clear, becoming translucent.
In an experiment, the effect of trypsin on a suspension of the milk at different
temperature was investigated.

10 cm3 of milk suspension and 10 cm 3 of trypsin solution were incubated separately in a

water bath at room temperature. After allowing the tubes to equilibrate to the temperature
of the water bath, their contents were mixed and the time taken for the mixture to clear
was recorded. The rate of the reaction (cm 3 per minute) was calculated by dividing the
volume of milk by the time for the reaction to finish. The investigation was repeated at
several temperatures. The results are shown in the table below.

Table 1 showing rate of reaction at different temperatures

Temp (⁰ C) Rate of reaction (cm3 min-1)

10 0.80
20 1.95
30 4.40
40 7.45
45 8.30
52 8.05
57 7.10
60 6.00
65 2.65
70 1.00

(a) Plot a graph of the rate of reaction at different temperatures. (4 mks)

(b) Explain the effect of temperature on the rate
(i) Between 10 and 40 ⁰C (2 mks)
(ii) Between 50 and 70 ⁰ C (3 mks)
(c) From Table 1 and your graph, estimate the optimum temperature for trypsin activity.
(1 mk)
(d) Name one other condition which should be kept constant during the experiment. (1
mk)
 cape biology unit one

(e) Trypsin is a digestive enzyme in the human body. Body temperature is 37 ⁰C.
Suggest a reason for the different optimum obtained from the graph. (1 mk)
(f) In the experiment described above, the point when the milk suspension had gone clear
was simply estimated by eye. Suggest a more reliable method which could be used. (1
mk)
94-Q6: 91