C1.1 Flashcards

1
Q

Define catalyst.

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2
Q

State the role of enzymes in the chemical reactions on which life is based. ​

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3
Q

State that enzymes speed up chemical reactions without being altered, so can be reused.

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4
Q

Define metabolism.

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5
Q

Define specificity in relation to enzyme structure and function.

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6
Q

Outline how control of metabolism is regulated by enzymes.

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7
Q

Contrast anabolic and catabolic reactions.

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8
Q

List three examples of anabolic processes.

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9
Q

List three examples of catabolic processes.

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10
Q

Outline properties of globular proteins.

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11
Q

Explain the relationship between enzyme structure and enzyme specificity, including the structure and function of the active site.​

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12
Q

Outline the stages of enzyme catalysis of a chemical reaction.

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13
Q

Describe the induced fit model of enzyme binding.​

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14
Q

Explain the role of random collisions in the binding of the substrate with the enzyme active site.

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15
Q

Compare enzyme and substrate movement involved in reactions that occur in the cytoplasm, with large substrates and with immobilized enzymes.

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16
Q

Discuss variation in specificity of different enzymes.

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17
Q

Define denaturation.

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18
Q

Outline the causes and effects of denaturation on enzyme structure and function.

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19
Q

Explain the effects of temperature, pH and substrate concentration on enzyme structure and function with reference to collision theory, temporary and permanent denaturation.

20
Q

Draw and interpret graphs showing the effects of temperature, pH and substrate concentration of the activity of enzymes.

21
Q

Identify the manipulated (independent), responding (dependent) and controlled variation in experiments of enzyme catalyzed reactions.

22
Q

State the unit for enzyme reaction rate.

23
Q

State two methods for determining the rate of enzyme reaction rates.

24
Q

Describe three investigative techniques for measuring the activity of an example enzyme.

25
Define activation energy.
26
State that activation energy is used to break or weaken bonds in the substrate.
27
Explain the role of enzymes in lowering the activation energy of a reaction.
28
Interpret graphs showing the effect of lowering the activation energy by enzymes.
29
Compare the location of synthesis of enzymes used within and outside of a cell.
30
State an example of an intracellular metabolic reaction and an extracellular metabolic reaction.
31
Outline the generation of heat energy by the reactions of metabolism.
32
Describe how birds and mammals maintain a body temperature greater than that of their environment.
33
Outline an example of maintaining temperature homeostasis using heat generated by reactions of metabolism.
34
State the reason for metabolic pathways.
35
Contrast linear metabolic pathways with cyclical reaction pathways.
36
State and example of a linear metabolic pathway and a cyclic metabolic pathway.
37
Outline the structure and function of an allosteric site.
38
Define enzyme inhibitor.
39
Describe mechanism of action of non-competitive enzyme inhibitors.
40
Describe mechanism of action of competitive enzyme inhibitors.
41
Outline the function of statins as an example of a competitive inhibitor.
42
Explain why the rate of reaction with increasing substrate concentration is lower with a non-competitive inhibitor compared to a competitive inhibitor.​
43
Outline the mechanism and benefit of feedback inhibition.
44
Illustrate end-product inhibition of the threonine to isoleucine metabolic pathway.​
45
Compare reversible and irreversible enzyme inhibition.
46
Outline the cause and consequence of mechanism-based inhibition.
47
Illustrate mechanism-based inhibition using penicillin as an example.​