C1.1 Flashcards

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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.

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20
Q

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

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21
Q

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

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22
Q

State the unit for enzyme reaction rate.

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23
Q

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

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24
Q

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

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25
Q

Define activation energy.

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26
Q

State that activation energy is used to break or weaken bonds in the substrate.

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27
Q

Explain the role of enzymes in lowering the activation energy of a reaction.

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28
Q

Interpret graphs showing the effect of lowering the activation energy by enzymes.

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29
Q

Compare the location of synthesis of enzymes used within and outside of a cell.

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30
Q

State an example of an intracellular metabolic reaction and an extracellular metabolic reaction.

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31
Q

Outline the generation of heat energy by the reactions of metabolism.

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32
Q

Describe how birds and mammals maintain a body temperature greater than that of their environment.

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33
Q

Outline an example of maintaining temperature homeostasis using heat generated by reactions of metabolism.

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34
Q

State the reason for metabolic pathways.

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35
Q

Contrast linear metabolic pathways with cyclical reaction pathways.

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36
Q

State and example of a linear metabolic pathway and a cyclic metabolic pathway.

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37
Q

Outline the structure and function of an allosteric site.

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38
Q

Define enzyme inhibitor.

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39
Q

Describe mechanism of action of non-competitive enzyme inhibitors.

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40
Q

Describe mechanism of action of competitive enzyme inhibitors.

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41
Q

Outline the function of statins as an example of a competitive inhibitor.

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42
Q

Explain why the rate of reaction with increasing substrate concentration is lower with a non-competitive inhibitor compared to a competitive inhibitor.​

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43
Q

Outline the mechanism and benefit of feedback inhibition.

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44
Q

Illustrate end-product inhibition of the threonine to isoleucine metabolic pathway.​

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45
Q

Compare reversible and irreversible enzyme inhibition.

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46
Q

Outline the cause and consequence of mechanism-based inhibition.

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47
Q

Illustrate mechanism-based inhibition using penicillin as an example.​

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