2.5 + 8.1 enzymes and metabolism Flashcards

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1
Q

what is anabolism

A

synthesis of larger molecules from smaller molecules

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2
Q

what is catabolism

A

breaking down complex molecules into smaller molecules

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3
Q

what is metabolism

A
  • all enzyme catalysed reactions in a cell
  • includes anabolism and catabolism
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4
Q

what are enzymes

A

biological catalysts that increase the rate of reaction without being consumed

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5
Q

what are 3 features of enzymes?

A
  1. enzymes lower Ea of reactions
  2. enzymes are highly specific as its active site is complementary in shape to its substrate
  3. enzymatic activity is lost when denatured due to loss of 3D conformation of active site
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6
Q

the two models of enzyme action are…

A

lock and key, induced fit

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7
Q

what does the lock and key model propose?

A
  • the active site is inflexible with a rigid shape
  • only substrates with exact shape can fit in active site
  • lock = active site on enzyme and key = substrate
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8
Q

how does the induced fit model extend the lock and key model?

A
  • increases the range of substrate specificity
  • proposes that when a substrate binds to an enzyme, it induces a change in conformation of the enzyme’s active site
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9
Q

what affects enzyme activity? (5 briefly)

A
  1. temp
  2. pH
  3. [substrate]
  4. [enzyme]
  5. [enzyme inhibitor]
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10
Q

how does temp affect enzyme activity?

A
  • incr temp -> incr kinetic energy
  • thus incr rate of effective collisions btw substrates and enzymes
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11
Q

how does pH affect enzyme activity?

A
  • pH affects the structure of the enzyme
  • drastic pH changes can cause denaturation, changing the shape of the active site
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12
Q

what is the effect of increasing [substrate]?

A
  • incr substrate leads to more chances of effective collisions w enzymes -> incr the % of active sites occupied
  • at high [substrate] there is saturation of all active sites
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13
Q

how do competitive inhibitors work?

A

they compete with the substrate at the active site

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14
Q

how do non competitive inhibitors work?

A

they bind to the allosteric site to alter the shape of the active site

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15
Q

_________ inhibition can be overcome by increasing [substrate]

A

competitive

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16
Q

what is a structural feature of competitive inhibition that enables it to function as a competitive inhibitor?

A

the inhibitor and substrate are similar in shape

17
Q

the synthesis of isoleucine from threonine involves _________ inhibition

A

end product

18
Q

end product inhibitors are typically _________ inhibitors

A

non-competitive

19
Q

how does end product inhibition control metabolism?

A
  • end product of a metabolic pathway acts as an inhibitor of the first enzyme in the pathway
  • accumulation of end product incr its chances of inhibiting the enzyme to stop the metabolic pathway
20
Q

what is a metabolic pathway?

A

a chain of enzyme-catalysed reactions

21
Q

in the synthesis of isoleucine, who is the end product inhibitor?

A

isoleucine

22
Q

what enzyme is used in the synthesis of isoleucine?

A

threonine deaminase

23
Q

isoleucine is an [competitive/non-competitive] inhibitor

A

non-competitive

24
Q

explain the end product inhibition of isoleucine

A
  • isoleucine is synthesised from threonine
  • isoleucine is non competitive inhibitor of threonine
  • binds to allosteric site of threonine deaminase,
    the enzyme in the first step
  • stops the metabolic pathway
25
Q

what are 2 ways enzymatic reactions can be tracked?

A

measure
1. rate of pdt formed
2. rate of disappearance of substrate

26
Q

why are enzymes immobilised (brief)

A
  1. so they can be reused
  2. so the reaction can be stopped quickly by removing the enzyme
27
Q

what is an example of enzyme immobilisation in the industry?

A

lactose-free milk

28
Q

who needs lactose-free milk

A

individuals w lactose intolerance

29
Q

how is lactose-free milk produced?

A

regular milk with lactose is passed over immobilised lactase