2.1.4 Enzymes Flashcards

1
Q

what is an example of an intracellular enzyme?

A
  • catalase
  • works inside cell
  • catalyses breakdown of hydrogen peroxide
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2
Q

what’s an example of an extracellular enzyme?

A
  • amylase
  • works outside cells in digestive system
  • catalyses hydrolysis of starch into maltose
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3
Q

what do enzymes do to activation energy?

A

reduce it

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4
Q

what is activation energy?

A

certain amount of energy needed for a reaction to occur

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5
Q

how do enzymes lower activation energy?

A
  • formation of an enzyme substrate complex
  • if two substrate molecules need to join, attaching to enzyme holds them together reducing repulsion
  • if enzyme is catalysing breakdown reaction, fitting into active site creates a strain in substrate bonds. bonds break up more easily
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6
Q

what does the induced fit model say about enzymes?

A

as substrate binds, active site changes shape slightly to fit substrate more easily

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7
Q

what factors affect enzyme activity?

A
  • temp
  • ph
  • substrate conc
  • enzyme conc
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8
Q

how does temp affect enzyme activity?

A
  • more kinetic energy so substrates move faster and more collisions so more enzyme substrate complex formed
  • if temp goes above certain level, vibration breaks bonds in enzyme, active site changes shape and substrate no longer fits
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9
Q

what is the temperature coefficient (Q10)?

A

how much the rate of reaction changes when temp is raised by 10°C

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10
Q

how does ph affect enzyme activity?

A
  • too low or too high ph messes up hydrogen and ionic bonds in tertiary structure
  • done by H+ and OH- ions
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11
Q

how does enzyme concentration affect enzyme activity?

A
  • more enzyme molecules = more likely for a substrate to collide and bind to form an enzyme substrate complex
  • ** if more enzyme than substrates**, all substrates will be used up so increasing conc will then have no effect
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12
Q

how does substrate concentration affect enzyme activity?

A
  • higher chance of collision and enzyme substrate complexes forming
  • more active sites used up
  • after saturation point, all active sites full so increase conc will not increase rate of reaction
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13
Q

why is there a need for diff enzymes in diff parts of any process in the body?

A
  • enzymes are specific
  • the substrates are different shapes
  • active site and substrates are complimentary
  • forms an enzyme substrate complex
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14
Q

what is a metabolic pathway?

A
  • series of connected metabolic reactions
  • product of first reaction takes part in second reaction but each reaction is catalysed by a different enzyme
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15
Q

what is product inhibition?

A

when an enzyme is inhibited by the product of the same reaction they catalyse

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16
Q

what is end product inhibition?

A

when the final product in a metabolic pathway inhibits an enzyme earlier on in the pathway

17
Q

what’s end product inhibition an example of?

A
  • negative feedback
  • high level of end product will inhibit enzyme catalysing reaction
18
Q

why is environment being too acidic bad for enzymes?

A
  • very high conc of H+ ions
  • alters tertiary structure
  • H+ ions affect interactions between amino acids’ R groups
  • R groups no longer interact and H/ionic bonds break
19
Q

how can cofactors/coenzymes affect structure of enzyme?

A
  • change tertiary structure
  • alter active site
  • alter bonds in tertiary structure
20
Q

what are reversible inhibitors?

A

weak hydrogen/ionic bonds between enzyme and inhibitor, inhibitor can be removed easily

21
Q

what are irreversible inhibitors?

A

strong bonds between enzyme and inhibitor so inhibitor can’t be removed easily