3.1.4.2 Many proteins are enzymes Flashcards

1
Q

what is an enzyme?

A

biological catalysts that speed up the rate of a chemical reaction in organisms without getting used up

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2
Q

where can enzymes catalyse metabolic reactions?

A

at a cellular level (respiration) and extracellularly (digestion)

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3
Q

what is formed when an enzyme binds to a substrate?

A

enzyme-substrate complex

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4
Q

how do enzymes speed up metabolic reactions?

A

by lowering the activation energy of a reaction due to bending bonds

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5
Q

what are the two models of enzymes?

A
  • lock and key
  • induced fit
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6
Q

what does the lock and key model of an enzyme suggest?

A

the shape of the active site is exactly complementary to the specific substrate molecule

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7
Q

what does the induced fit model of an enzyme suggest?

A

the active site can change shape slightly so it is complementary to the substrate, this distorts bonds in the substrate and therefore lowers activation energy

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8
Q

why is the induced fit model better than the lock and key model?

A

research has been done into inhibitors, suggesting that the structure of an enzyme is not as rigid as it was assumed to be, meaning that it can change shape

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9
Q

how does temperature affect enzyme activity until the optimum temperature?

A
  • increase in temperature causes an increase in kinetic energy
  • this causes molecules to move around more and increases the chances for more successful collisions
  • this increases the rate of enzyme activity
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10
Q

how does temperature affect enzyme activity beyond the optimum temperature?

A
  • hydrogen and other bonds break
  • this disrupts the secondary and tertiary structure
  • causes denaturation so rate of enzyme activity decreases
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11
Q

denaturation of enzymes due to temperature is…

A

permanent

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12
Q

what is pH?

A

the concentration of hydrogen ions of solution

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13
Q

what is the formula for calculating pH?

A

-log[H+]

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14
Q

how does pH affect the rate of enzyme activity?

A
  • changes ionic charges within the enzyme
  • causes hydrogen and ionic bonds to change
  • more likely to decrease the rate of enzyme activity than denature enzymes
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15
Q

denaturation of enzymes due to pH is…

A

generally reversible

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16
Q

what is competitive inhibition?

A
  • inhibitor has a similar shape to substrate
  • molecule binds to active site of enzyme before substrate can
  • prevents e-s complex forming
17
Q

what is non-competitive inhibtion?

A
  • molecule binds to allosteric site (site in the enzyme other than the active site)
  • changes the shape of the active site / alters tertiary structure
  • no longer complementary to the substrate so no e-s complexes form
18
Q

when competitive inhibitors are present, how would the rate of enzyme activity change if the concentration of the substrate increased?

A

enzyme activity would increase as substrates out-compete inhibitor to form e-s complexes

19
Q

when non-competitive inhibitors are present, how would the rate of enzyme activity change if the concentration of the substrate increased?

A

no change as active site changes shape so no e-s complexes can form

20
Q

what happens to e-s complexes during competitive inhibition?

A

less e-s complexes are formed

21
Q

what happens to e-s complexes during non-competitive inhibition?

A

no e-s complexes are formed