Enzymes and Proteins Flashcards

1
Q

What are the 2 types of inhibitors

A

competitive and non-competitive

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2
Q

Outline competitive inhibitors

A
  • bind at the active site of the enzyme
  • they have a similar shape to the substrate
  • prevent substrate from binding to active site
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3
Q

Solution for competitive inhibitors

A

increasing the concentration of substrates, decreases the impact of competitive inhibition, as fewer of the inhibitors are able to bind to the active site

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4
Q

What happens to the Vmax for competitive inhibitors

A

Vmax is not changed as there is still a substrate concentration where full enzyme activity can be achieved

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5
Q

What happens to the Km for competitive inhibitors

A

The Km is increased as it takes a higher substrate concentration to reach Vmax

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6
Q

Outline non-competitive inhibitors

A
  • bind to the allosteric site of the enzyme
  • alter the shape of active site and prevents the substrate to bind to the active site of enzyme
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7
Q

Solution for non-competitive inhibitors

A

no solution: increasing the concentration of substrates doesn’t reduce the effect of the inhibition

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8
Q

What happens to the Km for non-competitive inhibitors

A

Km remains unchanged

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9
Q

What happens to the Vmax for non-competitive inhibitors

A

Vmax decreases

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10
Q

What does Vmax mean/represent

A

refers to the point where all the active sites are saturated
- a low Vmax = high enzyme activity
- a high Vmax = low enzyme activity

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11
Q

What does Km mean/represent

A

refers to the substrate concentration which is equal to half of its maximum value
- high Km = high concentration of substrate needed to saturate enzyme (low enzyme-substrate) affinity

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12
Q

Define buffer

A

substances that resist changes in pH in addition of small amounts of acid or base

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13
Q

What can act as a buffer

A

amino acids

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14
Q

does an amino acid act as a buffer around its isoelectric point

A

no

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15
Q

Why can amino acids act as buffers

A

they can accept and donate protons

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16
Q

What are the assumptions made when calculating the ph of a buffer

A
  • salt completely dissociates into its ions
  • The concentration of the weak acid at equilibrium is approximately equal to the initial concentration of the weak acid
17
Q

What is UV-visible spectroscopy

A

a technique used in protein assays to measure the concentration of a protein in a sample

18
Q

What is product inhibition

A

Since metabolic processes often have multiple enzyme-catalysed steps, the end product of the whole process sometimes produces compounds that inhibit one of the enzyme-catalysed steps

19
Q

What types of bonds are responsible for competitive and non-competitive inhibitors when binding to the active site

A

competitive: IMFs
non-competitive: covalent bonds