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AS Biology > Enzymes > Flashcards

Enzymes Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

What does Catalase do?

A

Catalyses breakdown of hydrogen peroxide into water and oxygen

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2
Q

Is the breakdown of hydrogen peroxide intracellular or extracellular?

A

Extracellular

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3
Q

What does Amylase do?

A

Catalyses breakdown of carbohydrates from Starch to Maltose

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4
Q

What does Pepsin do?

A

Catalyses breakdown of proteins to peptides

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5
Q

Outline the Lock and Key hypothesis

A
  • Enzyme’s active site is formed by its’ tertiary structure and is complementary to substrate.
  • Substrate fits exactly in active site
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6
Q

Outline the induced fit hypothesis

A
  • Active site isn’t exactly matched to the substrate

- Active site changes slightly to better accommodate the substrate

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7
Q

What do Cofactors do?

A

Stabilise the E+S complex

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8
Q

Name the two ways in which cofactors can act to stabilise the E+S complex

A
  • As Co-substrates

- alter charge distribution

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9
Q

What is the definition of a ‘Prosthetic Group’?

A

A type of Cofactor

permanently bound to the enzyme

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10
Q

What cofactor is used by Carbonic Anhydrase?

A

Zinc

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11
Q

What is the definition of a Coenzyme?

A

A type of cofactor which is a non-protein molecule that is necessary for the function of the enzyme

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12
Q

Are coenzymes chemically changed in a reaction?

A

Yes

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13
Q

Where does a coenzyme bind to?

A

Temporarily, to the active site

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14
Q

When is an ES complex formed?

A

When the enzyme and substrate collide with enough kinetic energy

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15
Q

What bonds hold the ESC together?

A

Hydrogen bonds

Non-covalent

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16
Q

What is the effect of PH on enzyme activity?

A
  • PH change interferes with hydrogen bonding in in the enzyme’s tertiary structure
  • The enzyme’s tertiary structure is optimal for most efficient action
17
Q

What is the effect of temperature on enzyme activity?

A
  • Increase in temp means increase in rate

- more likely to collide with enough kinetic energy to form ESC

18
Q

What happens when temp increases beyond the enzymes’ optimum temp?

A

Enzyme becomes denatured. Hydrogen bonds maintaining the tertiary structure are broken, so active site changes shape

19
Q

What happens when an enzyme becomes denatured?

A

Active site no longer complementary to substrate, enzyme becomes totally inefficient

20
Q

What is the effect of enzyme concentration on enzyme activity?

A

ROR and enzyme concentration are directly proportional

21
Q

What is the effect of substrate concentration on enzyme activity?

A

ROR and substrate concentration are directly proportional, up to a point = Vmax

22
Q

What is Vmax?

A

At Vmax, all enzyme active sites are occupied, with no available active sites are free to bind with substartes

23
Q

What happens at Vmax?

A

The amount of enzyme becomes the limiting factor

24
Q

What is the definition of a Cofactor?

A

A non-protein component of an enzyme that is required in order for the enzyme to function

25
Q

What can inhibitors do?

A

Decrease the ROR of enzyme controlled reactions

26
Q

Describe Competitive inhibitors

A
  • Fits in Active site, but does not react
  • Competes with substrate for active sute
  • Effect is concentration dependant
  • Effects are reversible/minimised by raising substrate conc.
27
Q

Describe Non-Competitive inhibitors

A
  • Binds to allosteric site
  • Changes molecule shape preventing it working
  • This is permanent and cannot be rectified
  • Effect is dependant of substrate concentration
28
Q

What is Q10 temperature coefficient?

A

It shows how much the rate of reaction changes when the temperature is raised by 10 degrees

29
Q

What is the Q10 value of most enzyme-controlled reactions?

A

2

30
Q

What is End-product inhibition?

A

When the final product in a metabolic pathway inhibits an enzyme that acts earlier on in the pathway

AS Biology (12 decks)

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