Unit 3 AOS 2: Biochemical pathways Flashcards

Biology

1
Q

Anabolic reactions

A
  • Building up molecules
  • Needs energy
  • Endothermic
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2
Q

Catabolic reactions

A
  • Breaking down molecules
  • Releases energy
  • Exothermic
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3
Q

Why are enzymes beneficial to cells?

A

1) They speed up biochemical reactions.
2) They lower activation energy.

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4
Q

Active site

A

Where the substrate binds to the enzyme. It orientates the substrate into the correct position for the reaction to take place.

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5
Q

Where does the substrate bind?

A

The active site of the enzyme.

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6
Q

Substrate

A

The molecule that an enzyme binds to.

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7
Q

Product

A

The final molecule made by the enzyme.

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8
Q

3 factors that effect enzyme function?

A

1) temperature
2) pH
3) concentration

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9
Q

Optimal temperature

A

The temperature at which the enzyme works best.

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10
Q

Denaturation

A

Occurs when enzymes are moved out of their optimum range. It is irreversible and causes the bonds holding the enzymes together to break, causing a change in protein structure/shape.

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11
Q

What happens when the proteins are heated past their optimal temperature?

A

They undergo denaturation.

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12
Q

What happens when proteins are at a temperature too low?

A

Enzymes slow down and stop functioning (this is reversible and not denaturation)

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13
Q

What is the effect of pH?

A

Changes in pH can alter a protein’s shape, especially its active site, affecting its function. Each enzyme has an optimal pH range, and if it moves outside this range, the enzyme can denature and lose its ability to work.

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14
Q

What are enzymes?

A

Organic catalysts that often influence entire biochemical pathways.

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15
Q

Competitive inhibitor

A

Able to bind to the enzyme at the active site but doesn’t trigger a reaction. This blocks the substrate from being able to bind to the active site.

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16
Q

Non-competitor inhibitor

A

Will bind to the enzyme at the allosteric site (site other than active site) which causes the shape of the enzyme to change so the substrate can no longer fit.

17
Q

Reversible inhibitors

A

Form weak bonds with enzymes which can break. They slow but don’t stop the rate of reaction.

18
Q

Irreversible inhibitors

A

Form strong bonds with enzymes, resulting in that enzyme being unable to catalyse reactions indefinitely. These are mostly competitive inhibitors.

19
Q

Are non-competitive inhibitors affected by substrate concentration?

20
Q

How are competitive inhibitors overcome?

A

By increasing the substrate concentration.