B4 - Enzymes Flashcards

1
Q

What are enzymes?

A

Biological catalysts that speed up chemical reactions but are not changed or used up in the process
- long chains of amino acids that fold up to have different shapes that allow specific binding of substrates
- they are protein molecules

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2
Q

Metabolic pathways

A

Sequences of enzymatically catalysed chemical reactions in a cell
- since every chemical reaction within a cell is controlled by an enzyme: a group of these reactions makes a metabolic pathway

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3
Q

Catabolic pathways

A

Complex molecules are broken down to simpler ones and energy is released
- e.g. digestion

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4
Q

Anabolic pathways

A

Build up large chemicals and compounds which requires energy
- e.g. making glycogen in your liver

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5
Q

Lock and Key Theory

A

Theory of enzyme catalysis stating that the active site’s structure is complementary to the structure of the substrate

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6
Q

Active site

A

A region on an enzyme that binds to a protein or other substance during a reaction
- complementary in shape to the substrate it binds to forming an enzyme-substrate complex

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7
Q

Substrate

A

A specific reactant acted upon by an enzyme

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8
Q

Factors affecting enzyme activity (4)

A
  • Temperature
  • pH
  • Enzyme concentration
  • Substrate concentration
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9
Q

Enzyme Concentration on Enzyme Activity

A
  • Increasing the concentration of enzymes increases the rate of reaction
  • Enzymes are more likely to collide with substrates and therefore more E-S complexes form
  • If the concentration of substrate is limited then eventually there will be no further effect
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10
Q

Substrate Concentration on Enzyme Activity

A
  • Increasing the concentration of substrate increases the rate of reaction (True up to a saturation point)
  • Collisions are more likely so more E-S complexes form
  • The concentration will decrease over time therefore the rate of reaction will also decrease
    - therefore, the initial rate is the highest
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11
Q

What are optimum conditions?

A

Conditions in which the enzyme works best in

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12
Q

Optimum temperature for enzymes

A

37˚C body temp

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13
Q

What are reactions without enzymes like?

A

The reactions would need a lot more energy to take place
- chemical reactions need something to decrease their duration and increase their quality

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14
Q

Temperature on enzyme activity

A
  • Increasing the temperature increases the rate of reaction
  • The increase in kinetic energy means they can move faster and are more likely to collide and form E-S complexes
  • Increasing the temperature above the optimum can break bonds which results in the active site changing
  • The substrate no longer fits as the enzyme is denatured and doesn’t function as a catalyst
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15
Q

Complementary shape of an enzyme

A

The shape of the active site of an enzyme which is corresponding to the shape of the substrate

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16
Q

Denatured enzyme

A

An enzyme which no longer functions because its shape and active site has been changed and the substrate can no longer fit

17
Q

pH on enzyme activity

A
  • All enzymes have an optimum pH value.
  • Higher or lower than this the enzyme will denature and the active site changes shape
  • At this point the enzyme is no longer functional.
18
Q

Optimum pH for enzymes

A

Differs from enzymes, the only optimum condition enzymes in animal bodies share is optimum temperature

19
Q

Pepsin

A

Enzyme that breaks down proteins in the stomach

20
Q

Amylase

A

Enzyme in saliva that breaks the chemical bonds in starches

21
Q

Trysin

A

An enzyme in pancreatic juice that breaks down protein molecules

22
Q

Optimum pH for amylase, trysin and pepsin

A
  • amylase: approx. 7 pH
  • trypsin: 8-8.5 pH
  • pepsin: 1.9 pH
23
Q

Range of activity for amylase

A

approx. 4-10

24
Q

Range of activity for trypsin

A

approx. 5.8-10

25
Q

Range of activity for pepsin

A

0-3.5