4.2 - Factors Affecting Enzyme Activity Flashcards

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1
Q

How can factors affecting enzyme activity be investigated

A

Measuring rate of reactions they catalyse

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2
Q

Effect of temperature

A

Increasing temperature increases kinetic energy of particles.
As temp increases, particles move faster and collide more frequently
In enzyme controlled reaction, increase in temperature will result in more successful collisions = increase rate of reaction

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3
Q

Temperature coefficient

A

Q10. Measure of how much rate of reaction increases with a 10C rise in temp. Usually taken as 2 for enzymes (reaction doubles with 10C rise)

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4
Q

Denaturation from temperature

A

Enzymes are proteins.
Structure is affected by temperature.
At higher temperatures, bonds holding protein together vibrate more.
As temp increases, so do vibrations until bond strains and breaks.
Bond breakage causes tertiary structure of enzyme to change shape until it’s been denatured.

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5
Q

What happens when enzyme is denatured

A

Active site changes shape and is no longer complementary to substrate. Substrate no longer fits into active site and enzyme ceases to act as catalyst.

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6
Q

Optimum temperature

A

Temperature at which enzyme has highest rate of activity

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7
Q

Optimum temperature for many enzymes in human body

A

40*C

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8
Q

Optimum temperature for many thermophilic bacteria

A

70*C

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9
Q

Optimum temperature for enzymes in psychrophilic enzymes

A

Below 5*C

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10
Q

Difference between temperature being too high or too low

A

High - decrease is rapid denatured as active site has changed
Low - decrease less rapid as enzyme is just less active

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11
Q

Extremely cold environments

A

Deep oceans
High altitudes
Polar regions

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12
Q

Features if enzymes adapted to the cold

A

More flexible structures so are less stable than enzymes that work at higher temperatures
Smaller temperature changes denature them

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13
Q

What is a thermophile

A

Organism adapted to very hot environments

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14
Q

Examples of hot environments

A

Hot springs

Deep sea hydrothermal vents

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15
Q

Features of thermophilic enzymes

A

More stable due to increased number of bonds particularly H bonds and sulcus bridges in tertiary structures
Shape of enzymes and active sites are more resistant to temperature rises

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16
Q

What is a change in pH

A

Change in H ion concentration

17
Q

Why is pH important

A

Active site will only be correct shape when in certain H ion concentration

18
Q

How are proteins held in their precise 3D shape

A

H bonds & ionic binds betwieeen amino acid R groups. Bonds result from interactions between the polar and and charged R groups present on amino acids forming the primary structure

19
Q

What happens when pH changes from optimum

A

Structure of enzyme and active site site is altered.

If pH returns then protein returns to normal shape and catalyse reaction - renaturation

20
Q

How does H ion concentration affect enzymes

A

H ions interact with polar and charged R groups
Changing concentration changes degree of interaction
Interactions affect how R groups interact

21
Q

Effect of more H ions

A

Less R groups can interact

Bonds break and shape of enzyme changes

22
Q

Why does enzyme only function in narrow pH range

A

Shape of enzyme changes as pH changes

23
Q

Enzyme and substrate concentration

A

Increased number of either increases rate of collision of active site and substrate
Increases number for enzyme substrate complex
RoR can reach Vmax

24
Q

What happens at Vmax

A

All active sites are occupied. RoR can only be increased by increasing enzymes or temperature