Enzymes Flashcards

1
Q

Enzyme

A

An enzyme is a protein biological catalyst that speeds up chemical reactions by lowering the activation energy.

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2
Q

Biochemical pathway

A

Biochemical pathways involve multiple steps where an enzyme catalyses each step, and the product of the reaction becomes the reactant to the next step.

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3
Q

3 part enzyme diagram (synthesis)

A

Enzyme
Substrates (2)
Specific and complimentary active site
Enzyme-substrate complex
Product (1)
3 arrows

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4
Q

Temperature below optimum plan

A

Inactive (temp ↓ optimum)
↓kinetic energy =
↓ successful collisions =
↓ enzyme-substrate complexes=
↓products + ↓ rate of reaction

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5
Q

Temperature above optimum plan

A

Denatured (temp ↑ optimum)
Active site changes shape so it is no longer specific and complimentary to substrate
↓ successful collisions =
↓ enzyme-substrate complexes=
↓products + ↓ rate of reaction

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6
Q

pH below optimum plan

A

Denatured (pH below optimum)
Active site changes shape so it is no longer specific and complimentary to substrate
↓ successful collisions =
↓ enzyme-substrate complexes=
↓products + ↓ rate of reaction

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7
Q

pH above optimum plan

A

Denatured (pH below optimum)
Active site changes shape so it is no longer specific and complimentary to substrate
↓ successful collisions =
↓ enzyme-substrate complexes=
↓products + ↓ rate of reaction

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8
Q

Enzyme temperature graph

A
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9
Q

Enzyme pH graph

A
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10
Q

Enzyme concentration graph

A
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11
Q

Enzyme substrate concentration graph

A
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12
Q

Why does an enzyme substrate concentration graph plateau?

A

The enzymes become saturated (active sites become full)

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13
Q

What is a limiting factor?

A

A factor that prevents the rate of reaction from increasing any further

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14
Q

What could be the limiting factor in an enzyme substrate concentration graph?

A

Enzyme concentration

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15
Q

Competitive inhibitor plan

A

Competitive inhibitor is specific and complimentary to active site of enzyme
It attaches to active site
Substrate can’t attach
Less enzyme-substrate complexes
Less products + lower rate of reaction

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16
Q

Non-competitive inhibitor plan

A

Non-competitive inhibitors bind to the allosteric site
Active site changes shape so it is no longer specific and complimentary to substrate
↓ successful collisions =
↓ enzyme-substrate complexes=
↓products + ↓ rate of reaction

17
Q

Enzyme diagram- competitive inhibitor

18
Q

Enzyme diagram- non-competitive inhibitor

19
Q

Catalase substrate

A

Hydrogen peroxide

20
Q

Catalase products

A

water and oxygen

21
Q

How to test if an inhibitor is competitive or non-competitive

A

Increase substrate concentration.
If rate of reaction increases, the inhibitor is competitive
If rate of reaction stays the same / does not increase, the inhibitor is non-competitive