Biological Molecules - Enzymes Flashcards

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1
Q
A
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2
Q

What are the conditions required for enzyme reactions?

A

The molecules need to collide with enough energy to alter the molecular arrangement

The substrates must have the minimum amount of energy (activation energy)

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3
Q

How do enzymes alter their conditions in order to break down substrates?

A

they put strain on the active site which lowers activation energy, allowing reactions to take place at lower temperatures eg 37 degrees

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4
Q

Why do enzymes denature above 37 degrees?

A

The hydrogen bonds between the NH and OH groups are broken, causing the enzyme to change shape - denaturing the enzyme

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5
Q

Describe the induced fit model of enzymes

A

The active site of the enzyme only takes the shape of the substrate when they collide

flexibility in polypeptide chains allows enzyme to shape its active site around substrate - if all the bonds are formed in the right places T

now used in the place of the lock and key theory

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6
Q

Describe the lock and key model for enzymes

A

The enzyme is constantly shaped to fit the substrate - it never changes shape

This is inaccurate and no longer used

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7
Q

What are the factors affecting enzyme activity?

A

Temperature

pH

enzyme concentration

substrate concentration

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8
Q

How does the temperature affect enzyme activity?

A

Increases enzyme activity up to 37 degrees

After 37 degrees the enzymes begin to denature H+ bonds to holding together the tertiary structure breaks active site deforms

Below - not enough E to react

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9
Q

How does pH affect enzyme activity?

A

If the pH is above OR below optimum pH, the H+ and OH- bonds interfere with the ionic and H bonds in tertiary structure, deforming the active site and denaturing the enzyme

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10
Q

What is the optimum pH for enzymes?

A

Most in humans is around pH 7

However pepsin (digests proteins in the stomach) has an optimum pH of 2

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11
Q

What are the 2 types of enzyme inhibition?

A

Competitive and non-competitive

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12
Q

What is competitive inhibition?

A

When a molecule other than the enzyme’s specific substrate is complementary to the active site of the enzyme, occupying the enzyme and slowing down the rate of reaction

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13
Q

What is non-competitive inhibition?

A

When a molecule attaches itself to the enzyme (not the active site) and distort the enzyme shape, denaturing it

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14
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