Enzymes Flashcards

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1
Q

Why are enzymes biological catalysts?

A

They are found in living organisms and increase the rate of reaction.

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2
Q

Substrate molecule

A

The molecule the enzyme attaches to.

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3
Q

What type of protein are the vast majority of enzymes?

A

Globular proteins

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4
Q

How do enzymes bond to the substrate molecule?

A

Via the complementary active side, where amino acids on the surface form temporary bonds.

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5
Q

Activation energy

A

Energy required for a reaction to occur.

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6
Q

What do enzymes do to the activation energy barrier?

A

Reduce it

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7
Q

Is the lock and key or induced fit model correct?

A

Induced fit model.

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8
Q

Lock and key model

A

The tertiary structure of the enzyme does not change.

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9
Q

Induced fit model

A

The tertiary structure of the enzyme changes so the active site moulds itself around the substrate.

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10
Q

Optimum temperature for human enzymes

A

40’C

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11
Q

How do enzymes denature?

A

Tertiary structure changes / temporary bonds break, meaning the enzyme is no longer complementary.

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12
Q

pH

A

Concentration of hydrogen ions.

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13
Q

How to find pH on calculator

A

pH = -log (H+)

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14
Q

Effect of temperature on rate of reaction.

A

Increases due to increased kinetic energy, more successful collisions.

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15
Q

Where does a competitive inhibitor bind?

A

Active site of an enzyme.

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16
Q

Where does a non-competitive inhibitor bind?

A

Allosteric site rather than active site.

17
Q

How do competitive inhibitors work?

A

Have a similar structure to the substrate so prevent it binding to the active site.

18
Q

How do non-competitive inhibitors work?

A

By binding to the allosteric site, the tertiary structure of the changes meaning it is no longer complementary.

19
Q

How to reduce the effect of a competitive inhibitor.

A

Increase substrate concentration

20
Q

Can you decrease the effect of a non-competitive inhibitor with increased substrate concentration?

A

No as it changes the tertiary structure meaning the substrate can not bind.