Enzymes

Question 1

What biological molecule are enzymes made out of?

Answer 1

Proteins

Question 2

What are enzymes?

Answer 2

Biological catalysts

Question 3

What do anabolic enzymes do?

Answer 3

Builds molecules

Question 4

What do catabolic enzymes do?

Answer 4

Breaks down molecules

Question 5

Enzymes provide an area in which a reaction can happen by…?

Answer 5

Actively forcing a reaction

Question 6

Can enzymes be used repeatedly?

Answer 6

Yes

Question 7

Define active site

Answer 7

An area on which an enzyme-substrate binds

Question 8

Define tertiary structure

Answer 8

A 3D shape which is caused by bonds and interactions

Question 9

Define intracellular enzymes

Answer 9

Enzymes which catalyse reactions inside a cell

Question 10

Define extracellular enzymes

Answer 10

Enzymes which catalyse reactions outside a cell

Question 11

An enzyme has a … centre and a … outside

Answer 11

An enzyme has a hydrophobic centre and a hydrophilic outside

Question 12

Why does the pH affect enzymes?

Answer 12

As the extra H+ ions disrupt the hydrogen and ionic bonding within a molecule

Question 13

How does pH denature enzymes?

Answer 13

When the hydrogen and ionic bonds are disrupted, this can lead to the active site altering in structure or change. Some active sites have specific charges that allow it to bond with specific substrates. Therefore, the pH hinders bonding ability.

Question 14

How does temperature denature enzymes?

Answer 14

A high-temperature causes vibrations within the molecule. This weakens the bonds within the tertiary structure. This changes the 3D shape, which causes a change in structure and a proteins (enzymes’) job is reliant on its structure

Question 15

Name the two enzyme theories

Answer 15

Lock and Key

Induced Fit Theory

Question 16

What is the Lock and Key theory?

Answer 16

Once the substrate with the correct shape enters the active site, a reaction will occur. This is because the active site is directly complementary to the substrate shape.

Question 17

What is the Induced Fit theory?

Answer 17

The substrate collides with the active site and the active site changes shape due to attractive charges. The change in shape destabilises the substrate and helps to weaken and break bonds

Question 18

What is an enzyme-substrate complex?

Answer 18

Combination of the substrate and enzyme

Question 19

What is a competitive inhibitor?

Answer 19

A substance that slows down an enzyme reaction in any way

Question 20

How does a competitive inhibitor slow down an enzyme reaction?

Answer 20

It blocks the active site by binding briefly with it

Question 21

Why can’t enzymes catalyse competitive inhibitors?

Answer 21

Because enzymes are specific

Question 22

The change in shape that most competitive inhibitors cause is…?

Answer 22

Reversible

Question 23

What is a non-competitive inhibitor?

Answer 23

A substance that binds permanently to the enzymes allosteric site

Question 24

What does a non-competitive inhibitor cause?

Answer 24

Irreversible damage so the enzyme denatures

Question 25

What is a cofactor?

Answer 25

A substance that helps to control the rate of enzyme reactions. Some are attached to the molecule

Question 26

What is a coenzyme?

Answer 26

Organic molecules that bind briefly to the active site before or at the same time as the substrate

Question 27

Why may coenzymes not be able to be reused?

Answer 27

When the enzymes reaction is finished, the coenzyme may be changed