2.4 Enzymes Flashcards

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1
Q

What are enzymes?

A

Biological catalysts that affect the rate of reactions and remain chemically unchanged

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2
Q

What do Enzymes do?

A

Find an alternative route for a reaction to take place that requires a lower activation energy

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3
Q

Enzymes are soluble in solvents. Why?

A

They are globular proteins which have hydrophilic interactions on the outside and hydrophobic interactions on the inside

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4
Q

Where are Enzymes found?

A

Everywhere, every cell contains enzymes. Enzymes are involved in every chemical reactions

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5
Q

What is the description of the graph for Temperature (in relation to factors that affect enzyme action).

A

The graph has a steady increase until it reaches a peak. After the peak the rate of reaction will rapidly decline, some quicker than others based on the different enzymes.

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6
Q

What is the explanation of the graph for Temperature (in relation to factors that affect enzyme action).

A

It increases steadily at the beginning because there is an increase in kinetic energy and collisions due to the temperature increasing which will cause increased enzyme-substrate complex , enzyme-product complex and products. When it reaches the optimum it means that the likelihood of collisions is the highest. During the decrease, it leads to the enzyme becoming deactivated (when it’s too cold, it deactivated which is reversible instead of denaturing which is not reversible. It denatures when it gets too hot). This is because hydrogen and ionic bonds have been broken which leads to a change in shape of the active site. The active site is no longer complementary so there is no enzyme-substrate complex , enzyme-product complex or products

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7
Q

What is the description of the graph for pH (in relation to factors that affect enzyme action).

A

The graph will have a peak at a specific pH and when the pH gets further away from the peak number, the rate of reaction will decrease until it gets to 0 at points furthest from the peak. The increases are rapid.

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8
Q

What is the explanation of the graph for pH (in relation to factors that affect enzyme action).

A

When the rate of reaction is at 0 it means that hydrogen and ionic bonds have been broken which leads to a change in shape of the active site. The active site is no longer complementary so there is no enzyme-substrate complex , enzyme-product complex or products causing the 0. When the pH is at the peak, it means it is the optimum. At the optimum pH, there are more frequent collisions between enzyme and substrate which means there are high levels of enzyme-substrate complex, enzyme-product complex and products.

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9
Q

What is the description of the graph for enzyme concentration (in relation to factors that affect enzyme action).

A

the rate of reaction gradually increases as the enzyme concentration increases until it reaches a point to which it will plateau. Even if the enzyme concentration increases after the point, the rate of reaction won’t change.

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10
Q

What is the explanation of the graph for enzyme concentration (in relation to factors that affect enzyme action).

A

There will be an increase because there are more enzymes so that the substrates have more of a chance of colliding with an active site. There is an increase in enzyme-substrate complex, enzyme-product complex and products. The data will plateau because there is another limiting factor which is the substrate concentration.

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11
Q

What is the description of the graph for substrate concentration (in relation to factors that affect enzyme action).

A

the rate of reaction gradually increases as the substrate concentration increases until it reaches a point to which it will plateau. Even if the substrate concentration increases after the point, the rate of reaction won’t change.

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12
Q

What is the explanation of the graph for substrate concentration (in relation to factors that affect enzyme action).

A

There will be an increase because there are more enzymes so that the substrates have more of a chance of colliding with an active site. There is an increase in enzyme-substrate complex, enzyme-product complex and products. The data will plateau because there is another limiting factor which is the enzyme concentration.

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13
Q

What is the lock and key theory?

A

There is only one substrate that will fit the active site of the enzyme The substrate exactly fits the enzyme and the active site is complementary

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14
Q

What is it called when the enzyme and the substrate collide at the right angle due to the activation energy?

A

Enzyme-substrate complex

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15
Q

What is it called when an enzyme breaks down the substrate?

A

Enzyme-product complex

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16
Q

What is induced fit?

A

The enzyme’s active site will mold slightly around the substrate.

17
Q

Why is the lock and key theory not entirely accurate?

A

Substrate will never be the perfect fit for the enzyme’s active site.

18
Q

What is a buffer?

A

Maintains a certain variable. Also, a buffer is something that resists changes in pH or maintains the pH.

19
Q

What is an example of where a buffer works?

A

Certain chemicals in blood that help resist changes in pH so that the blood pH remains within fairly narrow limits close to pH 7.4.

20
Q

What can the chemicals in the blood do?

A

Accept or donate hydrogen ions (which are protons)

21
Q

What is an enzyme inhibitor?

A

Substance that reduces or stops a reaction.

22
Q

What are competitive inhibitors?

A

Where the inhibitor molecule has a similar shape to the substrate molecule.

23
Q

What do competitive inhibitors do?

A

Compete with the substrate for the enzyme’s active site. It then blocks the active site so reduced enzyme-substrate complex, enzyme-product complex and products. They are reversible by increasing the substrate concentration.

24
Q

Are competitive inhibitors reversible?

A

They are technically reversible by increasing the substrate concentration.

25
Q

What are non-competitive inhibitors?

A

don’t connect to the active site and instead attach to the allosteric site.

26
Q

What do non-competitive inhibitors do?

A

causes the enzyme’s active site to change which prevents enzyme-substrate complex, enzyme-product complex and products because the active site is no longer complementary to the substrate.

27
Q

Are non-competitive inhibitors reversible.

A

They are not reversible as the enzyme denatures.

28
Q

What are examples of enzyme inhibitors?

A

Pathogens, drugs, toxins, venoms.

29
Q

What are cofactors?

A

Mineral ions

30
Q

What do cofactors do?

A

A substance that has to be present to ensure that an enzyme-catalysed reaction takes place at the appropriate rate.

31
Q

What are coenzymes?

A

Chemical compounds that help the enzymes

32
Q

What are prosthetic groups?

A

Ions that are somehow integrated into the structure

33
Q

Are cofactors apart of the enzyme structure?

A

Some are, but others form temporary associations with the enzymes