4 Enzymes Flashcards

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1
Q

What is an enzyme?

A

A biological catalyst
Made of protein
Lowers activation energy
The active site is complementary to the substrate

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2
Q

How do you test for enzymes in a sample?

A

(Test for proteins)
Biuret’s solution

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3
Q

Intracellular vs extracellular

A

Intracellular: inside cell e.g. catalase
Extracellular: outside cell e.g. amylase

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4
Q

Define a catabolic reaction.

A

Break down

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5
Q

Define anabolic reaction.

A

Build up

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6
Q

State if the following are intracellular or extracellular enzymes:
a) catalase
b) trypsin
c) amylase

A

a) intracellular
b) extracellular
c) extracellular

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7
Q

State what the following enzymes catalyse the break down of and the products formed:
a) catalase
b) trypsin
c) amylase

A

a) hydrogen peroxide into water and oxygen
b) proteins into amino acids (hydrolysis of peptide bonds)
c) starch into maltose (hydrolysis)

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8
Q

Explain the lock and key hypothesis.

A

Substrate enters active site
Enzyme-substrate complex formed
Substrate broken down
Enzyme-products comped formed
Products leave active site

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9
Q

Explain the induced fit hypothesis.

A

Substrate enters active site
Enzymes-substrate complex is formed
Active sight slightly changes shape as substrate binds
Substrate is complementary to active site
Products leave the active site of enzyme

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10
Q

Explain one difference between the induced fit hypothesis and the lock and key hypothesis.

A

Lock and key hypothesis- the enzymes is rigid and the active site does not change shape
Induced fit hypothesis- the active site changes shape slightly as the substrate binds

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11
Q

How do enzymes lower activation energy?

A

When the substrate binds and forms an enzyme-substrate complex it strains the substrate
This distorts the bonds
And lowers the activation energy

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12
Q

What does it mean if an enzymes denatures?

A

The shape of the active site has changed
The enzyme-substrate complex cannot form
The enzyme no longer functions

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13
Q

Name 5 factors that have an effect on enzyme activity.

A

Temperature
pH
Concentration of substrate
Concentration of enzyme
Inhibitors

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14
Q

Name 3 ways enzyme catalytic reactions can be measured.

A

Measure the:
Disappearance of products
Formation of products
Rate of reaction

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15
Q

Describe how enzyme activity is affected as temperature increases/ at different pH’s.

A

Initially, the rate of reaction increases rapidly until it reaches a peak (easy enzyme-substrate contact).
After this, the rate of reaction decreases rapidly until it is finished.
Peak= optimum temperature/pH

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16
Q

Explain the term biological catalyst.

A

A substance that increases the rate of reaction
By lowering the activation energy
It speeds up metabolic reactions

17
Q

Describe how substrate and enzyme concentration affects rate of reaction/ enzyme activity.

A

As long as the enzyme/substrate concentration is high enough, the relationship between the enzyme/substrate concentration and rate of reaction is linear.
If the enzyme/substrate concentration is not high enough then Vmax is reached (maximum rate of reaction).

18
Q

What is the equation for the temperature coefficient?

A

Q10= rate at (t + 10 degrees)/ rate at t degrees

19
Q

What bonds are affected when an enzyme denatures and which structure are these bonds in?

A

Hydrogen and ionic bonds
Tertiary structure

20
Q

Is a denatured enzyme due to
a) temperature
b) pan
always permanent? Explain your answer.

A

a) yes- the specific shape of the active site is lost
b) no- if the structure is not changed significantly, renaturation can occur (original shape of active site is returned)

21
Q

Explain how low temperature affects enzymes.

A

The number of successful collisions decreases
Because the molecules have less kinetic energy
Therefore, fewer complexes are formed
And the rate of reaction is slower

22
Q

Explain how increasing the temperature affects enzymes.

A

The number of successful collisions increases
Because the molecules have more kinetic energy
More substrate-complexes are formed (and more products are formed)
And rate of reaction is faster

23
Q

Define the term ‘inhibitor’ in relation to enzymes.

A

A substance that indirectly or directly interferes with the functioning of the active site of an enzyme.
Most are temporary attachments, but there are also permanent inhibitors.

24
Q

Describe the differences between competitive and non-competitive inhibitors.

A

Competitive (C): similar shape to substrate
Non-competitive (N): doesn’t have to be like the substrate
C: can fit into active site of enzyme
N: attached to inhibitor site
C: competes with substrate
N: does not compete with substrate
C: causes a shower reaction
N: causes a change in shape of the active site so the enzyme cannot bind
C: direct
N: indirect

25
Q

What is end product inhibition?

A

The end product of a chain of reactions inhibits the enzyme in an earlier reaction (in the chain).

26
Q

What is a cofactor?

A

A non-protein substance
That binds to an enzyme
And is needed for the enzyme to function

27
Q

What is a coenzyme?

A

An organic cofactor (has carbon)

28
Q

What is a prosthetic group?

A

A cofactor
That is permanently attached to an enzyme.

29
Q

How do inorganic cofactors work?

A

They are (often) carriers- they move chemical groups from one enzyme to another
They are changed by participating in a reaction.

30
Q

What is precursor activation?

A

When an enzyme is activated by something to work.

31
Q

How do inorganic cofactors work?

A

They help the enzyme and substrate bind (change the shape of the active site to make fit better).
They are not part of the reaction.

32
Q

What is the cofactor for amylase?

A

Chlorine ion (Cl-)

33
Q

What enzyme is a zinc ion a prosthetic group for?

A

Carbonic anhydrase

34
Q

Name a source of coenzymes.

A

Vitamins