Enzymes Flashcards

1
Q

What type of protein are most enzymes?

A

Globular proteins

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2
Q

Most enzymes are globular proteins, what characteristics do they have because of this?

A

Because of this enzymes are mostly spherical and water soluble

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3
Q

Why are enzymes water soluble?

A

They have to exist in the cell which has an aqueous environment

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4
Q

What do most enzymes do?

A

They make reactions happen quicker i.e. they make biological reactions happen at a rate that sustains life

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5
Q

Give three examples of different types of enzymes.

A

Abzymes
Ribozymes
DNAzymes

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6
Q

What do abzymes do?

A

They speed up reactions of the immune system

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7
Q

What do enzymes act on?

A

Other molecules/substances

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8
Q

After a long period of time and many uses, what will happen to an enzyme?

A

They will wear out and eventually degrade

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9
Q

What is the molecule that an enzyme acts on called?

A

The substrate

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10
Q

What is an active site?

A

The area on an enzyme where a reaction occurs

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11
Q

What happens at the active site?

A

There is a moving around of electrons and the forming/breaking of bonds

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12
Q

What is formed when the substrate binds to the active site of the enzyme?

A

The enzyme/substrate complex is formed

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13
Q

What is formed after the enzyme/substrate complex?

A

The enzyme/product complex is formed

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14
Q

What happens after the enzyme/product complex is formed?

A

The products leave the active site of the enzyme

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15
Q

What is the most common type of reaction that occurs to form products?

A

The substrate is split to form products

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16
Q

Describe the relationship between chemical reactions and enzyme reactions.

A

Enzyme reactions are a specialised type of chemical reaction

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17
Q

List four characteristics of a chemical reaction

A

Reactants converted into products

May involve catalyst

Rate of reaction can be measured

Rate increases as temperature increases without a limit

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18
Q

List four characteristics of an enzyme reaction

A

Substrates converted into products

Always involve catalyst (enzyme)

Rate of reaction can be measured

Rate increases as temperature increases up to a limit

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19
Q

What happens to enzymes when a certain high temperature is reached?

A

Denaturation occurs

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20
Q

What happens when an enzyme is denatured?

A

The active site is lost, there is nowhere for the substrate to bind to -> the reaction cannot occur

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21
Q

Give the name of one of the fastest enzymes.

22
Q

What does it mean if a word end with ‘ase’?

A

The ending ‘ase’ indicates an enzyme

23
Q

What type of molecule are protein enzymes?

A

They are polypeptides

24
Q

What are polypeptides?

A

They are long chains of different amino acids

25
Describe the structure of a polypeptide. | 3
Chain is folded to achieve a specific overall shape Usually looks like a bumpy globe (globular) Surface features based on the different amino acids (side chains)
26
What happens if an enzyme is not folded correctly?
The active site will not be in the correct place, the reaction cannot occur
27
What happens if a substrate doesn't fit in an active site?
The reaction will not happen
28
Describe the structure of the active site. | 4
It has a 3D conformation Amino acids protrude from the surface There is a specific arrangement Amino acids are often charged
29
What keeps the substrate in the active site?
Reactions such as those between oppositely charged areas of the substrate and the active site
30
What is needed for an enzyme/substrate reaction to occur? | 3
Large amounts of the substrate - the more substrate the greater the chance one will come in contact with the activation site Activation energy (Ea) - the energy needed for the reaction to start An enzyme needed to bend the substrate into a shape so the reaction occurs more quickly
31
What is activation energy?
The minimum amount of energy needed for a reaction to start
32
Give an example of one form of activation energy.
It can come in the form of ATP
33
How exactly do enzymes increase the rate of reaction? | 2
They do this by slightly changing the conformation/shape of the substrate so that its more like the product This allows the reaction to occur more easily and therefore increases the rate of reaction
34
What would happen if the substrate 100% rigid and unyielding?
The reaction would not occur
35
What is enzyme kinetics?
Measuring the rates of reaction of enzymes
36
Give two ways we know catalysts do anything.
An increase in product formation A decrease in amount of substrate
37
How do we study enzyme kinetics? | 2
By using a substrate that is practical and convenient to monitor i.e. it is highly coloured or fluorescent, radioactive etc We can then use a spectrophotometer to monitor the reaction
38
Why does the amount of free enzyme decrease?
It decreases as the enzyme/substrate complex is made -> the ES complex increases
39
What happens as the amount of substrate decreases?
The amount of product increases
40
What does the Michaelis-Menten Equation allow us to do?
It allows us to calculate the expected velocity at a given [S] as we have established the Vmax and Km for an enzyme/substrate reaction pair
41
What is the Michaelis-Menten Equation?
Velocity = Vmax [S]/Km + [S]
42
What is the common rule of thumb for the relationship between temperature and rate of reaction?
That a 10 degrees increase in temperature doubles the rate of reaction (this only happens up to a certain point for enzyme reactions)
43
What is actually happening in enzyme inhibition?
The enzyme cannot complete a catalytic cycle
44
What is formed in enzyme inhibition?
An enzyme inhibitor complex is formed (EI complex)
45
What are the two forms of an EI complex?
Reversible of irreversible | two types of inhibition
46
What happens in reversible inhibition? | 3
The inhibitor can bind to and dissociate from the enzyme Activity is lost when the inhibitor is bound Must wait for the enzyme to become free to overcome this inhibition
47
What happens in irreversible inhibition? | 2
The enzyme is covalently modified and the activity is lost Must replace the enzyme to overcome this inhibition
48
What are the three forms of reversible inhibition?
Competitive Uncompetitive Mixed
49
What happens in competitive inhibition? | 2
The inhibitor binds at the active site This prevents the substrate from binding
50
What happens in uncompetitive inhibition? | 2
The inhibitor bind to the enzyme-substrate complex This does not happen at the active site
51
What happens in mixed inhibition?
The inhibitor can bind to the free enzyme of the enzyme substrate complex
52
How does pH influence enzyme activity?
By altering amino acid structure - particularly those in the active site