Enzymes Flashcards

(44 cards)

1
Q

What do enzyme-substrate complexes reduce?

A

Activation energy.

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2
Q

Why does an enzyme-substrate complex reduce activation energy?

A

Because it bends bonds.

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3
Q

What energy do few substrates have without enzymes?

A

Sufficient energy for the reaction.

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4
Q

What is the shape of the active site before binding in the induced fit model?

A

Not complementary.

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5
Q

What changes in the enzyme during induced fit?

A

The active site shape.

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6
Q

What does the change in enzyme shape during induced fit allow?

A

Substrate to fit / enzyme-substrate complex to form.

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7
Q

What forms when the substrate binds to the enzyme?

A

An enzyme-substrate complex.

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8
Q

What changes slightly to fit the substrate in the induced fit model?

A

The active site.

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9
Q

What does the active site do to bonds in the substrate?

A

Distorts/breaks/forms them.

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10
Q

What does induced fit do to activation energy?

A

Reduces it.

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11
Q

In the lock and key model, how does the active site behave?

A

Fixed/rigid shape.

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12
Q

Why does the substrate fit the enzyme in the lock and key model?

A

Active site is already complementary.

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13
Q

Why does an enzyme catalyse only one reaction?

A

Its active site has a specific shape.

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14
Q

What fits the enzyme’s active site?

A

Only one specific substrate.

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15
Q

What happens to enzyme activity as substrate concentration increases?

A

Increases then plateaus.

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16
Q

Why does enzyme activity plateau at high substrate concentration?

A

All active sites are occupied.

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17
Q

What forms per second at maximum substrate concentration?

A

Maximum number of enzyme-substrate complexes.

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18
Q

What happens to rate as enzyme concentration increases?

A

Increases then plateaus.

19
Q

Why does increasing enzyme concentration plateau the rate?

A

Substrate becomes limited.

20
Q

Why does increasing temperature increase enzyme activity?

A

More kinetic energy.

21
Q

What increases due to kinetic energy at higher temperature?

A

Enzyme-substrate complexes.

22
Q

What happens to enzymes above optimum temperature?

A

They denature.

23
Q

What structure changes when an enzyme denatures?

A

Tertiary structure.

24
Q

What happens to the active site when an enzyme denatures?

A

It changes shape.

25
What happens to enzyme activity when pH changes from optimum?
Decreases.
26
What bonds are broken when pH changes?
Ionic bonds and weak hydrogen bonds.
27
What part of the amino acid is affected by pH change?
R group charge.
28
Why can’t the substrate bind at extreme pH?
Active site changes shape.
29
What is the shape of a competitive inhibitor?
Similar to the substrate.
30
Where does a competitive inhibitor bind?
The active site.
31
What is the result of competitive inhibition?
Fewer enzyme-substrate complexes form.
32
Where does a non-competitive inhibitor bind?
At a site other than the active site (allosteric site).
33
What does a non-competitive inhibitor change?
The enzyme's tertiary structure.
34
Why can't the substrate bind during non-competitive inhibition?
Active site no longer complementary.
35
What does a DNA mutation change in a protein?
The primary structure.
36
What bonds form in different places after a mutation?
Hydrogen, ionic, and disulphide bonds.
37
What does this bond change alter?
The enzyme’s tertiary structure.
38
What can’t form if the active site shape is altered?
Enzyme-substrate complexes.
39
What is the proteome of a cell?
The full range of proteins a cell can produce at a given time.
40
What else can the proteome refer to?
The full range of proteins the genome can code for.
41
What do antigens on pathogens have?
A specific shape / specific tertiary structure.
42
Why do antibodies only bind specific pathogens?
Antibody is complementary to antigen / forms antibody-antigen complex.
43
Why can't insulin be taken orally?
It is broken down by enzymes / denatured / too large to absorb.
44
What happens to insulin if digested?
It becomes non-functional.