1b. ENZYMES Flashcards

1
Q

Define what an enzyme is

A

A biological catalyst

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2
Q

How do all enzymes speed up chemical reactions?

A

By lowering the activation energy

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3
Q

Why must enzymes be water soluble?

A

Because most enzyme controlled reactions occur in the cytoplasm or tissue fluid, which are aqueous

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4
Q

Give an example of an extracellular enzyme controlled reaction

A

Digestion

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5
Q

Give an example of an intracellular enzyme controlled reaction

A

Respiration, photosynthesis, protein synthesis

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6
Q

What is the functional part of an enzyme?

A

Active site

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7
Q

What is the 3D shape of an enzyme’s active site determined by?

A

The type and position of the hydrogen, covalent, ionic and disulphide bonds in its tertiary shape

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8
Q

Compare the shape of the substrate and the shape of the active site

A

They are complimentary

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9
Q

When an ESC is formed, what two things are interacting?

A

The substrate and the enzyme

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10
Q

Recall the two theories that describe how enzymes lower activation energy

A

Lock & key and induced fit

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11
Q

In the lock and key model, is the active site always complimentary to the substrate?

A

Yes

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12
Q

In the induced fit model, when is the active site not totally complimentary to the substrate?

A

Before the ESC is formed

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13
Q

Describe how thebinding of the substrate lowers activation energy in the induced fit model

A

As the active site changes shape, it distorts the bondswithin thesubstrate, lowering the activation energy.

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14
Q

Recall the two equations used to calculate rate of reaction

A

Product formed ÷ time & reactant formed ÷ time

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15
Q

Define what Vmax is, and how it’s reached

A

The maximum rate of an enzyme-controlled reaction. It is reached when all the enzyme’s active sites are full.

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16
Q

Explain why enzyme-controlled reactions have a high initial rate

A

Because the most ESC are formed at the beginning of a reaction

17
Q

Describe how to calculate the rate of reaction at a specific point on a graph, if the line is a curve

A

Calculate the tangent of the curve

18
Q

Explain why increasing temperature increases the rate of enzyme-controlled reactions

A

It increases the KE of the particles, which increases the frequency of collisions

19
Q

Explain how changing temperature may affect the rate of an enzyme controlled reaction

A

As temperature increases, rate increases

20
Q

Explain why changing temperature above the optimum may reduce the rate of reaction

A

Because the enzymes may denature

21
Q

Recall the equation to calculate pH

A

pH = -log10 [H+]

22
Q

Explain how changing pH may reduce the number of ESCs formed

A

As pH changes, more H+ causes the charges on the R groups of the amino acids in the active site to change, and the substrate will not be able to bind as easily. Less ESCs formed.

23
Q

Explain why changing pH causes the shape of an enzyme’s active site to change

A

The change in [H+] causes theionic and hydrogen bonds to break, which changes tertiary structure of active site. No ESCs can be formed.

24
Q

Explain why changing substrate concentration changes the rate of an enzyme-controlled reaction

A

It would change the frequency of collisions, changing the rate of ESCs formed

25
Explain why changing enzyme concentration changes the rate of an enzyme-controlled reaction
It would change the frequency of collisions, changing the rate of ESCs formed
26
Explain why and when the effect of changing enzyme and substrate concentration will no longer be seen
When Vmax is reached, when the reaction finishes, and when the enzyme becomes denatured
27
What is the purpose of inhibitors in your body?
To control the rate of metabolic reactions
28
Describe how competitive inhibitors work
The inhibtor has a similar shape to the substrate, and binds competitively to the active site, preventing ESCs forming
29
Describe the shape of competitive inhibitors
The same as the substrate / complimentary to the active site
30
Explain how Vmax can still be reached when a competitive inhibitor is used
By increasing substrate concentration, because this increases the probability of enzyme-substrate collisions
31
Describe how non-competitive inhibition works
The bind to an allosteric site on the enzyme, changing the shape of the active site
32
Explain why Vmax cannot be reached when a non-competitive inhibitor is used
Because they bind permanently to enzymes, so they are no longer available
33
Describe how a molecule binding to an enzyme may act as an activator
It may bind to an allosteric site on the enzyme, changing the 3D shape of the active site to make it complimentary to the substrate