Enzymes Flashcards

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1
Q

What do enzymes do?

A

They are biological catalysts that reduce the activation energy needed to start a reaction

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2
Q

Stages of reactions using enzymes

A

Substrate fits into a specific enzyme’s active site forming an enzyme-substrate complex.
They have complementary shapes.
Once reaction is complete there is a enzyme-product complex
The products are released
Enzyme is unchanged

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3
Q

What is the lock and key hypothesis?

A

Substrate fits into the enzyme. It is precisely the correct shape to fit into the active site

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4
Q

What is the induced fit hypothesis?

A

As the substrate binds to the active site, the active site changes shape slightly to fit the substrate more closely.

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5
Q

What are the 2 categories of enzyme?

A

Intracellular

Extracellular

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6
Q

Describe intracellular enzymes

A

Work inside the cell

For example, the enzymes in lysosomes

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7
Q

Describe extracellular enzymes

A

Work outside the cell
For example, in digestion the enzymes in the stomach (doesn’t happen in the cells)
And
fungal hyphae (fruit becoming furry)

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8
Q

How enzymes break things up

A

Strain the bonds between them

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9
Q

How enzymes help join things together

A

Hold reactants together in correct orientation to help make the bonds.

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10
Q

What are inhibitors?

A

Substances that affect enzymes.

Slow down the rate of enzyme-controlled reactions.

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11
Q

What are competitive inhibitors?

A

They are complementary to the enzymes active site.

Competitive because both the CI and the substrate can fit into the active site (they have SIMILAR shapes)

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12
Q

How do competitive inhibitors work?

A

CI blocks active site so enzyme-substrate complex can’t be formed, reducing the rate of reaction

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13
Q

Can you overcome competitive inhibitors?

A

Yes, by increasing substrate concentration.
Increases the chance of the substrate binding with the active site before the CI.
It is REVERSIBLE

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14
Q

How do non competitive inhibitors work?

A

Bind to Allosteric site, this changed the shape of the enzymes active site so an enzyme substrate complex can’t be formed, reducing the rate of reaction.
Substrate and NCI have different shapes.

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15
Q

Is it possible to overcome non competitive inhibitors?

A

No, enzyme is permanently changed so substrates, no matter how many there are, can bind to the active site.
It is IRREVERSIBLE.

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16
Q

What is the equation for the temperature coefficient?

A

Rate of reaction at T+10 degrees celsius

Rate of reaction at T degrees celsius`

17
Q

What is the normal temperature coefficient for enzyme reactions?

A

2

18
Q

`What are cofactors?

A

An inorganic ion that increases the activity of an enzyme

19
Q

What is a coenzyme?

A

Organic molecule required for enzyme function

20
Q

What is a prosthetic group?

A

Permanently bound to the enzyme, required for enzyme function.

21
Q

What is product inhibition?

A

When the product made from an enzyme controlled reaction acts as an inhibitor
Can be good - stop too much being made - waste

22
Q

What is the product, substrate and cofactor of amylase?

A

Glucose/maltose
Starch
Calcium ions

23
Q

When enzymes build larger molecules from smaller ones what is it called?

A

An anabolic enzymatic reaction

24
Q

How effective is the Software that predicts the 3D shape of a protein based on it’s amino acid sequence is at discovering the function of the enzyme

A

Tertiary structure determines shape of active site which relates to the function.
Protein folding is highly complex and there can be multiple solutions.
Therefore, function can be narrowed down but not fully predicted.

25
Q

What is a common source of coenzymes for humans?

A

Vitamins

26
Q

Similarity between cofactors and prosthetic groups?

A

Both bind to an enzyme to make formation of the enzyme substrate complex easier

27
Q

Difference between cofactor and prosthetic groups?

A

Prosthetic groups are permanently attached to the enzyme while cofactors can move or attach to the substrate