Enzymes Flashcards

1
Q

State the function of an enzyme

A

Biological Catalyst

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2
Q

Give the term for a building up reaction

A

Anabolic

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3
Q

Give the term for breaking down reactions

A

Catatonic

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4
Q

Define metabolism

A

The sum of all different chemical reactions.

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5
Q

Give the three factors that affect enzymes

A

pH
Temperature
Pressure

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6
Q

What is the maximum rate an enzyme can catalyse called?

A

Vmax (maximum initial velocity)

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7
Q

What do enzymes need in order to function?

A

Activation energy

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8
Q

What does a catalyst do?

A

Increase the rate of successful collisions of molecules

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9
Q

Name and describe the two key hypothesis of enzymes

A

Induced fit theory- enzyme slight changes shape to fit with substrate
Locke and key theory- enzyme fits perfectly with substrate

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10
Q

Where does the substrate bind?

A

The active site

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11
Q

What is it called when an enzyme attaches to the substrate?

A

An enzyme-substrate complex

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12
Q

What is an enzyme that acts within a cell called?

A

Intracellular enzyme

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13
Q

Give an example of an intracellular enzyme

A

Catalase- breaks down hydrogen peroxide to water and oxygen

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14
Q

What is an enzyme that are released from cells to act outside a cell called?

A

An extracellular enzyme

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15
Q

What is the purpose of extracellular enzymes?

A

To break down large polymers to make them able to move into the cell.

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16
Q

Describe the digestion of starch

A
  1. Starch polymers are broken down into maltose by amylase.
  2. Maltose is broken down into glucose by maltase, present in the small intestine
17
Q

Describe the digestion of proteins

A

A protease called trypsin digests proteins into smaller polypeptides, and is broken down by other enzymes into amino acids

18
Q

Describe denaturation.

A

The tertiary bonds are affected, changing the shape of the enzyme and meaning it can no longer fit to it’s substrate, slowing the rate of catalysation.

19
Q

How can substrate and enzyme concentration effect the rate of reaction?

A

Affceted by Vmax

20
Q

Define an inhibitor

A

Molecules that prevent an enzyme from carrying out their normal function

21
Q

Name the two types of inhibition

A

Competitive and non competitive inhibition

22
Q

Describe the process of competitive inhibitors

A

The inhibitor binds to the active site and block the substrate, decreasing enzyme availability and the rate of reaction

23
Q

Describe the process of non competitive inhibitors

A

The inhibitor bind to the allosteric site, changing the tertiary structure of the protein and preventing the substrate from being able to bind to the active site, decreasing enzyme availability and the rate of reaction

24
Q

Give an example of competitive inhibition

A

Statins- drugs that inhibit an enzyme aiding in the synthesis of cholesterol

25
Q

Name the site that a substrate does not bind to.

A

Allosteric site

26
Q

What is end-
product inhibition?

A

When the product of a reaction acts as the inhibitor to the enzyme producing it.

27
Q

What is the difference between a cofactor and a coenzyme?

A

A coenzyme is organic, a cofactor is not.

28
Q

What is the purpose of a cofactor?

A

A non-protein component that helps the enzyme carry out it’s function.

29
Q

Give an example of a cofactor

A

Amylase uses a chloride ion in the breakdown of starch

30
Q

Give an example of a coenzyme

A

NADP uses vitamin B3

31
Q

Describe precursor action.

A

Many enzymes are produced in an inactive form, and undergo a tertiary change to be actiavted. A precursor enzyme is called an apoenzyme.