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AS Biology > Enzymes > Flashcards

Enzymes Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

Where is amylase found?

A

Salivary gland

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2
Q

What is the role of amylase?

A

To convert starch into maltose

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3
Q

Where is protease found?

A

Stomach and small intestine

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4
Q

What is the role of protease?

A

Convert proteins into amino acids

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5
Q

Where is lipase found?

A

Pancreas and small intestine

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6
Q

What is the role of lipase?

A

To breakdown lipids into fatty acids and glycerol

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7
Q

State 3 features of an enzymes structure.

A

Globular, proteins with tertiary structure, active site

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8
Q

What part of an enzyme gives it many of its properties?

A

Active site

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9
Q

Why does the active site have a unique shape?

A

So that rhI enzyme can only catalyse one type of reaction

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10
Q

What is an anabolic reaction?

A

One which joins two different substrates together to form a new molecule

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11
Q

What is a catabolic reaction?

A

One substrate can be separated to form two new molecules

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12
Q

What is the lock and key model?

A

The shapes of the active site and substrate are specific to each other

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13
Q

What is the induced fit model?

A

The shape of the active site alters so that the substrate can fit

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14
Q

What is activation energy?

A

The minimum amount of energy needed for a reaction to occur

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15
Q

Initially how does the presence of enzymes affect the rate of reaction?

A

More enzyme = faster rate

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16
Q

What factors affect the rate of an enzyme reaction?

A

Enzyme concentration, substrate concentration, temperate, pH

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17
Q

Why does temperature increase the rate of an enzyme reaction?

A

The increased temp will mean an increased kinetic energy of the enzymes and substrates, as a result there will be a her frequency of collisions between enzyme and substrate, increasing the rate of reaction.

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18
Q

Why does the ROR go down at temperatures of over 40 degrees?

A

Because the enzyme become denatured.

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19
Q

Why do enzymes not work at very low temperatures?

A

Because the enzyme is inactivated as it has low kinetic energy

20
Q

What do extremes of pH do to enzymes?

A

Denature them

21
Q

What does the turn over number of an enzyme show?

A

The number of substrate molecules that one enzyme can turn into products in a given time

22
Q

What is the fasted acting enzyme?

A

Catalase

23
Q

What do enzyme inhibitors do?

A

Slow down or stop enzyme activity

24
Q

What are enzyme inhibitors an essential part of?

A

Cellular control

25
Q

What is cellular control?

A

Switching enzymes on or off

26
Q

What are the four types of inhibitors?

A

Reversible and irreversible, competitive and non-competitive.

27
Q

What does a reversible inhibitor do?

A

Temporarily stop an enzyme working

28
Q

What does an irreversible inhibitor do?

A

Jams the active site or changes it so that it can’t work any longer

29
Q

How does a competitive inhibitor work?

A

Competes with the substrate for the active site. It blocks the active site, preventing the substrate from binding.

30
Q

How would you overcome a competitive inhibitor?

A

By increasing the concentration of substrate as they are displaced from the active site

31
Q

How does a non-competitive inhibitor work?

A

Binds to an enzyme at a point away away from the active site. This changes the shape of the enzyme, preventing the substrate from binding.

32
Q

Does increasing concentration of substrate have an effect on non-competitive inhibitors?

A

No

33
Q

What is end product inhibition?

A

The final product may inhibit an early enzyme, deactivating the pathway so that excess product is not produced. When the product is in short supply again, the inhibition is lifted and the pathway is active again.

34
Q

What is an immobilised enzyme?

A

An enzyme thanks fixed or bound to a particular substance

35
Q

Where are immobilised enzymes frequently used?

A

In industry

36
Q

Give two reasons why immobilised enzymes are frequently used in industry?

A

Because the enzymes are frequently reused, and the products are not contaminated with the enzymes

37
Q

Give three uses of immobilised enzymes in industry.

A

Tenderisation of meat, lactose free milk, biosensors, manufacturing fructose from starch

38
Q

What are the four methods used by immobilised enzymes?

A

Encapsulation, entrapment, covalent binding, adsorption

39
Q

State three advantages of immobilised enzymes.

A

Enzymes can be recovered easily and reused, final product free of enzyme, increased stability and function over a wider range of temperature and pH than enzymes free in solution, different columns can be used for enzymes with differing pH and temperature so more than one enzyme can be used at the same time

40
Q

State three disadvantages of immobilised enzymes.

A

They can get washed out of the reactor, not very good at removing days, purified soluble enzymes have poor stability, if you overheat a system or process then you could lose a whole batch because of denaturation.

41
Q

State four properties of enzymes.

A

Speed up reactions, not used up, not changed, high turn over number.

42
Q

What are the three sites of enzyme action?

A

Extracellular, intracellular in solution, intracellular membrane bound.

43
Q

What is a catalyst?

A

A molecule which speeds up a chemical reaction, but remains unchanged at the end of the reaction.

44
Q

Define metabolic pathway.

A

A sequence of enzyme-controlled reactions in which a product of one reaction is a reactant in the next.

45
Q

What is digestion?

A

The breakdown of large molecules by hydrolysis into small, soluble substances that can be absorbed into the blood.

AS Biology (7 decks)

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