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SBI4U- Biochemistry > Enzymes > Flashcards

Enzymes Flashcards

1
Q

What are enzymes?

A

Proteins that act as a catalyst

- have a tertiary structure

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2
Q

Do enzymes participate in chemical reactions?

A

No- they can be used over and over again

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3
Q

What is the hydrolysis enzyme catalyzed reaction

A

2H2O2 -> 2H2O + O2

- catalase over the arrow

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4
Q

Define active site

A

The binding site for substrate

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5
Q

Compare the shape of a substrate and the active site

A

Have similar shape

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6
Q

Define substrate

A

Any molecule that is recognized by an enzyme and binds to it

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7
Q

What is formed when the substrate bonds to the enzyme?

A

Enzyme- substrate complex

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8
Q

What happens to the enzyme in a catalyzed reaction?

A

It does not get used up and can be used for another reaction

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9
Q

What happens to the enzyme active site when binding with substrate?

A

It changes its shape so it is a perfect fit to bind

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10
Q

What is the substrate apart of when bonding to active site?

A

Tertiary structure

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11
Q

Where is the enzyme written in a chemical reaction and why

A

Above the arrow because it doesn’t get used up

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12
Q

Define induced fit model

A

A model of enzyme activity that describes how an enzyme active site changes shape to better accommodate for a substrate
- forms complementary shape

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13
Q

What does it mean if you’re lactose intolerant?

A

You don’t have the enzymes (lactase) required to break down lactose

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14
Q

Define activation energy

A

The energy required to start a chemical reaction. All chemical reactions require a certain amount of activation energy.
- usually heat

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15
Q

How do enzymes affect activation energy and why?

A

Enzymes lower activation energy of chemical reactions, making them occur more readily (faster)

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16
Q

What does the enzyme do when it lowers activation energy?

A

Breaks the barrier so it’s easier for substrate to turn into product

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17
Q

Define a co-factor

A

A non protein atom or molecule that binds to an enzyme and is essential for catalytic activity
- (essential for enzymes to work)

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18
Q

Give examples of co-factors

A

Minerals

Ex. Mg, Fe (iron in hemoglobin), K, Cu, Zn, Na

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19
Q

Define co- enzyme

A

An organic molecule that acts as a co-factor

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20
Q

Give examples of co- enzymes

A

Vitamins (A and B)

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21
Q

What is the difference between vitamins and minerals,

A

Minerals are inorganic, vitamins are organic

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22
Q

Why is the co- enzyme important?

A

Without it the substrate cannot bind

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23
Q

How does enzyme concentration affect enzyme rate?

A

The more enzymes the faster the rate

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24
Q

How does substrate concentration affect enzyme rate?

A

The more substrate the faster the rate

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25
Q

Why does the curve flatten in an enzyme concentration graph?

A

The substrate ran out

- low in concentration

26
Q

Why does the curve flatten in a substrate concentration graph?

A

Rate stops increasing because enzymes ran out

-low in concentration

27
Q

How does pH affect enzyme rate?

A

When a substance moves away from its optimal pH level, the proteins denature and eventually drops to 0

28
Q

How does temperature affect enzyme rate?

A

When you move away from the optimal temperature, the protein either denatures (too hot) or the enzymes move too slow (too cold)

29
Q

Define enzyme inhibitor

A

Foreign agents that affect the enzymes ability to work

ex. venom or poison

30
Q

What do enzyme inhibitors do?

A

They lower the rate at which an enzyme catalyzes a reaction

31
Q

How do enzyme inhibitors lower the rate of a catalyzed reaction?

A

They bind to an enzyme and decrease its activity

32
Q

Where could enzyme inhibitors bind?

A

To the active site or other critical sites located elsewhere in the structure

33
Q

Define competitive inhibitor

A

Competitive inhibitor molecule resembles substrate and competes with the substrate for the active site

34
Q

Define noncompetitive inhibitor

A

Binds at the site other than the active site, causing the enzyme’s shape to change so that substrate cannot bind to active site

35
Q

Is a competitive or non competitive inhibitor more dangerous?

A

The noncompetitive inhibitor is more dangerous because it shuts down the active site so that substrate cannot bind

36
Q

What determines if the substrate or inhibitor gets the spot on the active site?

A

Depends on if there is more substrate or more inhibitor

37
Q

What does cyanide do to the body?

A

Effects the mitochondria which prevents the body from using oxygen

38
Q

What is arsenic?

A

Rat poison

39
Q

What do pesticides do?

A

Chemically inhibit insect’s enzymes

39
Q

What do pesticides do?

A

Chemically inhibit insect’s enzymes

40
Q

What happens if someone has poison?

A

They pump the stomach to get rid of the inhibitor (empty the stomach)

41
Q

Define allosteric

A

Can be controlled

42
Q

Define allosteric regulators

A

Molecules in the body that naturally regulate enzyme activity by binding to an allosteric site on the enzyme

43
Q

Are allosteric regulators foreign?

A

No, they belong in your body

44
Q

What does it mean to naturally regulate an enzyme?

A

Control the enzymes by speeding them up or slowing them down

45
Q

What two things could allosteric regulation do?

A

Inhibit or stimulate enzyme activity

46
Q

Describe how an allosteric regulator may stimulate enzyme activity

A
  1. enzyme binds to allosteric activator
  2. binding activator converts enzyme to high affinity state
  3. in high affinity state, enzyme binds substrate
47
Q

Describe how an allosteric regulator inhibits enzyme activity

A
  1. enzyme binds allosteric inhibitor
  2. binding inhibitor converts enzyme to low affinity state
  3. substrate is released
48
Q

Why would the body want enzymes to work faster?

A

For the bodily functions to work

49
Q

Why would the body want enzymes to slow down?

A

There is too much product

50
Q

Define feedback inhibition

A

When the allosteric inhibitor is the final product in a biochemical pathway, it inhibits the enzyme that catalyzes the FIRST reaction in the pathway

51
Q

What happens if product is scarce?

A

The inhibition is reduced and the rate of the reaction increases

52
Q

Define biochemical pathway

A

A set of interconnected chemical reactions in which the substrate of the first reaction becomes the product. This product now becomes the substrate of the next reaction and so on…

53
Q

Which enzyme is allosteric in the biochemical pathway?

A

The first one

54
Q

What happens when there is a lot of product?

A

Enzyme 1 is inhibited and the pathway stops

55
Q

What happens if there is too little product?

A

The enzyme 1 is not inhibited anymore and the pathway restarts

56
Q

How to determine the number of reactions in a biochemical pathway?

A

The number of arrows

57
Q

What is each reaction in a biochemical pathway controlled by?

A

A different enzyme

58
Q

What is the purpose of a biochemical pathway?

A

To make the final product

59
Q

Where is pepsin used and what is the optimal pH

A

In the stomach, 2

60
Q

Where is trypsin used and what is the optimal pH

A

Intestine, 8

61
Q

Where is amylose used and what is the optimal pH

A

In the mouth, 7

SBI4U- Biochemistry (7 decks)

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