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Biology mine > Enzymes > Flashcards

Enzymes Flashcards

1
Q

What is an anabolic reaction

A

Chemical reactions required for growth

Building up

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2
Q

What is a catabolic reaction

A

Breaking down

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3
Q

Enzymes can only increase the rate of reaction up to a certain point, what is this called?

A

Vmax

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4
Q

What energy is needed to be supplied for start of most reactions

A

Activation energy

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5
Q

How do enzymes help molecules

A

Help them collide more successfully so reduce activation energy needed

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6
Q

Deacribe the lock and key hypothesis

A

Area within tertiary structure of enzyme that has a a shape that is complimentary to a specific substrate molecule
‘Lock and key’
When substrate is bound to active site an enzyme substrate complex is formed. Substrate reacts and forms a enzyme-product complex.
Product is then released,leaving enzyme unchanged

Substrate held in a way atom groups interact
R group on active site interact with substrate too

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7
Q

Describe the induced fit model

A

Active site of an enzyme changes shape as substrate enters. Initial reaction between enzyme and substrate is weak, so change enzyme tertiary structure that strengthen binding on substrate molecule
Weakens a particular Bon in substrate so lower activation energy needed

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8
Q

What do all reaction in cells need

A

Substrates

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9
Q

Raw materials need to be supplied to cells, what can supply these materials

A

In our diet
Proteins
Polysaccharides
Enzymes break down large nutrient molecules into smaller ones

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10
Q

What are extra ellipse enzymes

A

Break down large nutrient molecules into smaller ones by digestion

They work outside of the cell that made them

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11
Q

What relies on extra cellular enzymes to make use of polymers for nutrition

A

Single and multicellular organisms

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12
Q

Describe digestion of starch

A

Begins in mouth to small intestines
Starch polymers are broken down partially into maltose by analyse (produce by pancreatic juice/saliva InMouth)

Maltose is then broken into glucose
Enzyme maltase used.
Glucose absorbed by cell lining to digestive system and absorbed into blood stream

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13
Q

Describe digestion of proteins

A

Trypsin is a protease that catalyses digestion of protein into smaller peptides, which are then broken down into amino acids
Trypsin is produced in prancreas in small intestines where acts as proteins

Amino acids made are absorbed by blood stream of cell lining of digest for system

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14
Q

How does temperature affect enzymes

A

Increase kinetic energy as particles move faster

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15
Q

What is temperature coefficient

A

Measure of how much the rate of reaction increases with a 10c rise in temp.

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16
Q

What happens if temperate is too hot in enzyme

A

Bonds become strained and break, changing tertiary structure
Denature for enzyme

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17
Q

What is an optimum temperature of an enzyme?

A

Enzymes highest activity rate

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18
Q

How are enzymes in the metabolic activities, for example, adapted to the cold?

A

More flexible Structures e.g. At active site- makes less stable than enzymes at higher temperatures

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19
Q

How do organisms that are adapted to the cold, denature?

A

When there are small subtle temperature changes

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20
Q

What’s a thermophile

A

Organism that’s adapted to live in high temperatures like hot springs

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21
Q

How do thermophile a survive in high temperatures

A

More bonds so more stable

E.g more h and sulfar bonds in tertiary structure

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22
Q

What does a change in pH often refer to in enzymes

A

Change in hydrogen ion concentration

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23
Q

What is the difference between low and high pH referring to hydrogen ions

A

Low PH- more hydrogen ions present

High pH- fewer hydrogen ions

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24
Q

What is the optimum pH

A

Had the right shape for active site at a specific hydrogen ion concentration

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25
Q

What is renaturation

A

When the next me becomes too acidic or alkalin, altering the structure
But then returns back to the optimum pH and the protein carries on normal shape and catalysing reactions

26
Q

What happens when the pH changes more significantly?

A

Structure of enzyme irreversible
Substrate can’t join active site
Therefore denatured
Reduces rate of reaction

27
Q

What do hydrogen ions react with (pH)

A

Polar and charged r groups

28
Q

When hydrogens interact with polar and charged R groups, what do they change?

A

The concentration of hydrogen ions, changing the degree of reaction

29
Q

The more hydrogen ions present, this means less….interact with eachother

A

R groups

30
Q

From the result of more hydrogen bonds therefore less R groups interacting with eachother, what does this lead too?

A

Leads to bonds breaking and shape of enzymes changing

31
Q

From the shape changing due to lots of hydrogen ions, when is it more like to be reversible

A

When there is fewer hydrogen ions present (high pH)

32
Q

Site of action for saliva

PH?

A

Mouth

7- neutral

33
Q

What enzyme is in salvia and salvias function

A

Amylase

Starch I maltose

34
Q

Where’s the site of action or gastric juice

pH level?

A

Stomach

1-2 acidic

35
Q

Enzyme in gastric juice

Function of gastric juice

A

Pepsin

Proteins to polypeptides

36
Q

Where’s the site of action for pancreatic juice

pH level

A

Small intestine

8 slightly alkaline

37
Q

What enzyme is involved in pancreatic juice

What’s its function

A

Trypsin -proteins to polypeptides

Maltase- maltose to glucose

38
Q

What happens when the concentration of a substrate is increased?

A

Number of molecules in particular area increases, therefore more number of substrate particles leading to higher collision rate with active site to form a enzyme-substrate complex.

39
Q

What happens when the enzyme concentration is increased?

A

More available active sites in an area, leading faster reactions of enzyme-substrate complexes

40
Q

Where does the rate of reaction increase up to

A

The max known as V max

41
Q

What is v max

A

Where all active sites are occupied by a substrate molecule and no more can be made.

42
Q

What is a way you could increase reaction when it has reached V max

A

Add more enzymes or increase temp
If
Concentration of enzymes increased =more active sites, reaching a higher V max

43
Q

By controlling the activity of enzymes at crucial points in the reaction pathway allows it too…

A

Regulates the rate and quantity of product formation.

44
Q

What can activate enzymes

What can deactivate them

A

Cofactors

Inhibitors

45
Q

What are inhibitors

A

Molecules that prevent enzymes from carrying out function as catalysts

46
Q

What are the two types of inhibitors

A

Competitive

Non competitive

47
Q

How does a competitive inhibitor work

A

A molecule that has a similar shape to active site so blocks the substrate from entering it.
Enzyme is now inhibited as can’t carry out catalyst functions

48
Q

What happens when a substrate and a competitive inhibitor is involved in a solution

A

Both compete to bind to active site of enzyme, therefore reducing the amount of substrate molecules binding to active site; slowing rate of reaction.

49
Q

Describe competitive inhibitors

A

Compete for active site

Only temporary so reversible

50
Q

Example of a competitive Inhibitor that ISNT reverisble

A

Aspirin

51
Q

How does a competitive inhibitor affect the rate of reaction?

A

Reduces rate of reaction.
But doesn’t change v max of enzyme it inhibits
If substrate concentration is increased enough there will be more substrate than inhibitor so original v max can still be reached

52
Q

Examples of competitive inhibitors

A

Statins

Aspirin

53
Q

What are statins

A

Synthesise cholesterol

Prescribed to reduce blood cholesterol concentration

54
Q

Describe aspirin

A

Inhibits active site of COX enzyme

Prevents synthesis of prostaglandins and thromboxane- chemical that reduces pain and fever

55
Q

How do non competitive inhibitors work

A

Binds to active site at anywhere but active site. (Allosteric site)
The binding causes tertiary structure of enzyme to change, altering shape

Substrate can’t bind anymore

56
Q

Affect of increasing concentration of enzyme or substrate to overcome non competitive inhibitors

A

No effect of

Over coming inhibitor

57
Q

What happens if you increase amount of non competitive inhibitors

A

Decreases rate of reaction as more active sites aren’t available

58
Q

Example of non competitive inhibitors

A

Organophosphates- insecticides- inhibits enzyme for nerve transmission

Proton pump inhibitors
Used to treat long term indigestion
Block enzyme system that secretes hydrogen ions in stomach.

59
Q

What does end product inhibition mean

A

Term used for enzyme inhibition Occurs when product of a reaction acts as an inhibitor to the enzyme that produce it. - serves as negative feed back control mechanism

60
Q

knk

A

m n

Biology mine (6 decks)

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