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Biology > Module 2.1.4 Enzymes Sambrook > Flashcards

Module 2.1.4 Enzymes Sambrook Flashcards

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1
Q

What is the turnover number ?

A

The number of reactions per enzyme per second

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2
Q

What are enzymes

A

-biological catalysts
- speed up metabolic reactions
- they remain unchanged

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3
Q

What are chemical catalysts?

A

-extreme in the following:
High Temp
High pressure
Ph

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4
Q

What are biological catalysts?

A

-low temp
-normal pressure
-neutral ph
-specific
-catalyse in both directions

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5
Q

What are enzymes made of?

A

-proteins (amino acids)

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6
Q

What does a gene mutation do to amino acid sequence of enzymes?

A

-no change as it’s degenerative
Or
-keep the protein the sme but change the structure
Or
-change the sequence enough so a totally different protein is made

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7
Q

What is the primary structure of enzymes?

A

The amino acid sequence

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8
Q

What is the secondary structure of enzymes?

A

Spiralling of the polypeptide

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9
Q

What is the tertiary structure of enzymes?

A

Folding of the polypeptide including the bonds between them giving the protein it’s specific shape-> including the active site

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10
Q

What is the quaternary structure of enzymes?

A

Multiple polypeptide chains jones together

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11
Q

Examples of metabolic disorders

A

-Tay sachs disease
-maple syrup urine disease
- phenylketonuria

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12
Q

Examples of structural disorders

A

-elhers danlos syndrome
-stone man syndrome

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13
Q

What are the 2 parts of the ACTIVE site?

A

-binding site
-catalytic site

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14
Q

What does the binding site do?

A

Bind and orient the substrate

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15
Q

What does the catalytic site do?

A

Puts pressure on the bonds-> reduces repulsion’s -> lowers the activation energy

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16
Q

How do enzymes lower the activation energy?

A

-put pressure on the bonds in the substrate when they bind to the active site
-this reduces the repulsion between the 2 substrate molecules holding them together allowing them to make a larger molecule

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17
Q

Explain the induced fit model

A
  • substrate binds to the active site
    -active site has a CONFORMATIONAL change
    -if another substrate were to enter the active site it would not bind in the correct places so would not cause this change
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18
Q

What are intracellular enzymes?

A

Enzymes that act within the cell

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19
Q

Catabolic definition

A

Metabolic pathways that BREAKDOWN molecules

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20
Q

Anabolic definition

A

Metabolism pathways that SYNTHESISE larger molecules

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21
Q

What are intermediate substrates ?

A

Products of enzyme reactions that become substrates in another reaction

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22
Q

What is catalase?

A

-an enzyme found in living organisms that is exposed to oxygen
-hydrogen is produced but must be broken down

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23
Q

What are extra cellular enzymes?

A

Enzymes that act outside the cell

24
Q

Explain enzyme action

A

-Mucor release hydrolytic enzymes from their hyphae that digest carbs, lipids and proteins
- the products are then reabsorbed into the hyphae

25
Q

What does catalase do?

A

Breaks down hydrogen peroxide to oxygen and water

26
Q

What’s a prosthetic group ?

A

-A non protein group that is part of a protein

27
Q

What is a cofactor?

A

A non- protein molecule that has to be present for an enzyme catalysed reaction to happen

28
Q

Why are all prosthetic groups cofactors but not all cofactors are prosthetic groups ?

A

All prosthetic groups are permanently bound to the enzyme

29
Q

Name for a red blood cell ?

A

Erythrocyte

30
Q

What is carbonic anhydrase ?

A

Used in erythrocytes to catalyse the conversion of carbon dioxide and water to carbonic acid

31
Q

What do temporary cofactors do?

A

-Some bind to the substrate to give it a complementary shape to the active site

-some change the charges on the molecules which make it easier for bonds to form

32
Q

What is a coenzyme?

A

Helps an enzyme carry out its function but is not used in the reaction itself

33
Q

What happens to an enzyme above optimum temperature?

A

1)increased vibration breaks weak bonds
2)tertiary structure of the enzymes is changed
3)active site becomes denatured
4) substrate will no longer be able to bind to enzyme

34
Q

How are optimum temperature and bonding related?

A

-the stronger the hydrogen and ion or bonds in the protein the higher the optimum temperature

35
Q

What is psychrophilic bacteria

A

-cold loving bacteria

36
Q

What is hyperthermophilic bacteria

A

Heat loving bacteria

37
Q

Substrate rate of reaction calculation

A

1
——————————————-
Time taken to reach end point

38
Q

Temperature coefficient calculation
Q10

A

R2 rate of reaction at (T+10C)
———————————————
R1 Rate of reaction at TC

39
Q

What are inactive precursors?

A

-enzymes that are only activated when they’re needed

40
Q

What do inactive precursors do?

A

Stops reactions from happening when they are not needed or would be harmful.

41
Q

What do inhibitors do ?

A

Reduce the activity of enzymes

42
Q

How do inhibitors work?

A

-bind to the enzyme and effect the way the substrate can bind to the active site

-by blocking the active site or causing a conformational change

43
Q

Effect of ph on enzymes

A

-hydrogen and ionic bonds hold the tertiary structure of the protein
-an excess of H+ or OH- ions can cause these bonds to break
-this alters the active site and denatures the enzyme

44
Q

Affect of substrate concentration on enzyme activity

A

-the greater the substrate concentration the higher the rate of reaction
-as the substrate molecules increases the likelihood of enzyme substrate complex formation increases.
-if enzyme concentration remains fixed but the amount of substrates increases all available active sites will become saturated
-any further increase in substrate concentration will not increase reaction rate

45
Q

Effect of enzyme concentration on enzyme activity

A

-the higher the enzyme concentration, the greater the number of active sits available
-greater the likelihood of enzyme substrate complex formation.
-as long as their is a sufficient substrate available the initial reaction increases linearly
-if substrate is limited increase in enzyme concentration will not increase the reaction and substrate becomes a limiting factor

46
Q

What is a competitive inhibitor

A

They only join to the active site
-either some of it or all of it

47
Q

What does a competitive inhibitor do?

A

-stops the substrate from bonding to the active site
-can be reversible or irreversible
-when the inhibitor leaves the substrate can bind again

48
Q

What is a non-competitive inhibitor?

A

-bind to anywhere on the enzyme other than the active site

49
Q

What does an non competitive inhibitor do ?

A

-cause conformational change of the active site
-stops the substrate form being able to bind
-irreversible or reversible

50
Q

What is a reversible inhibitor called ?

A

-inhibitor

51
Q

What is a irreversible inhibitor Called ?

A

-Inactivator

52
Q

How do competitive inhibitors affect rate of reaction ?

A

-if substrate concentration is increased the change of the substrate binding to the actuve sitr
-ROR increases as substrate concentration increases
-both reach same plateau just takes longer with inhibitor

53
Q

What is negative feedback ?

A

-mechanism in which a negative effect of homeostasis is reuturned to normal
-some controlled by end-product inhibition

54
Q

What is an end product inhibitor?

A

When the end product of a metabolic pathway becomes the inhibitor of the first part of that pathway

55
Q

What does an end product inhibitor do m?

A

Stops the pathways from happening all the time and producing too much intermediate or end product

56
Q

Examples of inhibitors

A

-ATPaze
-ACE
-Protease
-nucleoside reverse transcriptase inhibitor

Biology (8 decks)

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