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bio > c1.1- enzymes and metabolism > Flashcards

c1.1- enzymes and metabolism Flashcards

1
Q

metabolic reactions

A

chemical reactions that keep living organisms alive

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2
Q

anabolic reactions

A

reactions that build things up

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3
Q

anabolic reaction eg [2]

A
  1. condensation
  2. combining monomers into polymers
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4
Q

catabolic reactions

A

reactions that break things down

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5
Q

catabolic reactions eg [2]

A
  1. hydrolysis
  2. digesting polymers into monomers
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6
Q

fibrous protein interaction w water

A

insoluble in water

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7
Q

function of fibrous proteins

A

structural: support and strength
- extra cellular matrix inside: collagen (strengthening tissues)

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8
Q

fibrous proteins eg [2]

A
  1. keratin
  2. elastin
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9
Q

globular proteins interaction w water

A

soluble in water (mostly)

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10
Q

globular proteins function

A

functional (enzymes, antibodies, transport)

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11
Q

globular proteins eg [5]

A
  1. amylase
  2. insulin
  3. haemoglobin 4.immunoglobulins
  4. Na+/K+ pump
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12
Q

proteome

A

complete set of proteins expressed by an organism

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13
Q

genome

A

entire set of dna instructions found in a cell

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14
Q

substrate

A

reactant in a biochemical reaction that binds to the enzyme’s active site

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15
Q

enzyme

A

globular protein which acts as a biological catalyst that speeds up metabolic reaction by lowering the activation energy

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16
Q

catalyst

A

speeds up chemical reactions and will not be used up

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17
Q

active site

A

region on the surface of an enzyme which substrates bind and catalyses the reaction

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18
Q

active site function + why

A
  • attract substrate because polar/non polar region
  • depends on composition of r group
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19
Q

shape of active site and substrate

A

complementary + specific

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20
Q

when substrate is locked into the active site

A

reaction is catalysed then products are released and enzyme is used again

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21
Q

induced fit model

A
  • substrate inducing a conformational change in the active site
  • after: enzyme reverts to original shape
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22
Q

induced fit model pros

A

stressed the substrate (weaken the bonds) so reduces the activation energy of the reaction

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23
Q

how to increase the amount of enzyme-substrate complex [4]

A
  1. increase temp
  2. increase kinetic energy
  3. increase conc of substrate
  4. increase conc of enzyme
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24
Q

result of factors being increased [2]

A
  1. increased chance of successful collision
  2. increased rate of reaction
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25
Q

activation energy

A

amount of energy that must be put into a reaction to make it occur

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26
Q

lactose intolerance occurs because

A

ppl unable to produce the enzyme- lactase in insufficient quantities

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27
Q

composition of lactose + effect

A

dimer
- 2 sugars (galatose and glucose)
- slow when u try to absorb it

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28
Q

how does increased lactose in the intestines lead to diarrhea

A
  1. increased lactose in the intestines
  2. can not be digested due to the lack of lactase
  3. bacteria can use the lactose to reproduce
  4. the increase in bacteria population causes water potential in the intestine to drop
  5. blood has a higher water potential
  6. water diffuses from blood into small intestine using osmosis
  7. diarrhea occurs
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29
Q

solutions for lactose intolerance

A
  1. take a lactase supplement
  2. drink lactose-free milk
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30
Q

how to produce lactose-free milk

A

immobilise lactase with alginate beads

31
Q

y body temperature at 37 when optimum is 40?

A
  • bacteria assume optimum is 37
  • when they evolve: bacteria enzyme optimum is also 37
  • need u to survive and do things for them
  • when we are invaded: can increase temp then the bacteria enzymes denature but our enzymes work better
32
Q

optimum pH

A

enzymes only operate within a narrow range of pH

33
Q

deviation form the optimum pH

A
  • hydrogen bonds between amino acids in the structure of the enzyme are broken
  • loss of shape
34
Q

temp graph

A

notes
- asymmetrical

35
Q

pH graph

A

notes
- symmetrical

36
Q

conc graph

A

notes
- reaches a plateau

37
Q

metabolic pathways

A

chains or cycles of enzyme-catalysed reactions

38
Q

competitive enzyme inhibition

A

competitive inhibitor binds with active site so the substrate is blocked and cannot bind on the active site

39
Q

competitive enzyme inhibition eg

A

statins
name of enzyme blocked: HMG-CoA reductase
why
- less cholesterol produced in the body

40
Q

non-competitive enzyme inhibition

A

binding to allosteric site causing a conformational change in the active site so the substrate wont fit

41
Q

competitive enzyme inhibition graph

A

3 lines
notes

42
Q

competitive enzyme inhibition graph explanation

A
  • the higher the concentration of inhibitor, the slower the rate of reaction
  • if increase concentration of substrate then can counter concentration of inhibitor
  • even with competitive inhibition, the same maximum rate of reaction will be achieved if more substrate is added
  • did not change the number of enzymes available
43
Q

non competitive inhibition graph

A

3 lines
notes

44
Q

non competitive inhibition graph explanation

A
  • as the concentration of inhibitor increases, the rate of reaction decreases
  • fewer functional active sites available for reaction - maximum rate of reaction is also reduced- with fewer functional active sites
  • enzyme has reduced ability to process the substrates, even if the substrate concentration is increased
45
Q

irreversible binding of inhibitor causing

A

changes to the active site via covalent bonds

46
Q

irreversible binding of inhibitor + competitive inhibition eg: detailed

A

penicillin (antibiotic)
- inhibits transpeptidases → forms permanent covalent bond with a particular amino acid in the active site → enzyme breaks cross links in the bacterial cell

47
Q

enzyme catalysed reactions intracellular or extracellular

A

can be both

48
Q

glycolysis

A

linear metabolic reaction

49
Q

kreb + calvin cycle

A

enzyme catalysed, cyclical metabolic pathways

50
Q

feedback inhibition eg

A

first enzyme- threonine deaminase
first substrate- threonine
end product- isoleucine

51
Q

product

A

substances after the catalysed reaction

52
Q

collision

A

substrates and the active sites of enzymes will randomly hit each other

53
Q

why the presence of water is critical for most enzyme reactions

A

diffusion to allow movement (brownian motion)

54
Q

y enzymes tend to move slower than substrates

A

usually larger than substrates → more kinetic energy required to move

55
Q

enzymes involved in anabolism

A

synthase

56
Q

enzymes involved in catabolism

A

hydrolase

57
Q

advantages of immobilising enzymes

A

can be reused easily- easily separated from the product

58
Q

3 ways enzymes are immobilised

A
  1. alginate gel
  2. glass
  3. bonding with other enzymes to make bigger aggregates
59
Q

y lactose free milk is produced [3]

A
  1. galactose and glucose sweeter than lactose
  2. lactose tend to crystallise when milk is used to make into ice cream
  3. lactose is slower for bacteria to use for fermentation to make yogurt and cheese
60
Q

process that lactose-free milk produced by immobilised enzymes

A
  • lactase immobilise in alginate beads
  • milk cycled through the alginate beads, lactase breaks down lactose into glucose and galactose in the milk
61
Q

activation energy

A

minimum energy that substrates need to overcome in order for a reaction to occur

62
Q

how do enzymes lower the activation energy of a reaction

A
  • when substrate binds to the active site, substrate is altered to reach transition state
  • can be converted into products and be separate from enzyme’s active site
  • this binding lowers the activation energy
63
Q

inhibitor

A

substance that binds to an enzyme and reduce the enzyme’s activity

64
Q

what is necessary for substrate molecule and active site to come tgt

A

molecular motion

65
Q

how does size of substrate affect its movement

A

large- limits movement during interactions with enzymes

66
Q

what can gene mutations causing active site conformational change in transpeptidase lead to

A

bacterial resistance in penicillin

67
Q

characteristic of active site + substrate’s effect

A
  • not rigid
  • substrate can induce slight changes in the shape of active site
68
Q

how can end product inhibition be regulated

A

metabolic pathway regulated according to the requirement for its end product

69
Q

end product + non-competitive inhibition eg

A

1st enzyme- threonine deaminase
1st substrate- threonine
end product- isoleucine

70
Q

penicillin types of inhibition

A

irreversible
competitive
end product

71
Q

what does penicillin bind to

A

DD transpeptidase

72
Q

how does penicillin work [4]

A
  1. forms permanent covalent with certain amino acids in the active site
  2. enzymes break cross links in the bacterial cell
  3. cell wall is weakened
  4. bacteria killed by lysis
73
Q
A

bio (23 decks)

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