cc4 - enzymes Flashcards

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1
Q

metabolism

A

sum of all the enzyme controlled chemical reactions taking place in a cell

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2
Q

2 main types of reactions that make up metabolism

A

anabolic
catabolic

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3
Q

anabolism

A

set of metabolic pathways that synthesise complex molecules from smaller, simpler ,molecules

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4
Q

catabolism

A

set of metabolic pathways that breakdown complex molecules into smaller, simple molecule

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5
Q

enzyme

A

biological catalyst used to speed up rate of intracellular + extracellular biochemical reactions
not used up or permanently altered

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6
Q

intracellular enzyme

A

enzyme that acts within cells
e.g: catalase

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7
Q

extracellular enzyme

A

enzyme secreted by cells + functions outside of cells
e.g: amylase

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8
Q

active site of enzyme

A

region of enzyme that is complementary to shape of a specific substrate
substrate binds + reaction takes place

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9
Q

why is active site described as specific

A

3D structure of each enzyme (including active site) is unique due to presence of different side chains + branches
only specific substrates complementary to active site can bind

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10
Q

activation energy

A

minimum amount of energy required for a reaction to take place

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11
Q

catalysis

A

increase in rate of chemical reaction using a catalyst (such as an enzyme)
catalyst lowers activation energy of reaction

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12
Q

lock and key model

A
  1. substrate + active site of enzyme come into contact
  2. substrate binds, enzyme-substrate complex forms
  3. reaction takes place, products formed in enzyme-product complex
  4. products released from active site
    active site now free to bind to another substrate
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13
Q

induced fit hypothesis

A

model of enzyme action stating that once a specific substrate binds to active site, enzyme undergoes subtle conformational changes
puts strain on substrate, lowering activation energy for reaction

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14
Q

factors affecting rate of enzyme-controlled reaction

A

temperature
pH
substrate concentration
enzyme concentration

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15
Q

how temperature affects rate of enzyme-controlled reactions

A

as temp increases, molecules have more kinetic energy
molecules moved faster + collide more frequently
more ES complexes form
tate of reaction increases
rate peaks at optimum temperature

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16
Q

how increasing temp above optimum affects rate of enzyme-controlled reaction

A

increased vibration break H + ionic bonds in tertiary structure
active site changes shape, enzyme is denatured
no more ES complexes form
rate of reaction decreases

17
Q

how pH affects rate of enzyme-controlled reactions

A

enzymes have optimum pH
pH shifts from optimum
H + ionic bonds in tertiary structure are altered
interaction of polar + charged R groups changes
active site changes shape, enzyme is denatured
rate of reaction decreases

18
Q

buffer

A

molecules maintaining constant pH in a solution when small volumes of acid (H+) or base (OH-) are added

19
Q

how substrate concentration affects rate of enzyme-controlled reaction

A

if enzyme concentration is fixed, rate of reaction increases proportionally to substrate concentration
once all active sites are full, rate of reaction remains constant (graph plateaus)
enzyme concentration is limiting factor

20
Q

how enzyme concentration affects rate of enzyme-controlled reaction

A

if substrate concentration is fixed, rate of reaction increases proportionally to enzyme concentration
when all substrates occupy active sites, rate of reaction plateaus (substrate concentration is limiting factor)

21
Q

competitive inhibitor

A

molecule which competed for active site of enzyme, blocking it + preventing substrate from binding

22
Q

is competitive inhibition temp or permanent

A

generally temp
some cases (e.g: aspirin) may be permanent

23
Q

how increasing substrate concentration affects competitive inhibition

A

increase in substrate concentration
more substrate than inhibitor
rate of reaction increases

24
Q

non-competitive inhibitor

A

inhibitor binds to different part of enzyme (allosteric site)
tertiary structure of enzyme (including active site) changes shape
active site no longer complementary to substrate
substrate can’t bind + enzyme is inhibited

25
Q

is non-competitive inhibition temp or permanent

A

permanent

26
Q

how increasing substrate concentration affects non-competitive inhibition

A

won’t overcome effect of non-competitive inhibitor

27
Q

immobilised enzymes

A

enzymes attached to inert, insoluble material over which substrate passes + reaction takes place

28
Q

example of application of immobilised enzyme

A

biosensors

29
Q

why immobilised enzymes important in industrial processes

A

enable enzymes to be reused
improves enzyme stability in variable/extreme temps + pHs
increases efficiency of reactions