1.4 enzymes and biological reactions Flashcards

1
Q

what does metabolism mean?

A

all reactions of the body. they occur in sequences called metabolic pathways, which are controlled by enzymes.

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2
Q

what does anabolic mean?

A

building up molecules, e.g. protein synthesis.

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3
Q

what does catabolic mean?

A

breaking down molecules, e.g. digestion.

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4
Q

what protein structure is an enzyme?

A

tertiary; 3D globular shape.

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5
Q

what does intracellularly mean?

A

can act inside the cell.

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6
Q

what does extracellularly mean?

A

can be secreted by cells.

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7
Q

how do enzymes work?

A

the enzyme and substrate collide by binding successfully to form an enzyme-substrate complex.

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8
Q

what is important about the active site?

A

they have specifically shaped active sites that are complementary to the shape of the substrate.

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9
Q

what is activation energy?

A

the minimum energy required for a reaction to take place.

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10
Q

what is the lock and key theory?

A

the active site is a fixed shape - the substrate must collide in the right way in order for them to come together. they fit together like a lock and key.

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11
Q

what is the induced fit hypothesis? an example?

A

as the substrate comes into the active site, it changes its shape around the substrate, forming stronger bonds. it has been shown to occur with lysozyme.

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12
Q

what is an enzyme?

A

a biological catalyst that speeds up the rate of reaction by lowering activation energy. it stays unchanged and does not get used up in the reaction.

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13
Q

how does temperature affect enzyme activity?

A
  • as temperature increases, particles gain kinetic energy.
  • as kinetic energy is increased, there is a higher chance of the substrate colliding with the active site.
  • enzymes are inactive in lower temperatures.
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14
Q

what is the temperature in humans at which enzymes denature and what does this mean?

A

enzymes denature at 40°C. bonds begin to vibrate and break - weak hydrogen bonds break first.

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15
Q

how does pH affect enzyme activity?

A
  • amino acids contain basic + acidic groups. changes in pH can change the bonding between amino acids + therefore changes secondary + tertiary structure of the proteins.
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16
Q

what does a small change in pH mean?

A

small changes in pH are reversible in enzyme structure, so activity is reduced (inactivated).

17
Q

what does a large change in pH mean?

A

large changes in pH cause permanent damage to enzyme structure, which denatures them.

18
Q

how does substrate concentration affect enzyme activity?

A

if the amount of enzyme is constant, the rate of reaction will increase as the substrate increases.

19
Q

what happens at low substrate concentration?

A

all the enzyme’s active sites will become filled and work to full capacity and therefore stops the reaction.

20
Q

how does enzyme concentration affect enzyme activity?

A

as the enzyme concentration increases, there are more active sites available and therefore rate of reaction increases.

21
Q

what is a competitive inhibitor?

A

a substance that has a close structural resemblance to a substrate molecule and can bind temporarily to the active site instead of the normal substrate. this is reversible.

22
Q

how do competitive inhibitors work?

A

it blocks the active site so the substrate cannot bind to it.

23
Q

how are competitive inhibitors overcome?

A

adding more substrate outcompetes the competitive inhibitor.

24
Q

what is a non-competitive inhibitor?

A

a substance that has no structural resemblance to a substrate but binds to the enzyme at a point other than the active site - the allosteric site. some are reversible, some are not.

25
what does a non-competitive inhibitor do?
it changed the shape of the active site, so fewer enzyme-substrate complexes can be made.
26
how do non-competitive inhibitors affect enzyme activity?
it is not affected by increased substrate concentration as the active site is now a different shape.
27
what is an immobilised enzyme?
an enzyme fixed on an inert matrix.
28
what are 2 examples of an inert matrix?
- sodium alginate beads. - cellulose microfibrils.
29
how do immobilised enzymes work?
the substrate is added to the top of a glass column and flows down. they bind to the active site; both on and in the beads as substrate diffuses in.
30
what are 5 advantages of immobilised enzymes?
- reduces cost as column can be used repeatedly once set up. - enzyme is fixed and does not contaminate the product. - the products are easy to purify. - lower/higher temperatures can be used and still have higher yields than using the enzyme. - greater control over the reaction - enzymes can easily be added + removed.
31
how is lactose free milk made with immobilised enzymes?
milk is passed down a column containing immobilised lactase. lactose binds to active sites on lactase and is hydrolysed into glucose + galactose.
32
how do biosensors work?
- they have a specific enzyme (glucose oxidase) immobilised in a membrane. - glucose diffuses into the immobilised enzyme layer through a selectively permeable membrane. - a chemical to electrical signal is produced.
33
how is high fructose corn syrup made?
- starch broken down to oligosaccharides at 90°C by a-amylase. - oligosaccharides broken down to glucose at 60°C by glucoamylase. - glucose broken down to fructose by glucose isomerase. -used in diet foods.