1.4 - Biological reactions are regulated by enzymes Flashcards

1
Q

What is metabolism?

A

a series of enzyme-controlled reactions in the body

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2
Q

What are the two main types of reaction?

A

Anabolic reaction
Catabolic reaction

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3
Q

What does an anabolic reaction do? What does a catabolic reaction do?

A

Anabolic: protein synthesis where amino acids are built up into more complex polypeptides
Catabolic: digestion of proteins, where complex polypeptides are broken down into simple amino acids

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4
Q

what are enzymes?

A

all enzymes are tertiary globular proteins where the protein chain is folded back on itself into a spherical or globular shape

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5
Q

what can enzymes be described by and what does this mean?

A

can be described as biological catalysts as they speed up the rate of metabolic reaction, but they are not changed by the reaction and do not get used up.

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6
Q

where are all enzymes made?

A

inside the cell

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7
Q

what are the sites of enzyme action?

A

extracellular
intracellular

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8
Q

What are the two different models for enzyme reaction?

A
  1. lock and key theory
  2. induced fit hypothesis
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9
Q

What does the lock and key model suggest?

A

that the substrate has a complementary shape to the enzymes active site and therefore that many enzymes only catalyse one substrate

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10
Q

What does the induced fit hypothesis suggest?

A

active site of enzyme changes shape slightly to accommodate the substrate to form an enzyme substrate complex, the reverts to it’s original active site shape

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11
Q

what is the example for the induced fit hypothesis? And how does it work?

A

the enzyme lysozyme
it is an antibacterial enzyme in human saliva, tears and mucus
it attaches to the wall of bacteria and breaks glycosidic bonds

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12
Q

what does itt mean if an enzyme has disulphide bonds present?

A

it is likely to withstand quite high temperatures

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13
Q

Enzymes are biological catalysts. How do they bring about the effect of speeding up a reaction?

A

The substrates fit into the active site of the enzyme and therefore lowers the activation energy

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14
Q

What are the four factors affecting enzyme rate of reaction?

A
  1. substrate concentration
  2. temperature
  3. pH
  4. enzyme concentration
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15
Q

how does substrate concentration effect the enzyme rate of reaction?

A

when the substrate increases in an enzyme-controlled reaction, there is a greater chance of a successful collision between the substrate and the enzyme, resulting in more enzyme-substrate complexes forming.

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16
Q

what is a plateau?

A

the maximum rate of reaction for the conditions reached

17
Q

how does temperature effect the enzyme rate of reaction?

A

temp increases, enzyme and substrate molecules gain mroe kinetic energy, increasing chance of more successful collisions, therefore increasing chance of more substrate complexes formed.

18
Q

what happens above the optimum rate of reaction for enzymes?

A

rate of reaction decreases rapidly as hydrogen bonds in the tertiary structure break due to increased vibrations resulting in a change to the shape of the active site (denaturing)

19
Q

how does pH effect the enzyme rate of reaction?

A
  • a change in H+ or OH- can affect the bonds of the enzymes tertiary structure, causing a change in the active site
  • the active site is no longer complimentary to the substrate so fewer enzyme substrate complexes are formed which is irreversible
20
Q

What does OH- do to the pH? H+?

A

OH- increases pH
H+ decreases pH

21
Q

What does a competitive inhibitor do?

A

interferes with the active site of the enzyme so the substrate cannot bind

22
Q

How does a competitive inhibitor work?

A

It has a similar shape to the substrate and it is complimentary to the active site of the enzyme, this means it can block up the active site which forms an enzyme-inhibitor complex.
Therefore, this limits the number of enzyme substrate complexes that can form. Enzyme does not catalyse the reaction so no products formed, which reduces the reaction rate

23
Q

how does a non-competitive inhibitor work?

A

Attaches to an enzyme on the allosteric site, in doing so it changes the shape of the active site which means that enzyme-substrate complexes cannot form and thus no catalysis can happen(no product formed)

24
Q

What would a graph with a competitive inhibitor look like compared to without an inhibitor?

A

lower rate of reaction, eventually producing the same amount as without the inhibitor but it takes longer

25
Q

What would a graph with a non-competitive inhibitor look like compared to without an inhibitor?

A

lower rate of reaction never producing the same amount as no product formed

26
Q

What are immobilised enzymes?

A

enzymes that are fixed to an inert matrix

27
Q

What are the two ways in which immobilised enzymes can be achieved?

A
  1. entrapment - held inside a gel eg silica gel
  2. micro-encapsulation - trapped inside a micro-capsule eg alginate beads
28
Q

What are the advantages to immobilised enzymes?

A
  1. enzyme can be easily recovered and reused
  2. product is not contaminated by the enzyme
  3. more stable at higher temp
  4. catalyse reactions in a wider range of pH
29
Q

What is the result in immobilising enzymes?

A

several enzymes with different temperature and pH optima can be used at the same time and enzymes can be easily added or removed giving greater control over the reaction.

30
Q

What is an example of micro-encapsulation and how does it work?

A

Alginate beads
- beads containing the enzyme can be packed into glass column, and substrate added at one end
- rate of flow of substrate over beads can be controlled with a slower flow rate giving more time for enzyme-substrate complexes to form therefore yield more product
- bc enzymes in own ‘micro-environement’ enzymes are less susceptible to changes in pH, temp and action of chemicals such as organic solvents

31
Q

What is a buffer solution and what does it do?

A

a chemical that resists changes in pH
it neutralises excess acids or alkali’s and can be used to maintain the pH for a reaction