🩷 3.1.4.2 Many proteins are enzymes Flashcards

(24 cards)

1
Q

What are enzymes?

A

It is a protein which is a biological catalysts which lower the activation energy of the reaction it catalyses

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2
Q

What is the induced fit model ?

A
  • The enzymes active site and the substrate are not initially complementary
  • The active site moulds around the substrate, becoming complimentary and putting pressure on the substrates bonds
  • The bonds bend and break causing the activation energy of the enzyme to reduce
  • Enzyme-substrate complexes are formed
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3
Q

What is the lock and key model?

A

The enzyme active site is initially complementary to the substrate. They bind and form enzyme-substrate complexes.

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4
Q

Define active site

A

The area on the enzyme to which the substrate binds. The active site is only complementary to one substrate. When they bind they form enzyme substrate complexes

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5
Q

Define enzyme substrate complexes

A

These form due to successful collisions between enzymes and substrates

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6
Q

Define kinetic energy

A

This is the movement energy conferred to particles due to temperature

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7
Q

Define successful collisions

A

Collisions which result in enzyme substrate complexes forming

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8
Q

Define complementary shape

A

When the shape of the substrate allows it to fit into the shape of the enzymes active site

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9
Q

Define tertiary structure

A

This defines the shape of the active site

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10
Q

Define specific shape

A

The shape of both the substrate and the enzyme are specific to each other so that no other substrate can bind

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11
Q

Define similar shape

A

Used to describe the relationship between competitive inhibitors and substrates

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12
Q

What are the four factors affecting rate of reaction?

A
  • temperature
  • concentration of substrate
  • concentration of enzyme
  • ph
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13
Q

Describe what would happen on a graph when temperature changes

A

When temperature increases, between … and … rate of reaction increases until optimum temperature. Final temperatures between … and … rate of reaction decreases

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14
Q

Explain what would happen when temperature changes on a graph

A
  • As temperature increases rate of reaction increases due to the increase in kinetic energy of the molecules
  • This means that there are more successful collisions so more enzyme substrate complexes are formed up until the optimum temperature
  • After this point, the enzymes denature and bonds break, causing the tertiary structure to change
  • The active site is no longer complementary to that of the substrate so no more enzyme substrate complexes are formed
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15
Q

Describe what would happen on a graph when ph changes

A

As ph increases between … and … rate of reaction increases. After the optimum ph … rate of reaction decreases

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16
Q

Explain what would happen when ph changes on a graph

A
  • At low Ph there is a high concentration of hydrogen ions (H+) which are also known as protons.
  • These break the hydrogen/ionic bonds causing the tertiary structure to change and making the active site no longer complementary to the substrate.
  • This means that there are less enzyme substrate complexes formed
  • After the optimum ph, as the ph increases the concentration of hydroxyl ions (OH) increases
  • These also break the hydrogen/ionic bonds causing the same effect as the protons
17
Q

Describe the effect of substrate concentration on graphs

A

As substrate concentration increases, the initial rate of reaction increases. The rate of reaction then plateus

18
Q

Explain the effect of substrate concentration on a graph

A
  • Initially the rate of reaction increases as the increase in substrate concentration causing as increases in the number of enzyme substrate complexes formed
  • The rate of reaction then plateaus because enzymes become the limiting factor as all of there active sites have become saturated
19
Q

Describe the effect of enzyme action on a graph

A

As enzyme concentration increases rate of reaction increases

20
Q

Explain the effect of enzyme concentration on rate of reaction

A
  • Increasing enzyme concentration increases the rate of reaction as more enzyme substrate complexes are formed however in reality, enzyme concentration would not exceed that of the substrate
21
Q

Describe and explain the effect of a competitive inhibitor

A
  • The competitive inhibitor and the substrate are a similar shape
  • They can both (separately) bind to the enzymes active site and compete to do so
  • The higher the concentration of the competitive inhibitor, the fewer enzyme substrate complexes formed
22
Q

Describe and explain the effect of a non competitive inhibitor

A
  • The non competitive inhibitor binds to the enzyme away from the active site
  • This changes the shape of the active site as it changes its tertiary structure
  • The substrate is no longer complementary to the active site so no enzyme substrate complexes can be formed
23
Q

On a graph with competitive inhibitor, non competitive inhibitor and normal enzyme, which inhibitor would catch up to the normal enzyme with increasing substrate?

A

Competitive inhibitor

24
Q

Which inhibitor cannot be overcome by increasing substrate concentration and why?

A

Non competitive inhibitor due to it causing a change in the shape of the active site