Biological Reactions Regulated By Enzymes- Unit 1.4 Flashcards

1
Q

Where do the enzyme and substrate combine?

A

The active site

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2
Q

What protein structure do all enzymes have?

A

Tertiary in 3D spherical globular shape

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3
Q

Anabolic vs catabolic enzymes.

A

Anabolic- build larger products from smaller substrates.

Catabolic- break large substrates into smaller products.

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4
Q

What is the function of a lysozyme?

A

To destroy pathogenic bacteria by breaking down their cell walls by breaking glycosidic bonds between the amino sugars.

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5
Q

How is a substrate held in place when attached to a lysozyme?

A

Hydrogen and ionic bonds

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6
Q

What is the lock and key hypothesis?

A

There is an exact fit between substrate and active site of an enzyme.

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7
Q

What is the induced fit hypothesis?

A

Active site is not exactly the right shape to begin with. The substrate changes the shape of the active site to fit the substrate perfectly. (complementary shape)

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8
Q

Name 2 enzyme properties.

A
  1. Specific- each enzyme will catalyse only one particular reaction.
  2. Very efficient & have a high turnover number. (can convert many molecules of substrate into product per unit)
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9
Q

What is activation energy and what is it used for?

A

Energy needed to start chemical reactions by breaking chemical bonds inside molecules.

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10
Q

Do body enzymes increase or decrease the activation energy of a reaction?

A

The lower it, reducing input of energy needed to allow reactions to take place, meaning they can take place at lower temperatures.

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11
Q

What are the factors that can affect enzyme activity? (4)

A

Changing:

  1. Temperature
  2. pH
  3. Substrate concentration
  4. Enzyme concentration
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12
Q

What happens when temperature is increased?

A
  1. Gives molecules greater kinetic energy as enzyme & substrates move around quicker, increasing chance of collision.
  2. Increase rate of reaction.
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13
Q

For each 10°C rise…

A

Rate of reaction doubles

general rule

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14
Q

How do enzymes denature?

A

Vibrations break hydrogen bonds within the active site, causing shape to change.

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15
Q

What is the turn-over number?

A

The number of substrate molecules that one enzyme molecule can turn into products in a given time.

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16
Q

What is a limiting factor?

A

A factor is limiting when an increase in its value causes an increase in rate of reaction.

17
Q

What is an enzyme inhibitor? (2)

A
  1. Any substance which decreases rate of an enzyme catalysed reaction or stops it.
  2. Can be competitive of non-competitive.
18
Q

Describe competitive inhibitors. (2)

A
  • Structurally similar to substrate.

* Can fit into active site, preventing enzyme-substrate complex forming.

19
Q

What effect will increasing substrate concentration have on a competitive inhibitor?

A

Decreasing likeliness of inhibitor colliding with enzyme as less likely to bind with active site.

20
Q

Describe non-competitive inhibitors. (2)

A
  • Do not bind to active site, but does anywhere else.

* Alters overall shape or enzyme, including active site so that substrates cannot fit onto it.

21
Q

What effect will increasing substrate concentration have on a non-competitive inhibitor?

A

Will not increase rate of reaction as substrate can no longer fit into enzymes active site.

22
Q

What are immobilised enzymes?

A

Fixed, bound or trapped on an inert matrix. (prevent them from moving, reducing frequency of successful collisions)

23
Q

Name advantages of using immobilised enzymes. (7)

A
  1. Enzyme does not contaminate product.
  2. Can be recovered & reused.
  3. Only small quantity needed.
  4. Great stability.
  5. Denature at higher temperatures.
  6. Catalyse reactions over wider range of pH.
  7. Greater control over process.
24
Q

What are biosensors?

A

Can detect biologically important molecules rapidly, even at low concentrations.
e.g. Used to measure blood glucose in diabetics.

25
Q

How do biosensors work?

A

Use immobilised enzymes on a gel membrane to detect chemical changes and turns it into an electrical signal.