Enzymes Flashcards

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1
Q

Significance of Vmax

A

Maximum rate of reaction, different for different enzymes and reflects their turnover number

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2
Q

Km

A

Gives you an idea of the efficiency of enzymes - higher turnover, higher Km

Half Vmax

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3
Q

Without enzymes

A

Most of body’s biochemical reactions would be too slow

Enzymes are proteins, identified using Biuret test (purple)

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4
Q

Enzymes

A

Speed up reactions without being changed at the end of the reaction

Only speed up 1 reaction as they are specific

Can be intracellular (DNA helical and DNA polymerase)

Or extracellular (digestive enzymes eg amylase that catalyse hydrolysis reactions)

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5
Q

Intracellular

A

Synthesised in the cell and work in the cell

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6
Q

Extracellular

A

Synthesised in the cell and works outside the cell

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7
Q

Zymase

A

First enzyme to be discovered, in yeast

Catalyses conversion of sugars to alcohol

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8
Q

Properties of enzymes

A
  • generally work very rapidly
  • not destroyed or used up by the reactions that they catalyse
  • they are specific, work by the lock and key hypothesis so they are only found in small amounts inside cells
  • proteins, and are chains of amino acids
  • complex tertiary structure held together by hydrogen, ionic and disulphide bonds
  • denatured by several factors including high temperatures and pH changes
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9
Q

Practical application

A

Catalase is an enzyme found in all living cells, and it speeds up the breakdown of hydrogen peroxide inside the cells to the products water and oxygen

Good sources of catalyse include liver, potato and celery

2H2O2 > 2H2O + O2

V fast turnover rate

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10
Q

Turnover rate

A

No substrate molecules converted into products

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11
Q

Reactions at low temperatures

A

Enzymes ensure reactions can happen at relatively low temperatures

They lower the activation energy of the reaction

Activation energy is the minimum energy required to overcome the repulsion between molecules

They do this by forming an E-S complexes and bending bonds

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12
Q

Formation of an enzyme-substrate complex increases the rate of reaction

Explain how

A

By lowering activation energy by bending bonds

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13
Q

Explain why maltase only breaks down maltose

A

Tertiary structure means the active site is complementary to maltose

Description of induced fit

Enzymes lower activation energy by forming E-S complexes

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14
Q

Once reaction is complete

A

The enzyme is free to bind with another molecule of substrate

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15
Q

Enzymes type

A

Globular protein with a complex tertiary structure

The combination of the enzyme with its substrate molecules is called an E-S complex and the part of the enzyme that fits with the substrate is called the active site

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16
Q

Prosthetic groups

A

Some have prosthetic groups that are non-protein and some are activated by inorganic ions e.g. ATP hydrolyse and calcium ions

17
Q

Globular

A

As globular proteins, anything that affects the 3D shape, affects the ability of the enzyme to do its job

18
Q

Lock and key hypothesis

A

Enzymes are specific to the reactions that they catalyse

Only 1 substrate or type of substrate will fit into the active site

The active site and substrate are complementary shapes

The ability of the enzyme to combine with the substrate is due to its tertiary shape

19
Q

Induced fit hypothesis

A

Enzymes and substrate slot together to form a E-S complex which enables the enzyme to lower the activation energy

Once the reaction has been catalysed, the products are no longer complementary shapes to the active site and the complex breaks up

Releasing the products and freeing the enzyme for further catalytic action

20
Q

Induced fit development

A

Built on the lock and key hypothesis, suggesting that enzymes are more flexible and can mould to the shape of the substrate when it enters the active site