Enzyme Kinetics Flashcards

1
Q

What are enzymes ?

A
  • enzymes are biological catalysts
  • they work under mild conditions
  • they are specific for a particular reaction and a particular substrate
  • they can be regulated to control the speed of reactions
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2
Q

What do enzymes do ?

A

1) they bind 2 substrate molecules and orientate them to lower the activation energy
2) they bind a substrate and rearrange the electrons to lower the activation energy
3) they place a strain on the bonds in the substrate to lower the activation energy

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3
Q

What is enzyme kinetics ?

A

The study of how the rate of the catalysed reaction changes when the experimental conditions are changed

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4
Q

Briefly describe what happens when a substrate binds to an enzyme

A

The substrate binds to the enzyme and this is a reversible process
The reaction then occurs and the products dissociate

E + S <> ES > E + P

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5
Q

How does substrate concentration affect enzyme activity ?

A

At low substrate concentration, only a small amount of enzyme substrate complexes form
As substrate concentration increases the number of enzyme substrate complexes formed increases
At high substrate concentration most of the enzymes have a substrate bound and so the enzyme is now limiting the rate of the reaction and the rate of the reaction will remain the same

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6
Q

What is V max ?

A

It is the maximum velocity of the enzyme

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7
Q

What is the name given to the equation used to calculate the velocity of an enzyme ?

A

The Michaelis - Menten equation

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8
Q

What are the 2 isoenzymes of hexokinase ?

A
  • hexokinase (found in all cells)
  • glucokinase (found in liver and pancreatic beta cells)

They both catalyse the same reaction but have different kinetics

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9
Q

What has enzyme inhibition been useful for ?

A

It has been useful in -
• understanding how enzymes work
• producing drugs

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10
Q

What are the 2 types of reversible inhibition ?

A
  • competitive inhibition
  • non competitive inhibition
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11
Q

How does competitive inhibition work ?

A

The inhibitor has a similar tertiary structure to the substrate and so it binds to the enzyme active site
This means the substrate and inhibitor cannot be active at the same time

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12
Q

How does non-competitive inhibition work ?

A

The inhibitor binds to the allosteric site and changes the tertiary structure of the enzyme active site so the substrate is no longer able to bind to the active site

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13
Q

What is irreversible inhibition ?

A

It is when an inhibitor binds to an enzyme permanently

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14
Q

What can irreversible inhibitors be used for ?

A

In the diagnosis and treatment of disease

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