Enzyme activation energy

Enzymes catalyze chemical reactions. (IB Topic 2.5) We know that they have an active site
where the substrate binds and that when a substrate collides with an active site then a reaction
occurs.

The reason that enzymes speed up these reactions is all to do with the reaction’s activation
energy.
Activation energy = the minimum amount of energy required to start a chemical reaction.

Watch the animations about enzymes on this website:

http://www.ryancshaw.com/Files/micro/Animations/Enzyme-Substrate/micro_enzyme-
substrate.swf then answer the following questions.

1. Name a specific biological example of the reaction in the diagram above?

Write a word equation of the reaction (If you are struggling thing ‘digestion’)
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2. Describe what happens at the peak of the graph shown above.

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© David Faure, InThinking www.thinkib.net/biology 1

 Enzyme activation energy

3. Explain what enzymes do to the activation energy of a reaction and why this speeds up
the reaction?

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Extension / Revision
4. Explain how enzymes work, the active site, and the words substrate and product.

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© David Faure, InThinking www.thinkib.net/biology 2

 Competitive and non-competitive inhibitors

Enzymes catalyse specific reactions. The substrate binds to the active site forming an enzyme-substrate
complex, the reaction occurs and products are released from the active site.

1. Describe what is happening in the enzyme catalyzed reaction shown above.

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2. The table below compares the effect of a competitive inhibitor with a non-competitive
inhibitor.

The difference between a competitive inhibitor and a non-competitive inhibitor is

the place where the inhibitor binds.

Competitive inhibitor Non-competitive inhibitor

Binds at the active site and prevents Binds away from the active site, and can
substrate from binding to the active site. bind with the enzyme substrate complex.
Enzymes function normally if the substrate Prevents the enzyme functioning even if
has already bound to the active site. the substrate binds.

© David Faure, InThinking www.thinkib.net/biology 1

 Competitive and non-competitive inhibitors

Annotate the diagram below to show where a competitive inhibitor and a non-
competitive inhibitor will attach.

3. Sometimes a non-competitive inhibitor is produced by a metabolic pathway

Explain why the inhibition of the first enzyme in this metabolic pathway by the final
product, isoleucine, will make the reaction slow down when isoleucine molecules
increase in concentration.
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© David Faure, InThinking www.thinkib.net/biology 2

 Competitive and non-competitive inhibitors

The problem with competitive inhibitors is that as the substrate accumulates it competes more and
more successfully for the active site. At very high substrate concentration this gives a nearly normal rate
of formation of product.

1. Name a competitive inhibitor and the enzyme it inhibits

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2. Using the graph above compare the effect of a competitive inhibitor with a non-
competitive inhibitor.

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Enzymes have an active site where the substrate binds.

When a substrate collides with an active site a reaction occurs.

The difference between a competitive inhibitor and a non-competitive inhibitor is the

place where the inhibitor binds.

Competitive inhibitor Non-competitive inhibitor

Binds at the active site and prevents Binds away from the active site, and can
substrate from binding to the active site. bind with the enzyme substrate complex.
Enzymes function normally if the substrate Prevents the enzyme functioning even if the
has already bound to the active site. substrate binds.

© David Faure, InThinking www.thinkib.net/biology 1

 Competitive and non-competitive inhibitors

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3. Explain why an enzyme inhibited by a competitive inhibitor will continue to function
normally if it is flooded with a very high concentration of substrate.
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The graphs below show the effects of adding two inhibitors to the rate of reaction of an
enzyme. The blue line shows the enzyme rate at different substrate concentrations without an
inhibitor. The red lines show low concentration, medium conc. and high conc.

4. Describe the effect of increasing the concentration of inhibitor A in the graph shown
above.

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5. Deduce with a reason which enzyme is a non-competitive inhibitor?

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© David Faure, InThinking www.thinkib.net/biology 2

 Competitive and non-competitive inhibitors

Treatments of ethylene glycol intoxication

It is important to act promptly in cases of ethylene

glycol poisoning to prevent further conversion of
the remaining ethylene glycol into its toxic
metabolites in the liver.

Injecting ethanol or fomepizole will inhibit the

enzyme alcohol dehydrogenase and prevent
further metabolism of ethylene glycol.
These are both competitive inhibitors.

Extension
6. Suggest how a non-competitive inhibitor of alcohol dehydrogenase would work.
Annotate the diagram above if you wish.

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If you were a research biochemist and had conducted tests on a new trial inhibitor of
alcohol dehydrogenase, you might draw graphs of your results like the ones above.

7. Explain how the graphs of reaction rate against substrate concentration with and
without the inhibitor would show you whether the inhibitor was competitive or non-
competitive?

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© David Faure, InThinking www.thinkib.net/biology 3