Enzyme Inhibition
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Transcript of Enzyme Inhibition
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{Enzyme Inhibition
Why enzymes don’t work
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An enzyme is just a folded protein
Remember!!!
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Organic catalysts-speed up the rate of the reaction
Proteins have –ase after their name
Enzymes are…
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Enzymes
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Enzymes fit together with substrates to aid a chemical reaction
Lock and Key vs Induced Fit Video on my website that you
need to watch and take notesDue by Friday!
Enzymes
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There are several things that can effect the rate at which an enzyme works: temperature, pH, enzyme concentration, substrate concentration, and the presence of inhibitors or activators.
Things effecting the rate at which and enzyme works
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When and enzyme stops working in its normal manner. This could be due to a variety of inhibitors including: nonspecific, competitive, and noncompetitive.
What is enzyme inhibition?
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Non-specific: Any physical or chemical change that ultimately denatures any enzyme – irreversible
Denature – when the enzyme loses its folded shape; it basically falls apart because bonds have been broken
Non-specific vs Specific
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It fell apart
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Temperature – normally if you increase a temperature you speed up a reaction. However if you increase the temperature too much and it is no longer in the enzymes optimum range it will cause it to denature.
Things that can cause an enzyme to denature
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Example of a protein that has denatured due to increased temperature
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pH – an increase or decrease of pH out of the enzymes optimum range can cause denaturation.
Things that can cause an enzyme to denature
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Specific inhibition – only works on specific enzymes, not all of them
Competitive and non-competitive inhibition
Non-specific vs specific
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Competitive vs non-competitive
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An inhibitor competes with the substrate for the active site
Like a race Normally reversible if other substrates are available for the inhibitor to bind with
Competitive Inhibition
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An inhibitor binds to the enzyme at a site different than the active site.
This special site that is just for the inhibitor is called the allosteric site
Non-competitive Inhibition
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The binding of the inhibitor to the allosteric site normally changes the conformation of the active site so the substrate and enzyme can’t bind
Non-competitive Inhibition
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Normally this type of inhibition is not permanent.
However this is not true in all cases, sometimes it is irreversible and the enzyme can no longer work.
Non-competitive Inhibition
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Cofactors are non-protein inorganic chemical compounds bound to a protein Helps the protein function during
biochemical reactions and increase the rate at which the enzyme works
Coenzymes are organic molecules (usually vitamin or mineral) that are required by certain enzymes to carry out reactions
Cofactors and Coenzymes