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Enzymes (Factors that affect Reaction Rate (A temperature that is too high…
Enzymes
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Inhibitation
Competitive inhibitors are a similar shape to the substrate, meaning that it can bind to the active site of the enzyme
The forming of enzyme inhibitor complexes means that a lower amount of enzyme substrate complexes can be formed.
The effect that the competitive inhibitor has can be limited if a larger concentration of substrate is added.
Non-competitive inhibitors can bind to an allosteric site or somewhere which generally isn't the active site of the enzyme.
This distorts the tertiary structure of the enzyme and changes the shape of the active site. As a result, the active site is no longer complementary to the substrate meaning that this enzyme is useless.
The Two Theories
Lock and Key Theory
The substrate and enzyme are specific to each other. The active site and the substrate are specific to each other.
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Induced Fit Model
The substrate and enzyme are specific. The substrate is not completely complementary to the active site.
When the substrate binds to the active site, the active site changes shape slightly.
The enzyme puts pressure on the substrate causing bonds to be broken and formed with a lower activation energy.
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