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Models of Enzyme Action quiz
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What are the two main models that describe enzyme-substrate interaction?
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What are the two main models that describe enzyme-substrate interaction?
The two main models are the lock and key model and the induced fit model.
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Terms in this set (15)
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What are the two main models that describe enzyme-substrate interaction?
The two main models are the lock and key model and the induced fit model.
In the lock and key model, how is the enzyme's active site described?
The active site is rigid and unchanging in the lock and key model.
How does the substrate fit into the enzyme in the lock and key model?
The substrate fits precisely into the active site, like a key fits into a lock.
What does the lock and key model imply about the specificity of enzyme-substrate interaction?
It implies a very specific and unchanging interaction between the enzyme and substrate.
How does the active site compare to the substrate in the lock and key model?
The active site is identical in shape to the substrate in the lock and key model.
What is the main feature of the induced fit model regarding the active site?
The active site is flexible and can change shape to accommodate the substrate.
How does the active site interact with the substrate in the induced fit model?
The active site adapts its shape to fit the substrate, allowing a dynamic interaction.
Is the active site a perfect match to the substrate in the induced fit model?
No, the active site only resembles the substrate and is not an identical match.
Which model is considered a more accurate representation of most enzyme actions?
The induced fit model is considered more accurate for most enzyme actions.
What happens to the enzyme's active site when the substrate binds in the induced fit model?
The enzyme's active site changes shape to accommodate the substrate.
What is formed when the enzyme and substrate interact in either model?
An enzyme-substrate complex is formed.
How does the lock and key model view the complementarity between enzyme and substrate?
It views them as perfectly complementary in shape.
How does the induced fit model view the complementarity between enzyme and substrate?
It sees them as similar but not identical, requiring the active site to adjust.
Why is the lock and key model less accurate for most enzyme-substrate interactions?
Because most enzymes and substrates do not match up perfectly in shape.
What allows the enzyme to form a complex with the substrate in the induced fit model?
The flexibility and ability of the active site to change shape allows complex formation.