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Energy and Equilibrium

Quick questions on Enzyme inhibition: H2 Biology Energy and Equilibrium

6short Q&A pairs drawn directly from our worked dot-point answer. For full context and worked exam questions, read the parent dot-point page.

What is competitive inhibition?
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A competitive inhibitor has a shape similar to the substrate and binds the active site, competing with the substrate for it. While the inhibitor is bound, the substrate cannot enter, so the rate falls. Because the two compete, increasing the substrate concentration raises the chance that substrate wins the active site, so the inhibition can be overcome and the maximum rate is eventually reached.
What is non-competitive inhibition?
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A non-competitive inhibitor binds a site other than the active site (an allosteric site). This changes the shape of the active site so the substrate can no longer bind effectively. Because the inhibitor does not compete for the active site, increasing substrate cannot overcome it, and the maximum rate is reduced.
What is end-product inhibition (feedback control)?
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In a metabolic pathway, the final product often inhibits an enzyme catalysing an early (committed) step, usually by binding an allosteric site. As product accumulates it slows the pathway; as product is used up, inhibition is relieved and the pathway speeds up. This negative feedback prevents waste and keeps product levels balanced.
What is q1?
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State where a competitive inhibitor binds on an enzyme. [1 mark]
What is q2?
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Explain why increasing substrate concentration does not overcome non-competitive inhibition. [2 marks]
What is q3?
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Explain why end-product inhibition is described as negative feedback. [2 marks]

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