What is allosteric inhibitor?
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An allosteric inhibitor by binding to allosteric site alters the protein conformation in active site of enzyme which consequently changes the shape of active site. Thus enzyme no longer remains able to bind to its specific substrate. Hence enzyme is unable to perform it's catalytic activity i.e enzyme is now inactive. This process is called allosteric inhibition.
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Allosteric inhibition is the negative control of a enzyme activity, by binding an inhibitory substance (effector molecule) to the enzyme. This binding doesn't happen at the active site, but leads to a conformational change which - in the negative control - reduces their affinity for their substrates.
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