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    hi, im just revising enzyme inhibition and was slightly confused by why a competitive inhibitor doesn't get catalysed by the enzyme once its blocking the active site?

    thanks in advance !
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    Because the inhibitor is blocking the active site and not allowing the substrate to bind with it which prevents enzyme-substrate complexes from forming.

    Is that why you meant? :s


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    no but thanks for reply.

    i mean like when the inhibitor blocks the active site and forms an enzyme-inhibitor complex, why does the enzyme not break down the inhibitor like it would if an enzyme-substrate complex was formed?
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    Competitive inhibitors often have subtly different shapes which means that though they can fit in the pocket they aren't chemically suitable to be processed as the native substrate would.
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    oh okay so an enzyme can only catalyse a substrate if they have chemical similarities?

    so a competitive inhibitor to maltase for example will contrast chemically, whereas maltase and maltose will be very similar and thus can go ahead with the reaction?

    thanks.
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    Substrates have a complimentary shape - so, they will fit into the active site AND bind chemically with the active site. While competitive inhibitors have a similar shape so they will be able to fit inside the active site, but won't be catalysed because the shape isn't complimentary and doesn't fit 'perfectly'.
    Do you do chemistry? :-)
 
 
 
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