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    Hey!

    Can you please explain how competitive and non-competitive inhibitors work.

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    (Original post by wigman15)
    Hey!

    Can you please explain how competitive and non-competitive inhibitors work.

    Thanks
    A competitive inhibitor binds reversibly to the active site of an enzyme. It is structuraly very similar to the substrate itself. It therefore competes with the substrate, and can be removed when the substrate is in a high enough concentration. An irreversible inhibitor binds to another region on the enzyme molecule in such a way as to alter the shape of the enzyme's active site, for example it may attract and electron from the active site region, in the case of NAD+. In this case, the effects are irreversible as the enzyme will have denatured.
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    Thanks for the breakdown. I get it now!
 
 
 

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