Proteins and Enzymes

ID #2384

In reversible inhibition, competitive or non-competitive, will the inhibitor eventually fall out? What about in the event that it is attached to the allosteric site? Also will the inhibitor have a higher chance of staying attached if the conformational change in enzyme completely prevents substrate binding?


In reversible inhibition, yes, the inhibitor will eventually leave the site. The inhibitor may bind again after it has left the site, however. 
This is true of the allosteric site as well. 
As for the relationship between the inhibitor and the substrate, that depends on whether it is a competitive or non-competitive inhibition. 
In either case, the inhibitor won't be released more quickly if the substrate is present. It's more a race to see what will happen after the inhibitor is released. 
In competitive interactions, the dependence on substrate is based on probability. Basically, who gets to bind the active site once the inhibitor has been released depends on if there is more substrate or inhibitor around. 
In non-competitive interactions, it does not matter. This is because the inhibitor is targeting the allosteric site. Because of that binding, the active site is changed so that it can't bind the normal substrate.

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