Proteins and Enzymes

ID #2391

Can a substrate bind to the active site with the inhibitor binding to the allosteric site afterwards, kicking it out? Also can a high concentration of substrate prevent the inhibitor from reaching the allosteric site?


In non-competitive reversible inhibition binding an inhibitor to the allosteric site changes the conformation of enzyme's active site to prevent substrate binding. 
The important part to understand here is the inhibitor and the substrate are not binding to the same location. So, increasing the concentration of substrate is NOT going to prevent the inhibitor from binding the allosteric site because the substrate is NOT competing with the inhibitor to bind the allosteric site. 
If a substrate is bound at the active site of an enzyme, the enzyme will convert the substrate to product releasing the product quickly because the point of using an enzyme is to speed up the rate of a naturally occurring reaction. So as one of the slides from lecture 7 show, we're talking about the inhibitor binding the allosteric site to prevent the next substrate from binding the active site in non-competitive reversible enzyme inhibition. 

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