<p>What is the difference between allosteric inhibition and noncompetitive inhibition?</p>
<p>Different sources equivocate on this issue, and all that I could find on the internet was:</p>
<p>“All you really know when you identify an inhibitor as “non-competitive” is that it reduces the active concentration of enzyme without changing the affinity of the enzyme toward substrate.
Non-competitive inhibition is primarily defined on the basis of the effect on enzyme kinetics: insensitivity to substrate concentration. Such insensitivity could be brought about by interference with the activity of the enzyme without distortion and without affecting substrate binding by blocking or masking a side chain necessary for the catalysis (Hg++ masking a sulfhydral, or a small organic compound binding to a Cu++ which acts as a necessary prosthetic group). Allosteric inhibition on the other hand always involves a distortion or change in the shape of the protein.”</p>
<p>I don’t know what to make of this info. My Campbell AP Bio book told me that noncompetitive inhibition also engages in enzyme’s conformational change… </p>
<p>Will someone help me? Thanks :D</p>