Describe how molecular shape is important in explaining the way in which enzymes may be affected by inhibitors

Answer 1

A non-competitive inhibitor would bind to the enzyme at a site far off from the active site.But this binding would affect the geometry of the active site in such a manner that there would be no nice fitting of the the substrate and hence there would not be any catalysis.

Answer 2

The effectiveness of the inhibitor in binding to the enzyme's active site (or other site if the inhibitor is allosteric) is dictated by its shape. If the inhibitor is non-allosteric, then it must bind to the active site with higher affinity than the ligand molecule, or else it won't be a very effective inhibitor. If the inhibitor is allosteric, then it must bind to the enzyme and change the enzyme's shape so that the ligand can no longer bind to the active site. Enzyme shape is also important for this process, since an inhibitor's molecular shape often determines whether it will be able to bind at all.

Answer 3

It's not that important.