Enzyme Inhibitors

Enzyme Inhibition:
Competitive inhibitors bind to the active site of the enzyme. They have a shape similar to that of the substrate, which allows them to fit the active site of the enzyme. If the amount of substrate is higher then the amount of inhibitor though, as the inhibitor doesn’t stay there, it when it goes, the active site it leaves empty has to be filled, and if the substrate concentration is higher, the active site is more likely to be filled by a substrate as opposed to an inhibitor. Therefore, competitive inhibition can be overcome.
Non-competitive inhibitors attach to the inhibitor at a site other then the active site. When it attaches to the enzyme, it changes the shape of it, and the shape of the active site, so a substrate cannot occupy it, therefore, the enzyme can’t function. The substrate and inhibitor are not competing for the same site, so an increase is substrate will not affect it, so it cannot be overcome.
Enzyme inhibition is when substances directly or indirectly interfere with the functioning of the active site of an enzyme and thus, reduce its activity.
1) A competitive inhibitor enters the active site, as it is about the same shape as the substrate, and it blocks a substrate from entering. It can be over come, though, if the substrate concentration is increased. A non competitive inhibitor enters the enzyme at a site other then the active one and therefore, the substrate concentration cannot affect it, as they aren’t competing for the same site and they can’t be over come. By enter at another site, they change the shape of the enzyme, and therefore, the active site, so no more enzyme substrate complexes could be formed and no more products would be made.
2) You could tell if a inhibitor was competitive or non competitive by increasing the amount of substrate, as an increase in substrate only affects competitive inhibitors, so they would be non competitive if nothing happened.