Enzyme activity can be prevented by inhibitors. The two
types of inhibitors are competitive and non- competitive.
A competitive inhibitor bears a similar shape to that of the
substrate, therefore it can compete with the substrate t bind to the active
site of the enzyme. If an inhibitor binds to an enzymes active site before the
substrate does, the substrate cannot bind to that particular active site as it
has been blocked. If there is a high concentration of inhibitors, the inhibitors
will take up almost all of the active sites, leaving non for the substrates.
However, if there is a high amount of substrate then the chances of the
substrate binding to an active site before the inhibitor does are increased.
Non-competitive inhibitors bind to the enzyme away from the
active site. This changes the shape of the active site and therefore substrates
can no longer fit. Unlike w
ith competitive inhibitors, increasing the
concentration of substrates will not make much of a difference as they are not
both competing for the active site.The graph shows how increasing the amount of subtrate concentration would affect the rate of reaction for both types of inhibitors.