This occurs when an inhibitor does not bind to the active site but does bind to a different part of the enzyme and changes the active site shape.
This stops the substrate binding to the enzyme and decreases the reaction rate. Non-competitive inhibition cannot be reversed by increasing the substrate concentration. Examples of non-competitive inhibitors include cyanide, mercury and silver.
Competitive and non-competitive inhibitors can affect the reaction rates in a metabolic pathway.
The graph levels off because all of the active sites are occupied with the substrate.
There is a gradual increase in reaction rate because competitive inhibitors are occupying only some of the enzyme active sites. As substrate concentration increases, the substrate molecules outnumber the inhibitor so the reaction rate reaches the maximum.
Most enzyme molecules have become inactive but some are unaffected by the inhibitors so reaction rate remains low. An increase in substrate concentration does not increase reaction rate.