An enzyme's activity can be reduced or stopped, temporarily, by a reversible inhibitor
There are two types of reversible inhibitors:
Competitive inhibitors have a similar shape to that of the substrate molecules and therefore compete with the substrate for the active site
Non-competitive inhibitors bind to the enzyme at an alternative site, which alters the shape of the active site and therefore prevents the substrate from binding to it
Competitive and non-competitive inhibition
Reversible inhibitors can act as regulators in metabolic pathways
Metabolic reactions must be very tightly controlled and balanced, so that no single enzyme can ‘run wild’ and continuously and uncontrollably generate more and more of a particular product
Metabolic reactions can be controlled by using the end-product of a particular sequence of metabolic reactions as a non-competitive, reversible inhibitor:
As the enzyme converts substrate to product, the process is itself slowed down as the end-product of the reaction chain binds to an alternative site on the original enzyme, changing the shape of the active site and preventing the formation of further enzyme-substrate complexes
The end-product can then detach from the enzyme and be used elsewhere, allowing the active site to reform and the enzyme to return to an active state
This means that as product levels fall, the enzyme begins catalysing the reaction once again, in a continuous feedback loop