Answer:
use own words
Step-by-step explanation:
In competitive inhibition, an inhibitor molecule is similar enough to a substrate that it can bind to the enzyme's active site to stop it from binding to the substrate. ... In noncompetitive inhibition, an inhibitor molecule binds to the enzyme at a location other than the active site (an allosteric site)
hat is the difference between competitive and non competitive inhibition?
The main difference is that in competitive inhibition, the inhibitor binds directly to the active site of the enzyme. ... Competitive inhibition can be overcome by increasing the concentration of the substrate. This cannot occur with non-competitive inhibition.