What is the difference between competitive and non-competitive inhibition of enzymes?

The main difference is that in competitive inhibition, the inhibitor binds directly to the active site of the enzyme. This therefore prevents the substrate from binding to the enzyme and forming the enzyme-substrate complex. It is directly competing with the substrate. In non-competitive inhibition, the inhibitor binds to a site on the enzyme that is NOT the active site. In doing so, it alters the conformation of the active site, meaning that the substrate can no longer bind to the active site on the enzyme. Competitive inhibition can be overcome by increasing the concentration of the substrate. This cannot occur with non-competitive inhibition.

Answered by Samantha D. Biology tutor

40737 Views

See similar Biology A Level tutors

Related Biology A Level answers

All answers ▸

In which ways are the lungs adapted for efficient gas exchange?


Describe the structure of a protein.


Describe the structural differences between DNA and RNA.


What is the role of mitosis in organisms?


We're here to help

contact us iconContact usWhatsapp logoMessage us on Whatsapptelephone icon+44 (0) 203 773 6020
Facebook logoInstagram logoLinkedIn logo
Cookie Preferences