How are enzymes inhibited?

There are two types of enzyme inhibition: competitive and non-competitive. 

Competitive inhibition:
This occurs when an enzyme's active site is filled by an inhibitor. The inhibitor will have a complementary shape to the enzyme's active site and thus be able to bind to the active site and stop enzyme-substrate complexes from being formed. This inhibition is usually temporary. 

Non-Competitive Inhibition: 
This occurs when an inhibitor binds to a site on the enzyme that is not the active site. When this happens, the enzyme's active site changes shape, meaning the substrate is no longer complementary to the active site. Enzyme-substrate complexes can no longer be formed, resulting in a usually permanent inhibition. 

BM
Answered by Beth M. Biology tutor

4993 Views

See similar Biology A Level tutors

Related Biology A Level answers

All answers ▸

Frequent treatment with antibiotics can result in resistant strains of bacteria, explain how.


Describe and explain the function alveoli


What is the differences between mitosis and meiosis?


What are the differences between globular and fibrous proteins?


We're here to help

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

© MyTutorWeb Ltd 2013–2025

Terms & Conditions|Privacy Policy
Cookie Preferences