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

5184 Views

See similar Biology A Level tutors

Related Biology A Level answers

All answers ▸

What are the similarities/differences between neuromuscular junctions and cholinergic synapses?


Describe the processes that take place during each stage of mitosis.


Explain what are the primary, secondary, tertiary and quaternary structures of a protein


Describe the pathway of electrical activity in the heart during contraction.


We're here to help

contact us iconContact ustelephone icon+44 (0) 203 773 6020
Facebook logoInstagram logoLinkedIn logo

MyTutor is part of the IXL family of brands:

© 2025 by IXL Learning