How do non-competitive inhibitors work?

A non competitive inhibitor has a different shape to the substrate molecule.The inhibitor binds to an allosteric site.This causes a conformational change meaning the substrate is no longer able to bind to the active site.No enzyme substrate complex is formed therefore the reaction cannot take place.

KG
Answered by Kayatre G. Biology tutor

2770 Views

See similar Biology A Level tutors

Related Biology A Level answers

All answers ▸

In genetics, what does co-dominance mean?


Why do foetuses have different haemoglobin to adults?


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


How is the lung adapted for gaseous exchange?


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:

© 2026 by IXL Learning