H1 Biology and H2 Biology
What are the effects of non-competitive inhibitors on enzyme-catalysed reactions?
Notes from the video ‘H2 Biology Tuition | H1 Biology Tuition | Non-Competitive Inhibitors’:
In this Biology tutorial, we would learn about the effects of non-competitive inhibitors on enzyme-catalysed enzymes.
A non-competitive inhibitor binds to allosteric sites, or sites that are not the active site, on enzymes
Some inhibitors bind reversibly via weak bonds such as hydrogen bonds, while others bind irreversibly via strong covalent bonds.
This binding alters the conformation of the specific enzyme active site such that it is no longer complementary in shape to the substrate and rate of formation of enzyme-substrate complexes decreases so the rate of reaction is reduced.
The rate of reaction decreases as concentration of inhibitors increases and this effect cannot be neutralized by increasing the substrate concentration.