Enzyme Inhibition (College Board AP® Biology): Study Guide

Cara Head

Written by: Cara Head

Reviewed by: Ruth Brindle

Updated on

Competitive & noncompetitive enzyme inhibition

  • Enzyme inhibitors slow down or stop enzyme activity, decreasing the rate of reaction

  • Increasing the concentration of an inhibitor, therefore, reduces the rate of reaction and eventually, if inhibitor concentration continues to be increased, the reaction will stop completely

Competitive inhibitors

  • Competitive inhibitors have a similar shape to that of the substrate molecules and therefore compete with the substrate for the active site

  • Competitive inhibitors can bind reversibly or irreversibly to the active site of the enzyme

Reversible inhibitors

  • Reversible inhibitors do not form covalent bonds with the enzyme, unlike irreversible inhibitors, therefore their effects can be reduced or reversed by:

    • removing the inhibitor

    • increasing substrate concentration (in the case of competitive inhibitors)

  • This can increase the rate of reaction once more

Irreversible inhibitors

  • An irreversible inhibitor of enzymes is a molecule that binds to an enzyme and permanently inactivates it, usually by forming a covalent bond in the active site

  • The inhibition cannot be reversed by removing the inhibitor or increasing substrate concentration as the inhibitor permanently bonds to the active site, blocking substrates from binding

Noncompetitive inhibitors

  • Noncompetitive inhibitors bind to allosteric sites (not the active site) of an enzyme

  • They can attach with or without the substrate already bound

  • Binding alters the active site's shape, preventing substrate binding or reducing enzyme-substrate complex formation

  • Increasing substrate concentration does not overcome inhibition, as the inhibitor does not compete for the active site

  • The active site remains altered, blocking enzyme function

Competitive and non-competitive inhibition, downloadable AS & A Level Biology revision notes
Competitive and non-competitive inhibition

Rate of enzyme reactions & inhibitors

  • A competitive inhibitor will lower the initial rate of reaction by occupying some of the available active sites

    • Eventually, the same amount of product will be produced as would have been produced without the competitive inhibitor, therefore the maximal rate is not affected

  • Non-competitive inhibitors lower the initial rate of reaction and the maximal rate of reaction will be lower, therefore a lower amount of product is produced than would normally be produced

The effect of inhibitor concentration on an enzyme-catalysed reaction, downloadable AS & A Level Biology revision notes
The effect of inhibitor concentration on the rate of an enzyme-catalysed reaction

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Cara Head

Author: Cara Head

Expertise: Biology Content Creator

Cara graduated from the University of Exeter in 2005 with a degree in Biological Sciences. She has fifteen years of experience teaching the Sciences at KS3 to KS5, and Psychology at A-Level. Cara has taught in a range of secondary schools across the South West of England before joining the team at SME. Cara is passionate about Biology and creating resources that bring the subject alive and deepen students' understanding

Ruth Brindle

Author: Ruth Brindle

Expertise: Biology

Ruth graduated from Sheffield University with a degree in Biology and went on to teach Science in London whilst also completing an MA in innovation in Education. With 10 years of teaching experience across the 3 key science disciplines, Ruth decided to set up a tutoring business to support students in her local area. Ruth has worked with several exam boards and loves to use her experience to produce educational materials which make the mark schemes accessible to all students.