This site is intended for healthcare professionals

Go to /sign-in page

You can view 5 more pages without signing in

Enzyme kinetics

Authoring team

Enzymes are thought to work by reducing the activation energy for a given equilibrium reaction. This may be via the formation of an intermediate state complex between enzyme and substrate. Enzyme kinetics deals with the way in which enzyme-catalyzed reactions are modified by variations in variables such as:

  • temperature
  • pH
  • enzyme concentration
  • substrate concentration
  • inhibitors

Some reactions do not obey the normal kinetic phenomena; binding of substrate at one site may alter the binding of further substrate at a second site on the same enzyme. This is an allosteric interaction resulting in co-operativity - one active site modulating the function, usually increasing the sensitivity, of another.


Create an account to add page annotations

Annotations allow you to add information to this page that would be handy to have on hand during a consultation. E.g. a website or number. This information will always show when you visit this page.

The content herein is provided for informational purposes and does not replace the need to apply professional clinical judgement when diagnosing or treating any medical condition. A licensed medical practitioner should be consulted for diagnosis and treatment of any and all medical conditions.

Connect

Copyright 2024 Oxbridge Solutions Limited, a subsidiary of OmniaMed Communications Limited. All rights reserved. Any distribution or duplication of the information contained herein is strictly prohibited. Oxbridge Solutions receives funding from advertising but maintains editorial independence.