This site is intended for healthcare professionals

CPD
CPD
Pro
Pro
Sign in
Go to /sign-in page

You can view 5 more pages before signing in

Go to /pro/cpd-dashboard page

This page is worth 0.05 CPD credits. CPD dashboard

Go to /account/subscription-details page

This page is worth 0.05 CPD credits. Upgrade to Pro

Fructose metabolism

Last reviewed dd mmm yyyy. Last edited dd mmm yyyy

Authoring team

Plasma fructose may enter cells for glycolysis or gluconeogenesis by one of two pathways:

  • in hepatocytes:
    • fructokinase converts fructose to fructose-1-phosphate
    • fructose-1-phosphate aldolase converts fructose-1-phosphate to dihydroacetone phosphate and glyceraldehyde
    • triose kinase converts glyceraldehyde to glyceraldehyde-3-phosphate
    • triose phosphate isomerase converts dihydroacetone phosphate to glyceraldehyde-3-phosphate
    • glyceraldehyde-3-phosphate then enters further glycolytic or gluconeogenic reactions according to the energy status of the hepatocyte

  • in other cells, particularly adipocytes:
    • hexokinase converts fructose into fructose-6-phosphate; fructose competes with glucose for phosphorylation
    • fructose-6-phosphate enters glycolysis

Related pages

Create an account to add page annotations

Create a free account

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.