This site is intended for healthcare professionals

Go to /sign-in page

You can view 5 more pages before signing in

Malate-aspartate carrier system

Last reviewed dd mmm yyyy. Last edited dd mmm yyyy

Authoring team

The malate-aspartate carrier system acts across the inner mitochondrial membrane as a means of:

  • replenishing supplies of oxidized NAD within the cytoplasm in order to permit continued glycolysis
  • passing energy in the form of reduced NAD across the mitochondrial membrane, across which it cannot physically pass, for conversion to ATP within the mitochondria
  • transferring oxaloacetate from mitochondrion to cytoplasm during gluconeogenesis

Cytoplasmic malate dehydrogenase oxidizes NADH to NAD in tandem with reduction of oxaloacetate to malate. Malate is capable of diffusion across the inner mitochondrial membrane where the reverse reaction takes place with the formation of NADH and oxaloacetate.

Oxaloacetate is then converted to aspartate within the mitochondrion by the action of aspartate aminotransferase. Aspartate, unlike oxaloacetate, is capable of diffusing outwards where it then undergoes the reverse reaction to regenerate oxaloacetate.

During gluconeogenesis, the reverse series of reactions take place. These permit mitochondrial oxaloacetate, derived from pyruvate, to cross the inner mitochondrial membrane.


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.