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The polyol pathway involves the synthesis of fructose from glucose, but does not require energy from ATP like glycolysis does.<ref name="wikipedia"/>
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<ref name="Steuber"/> The first step of the pathway is the production of sorbitol from glucose, catalyzed by aldose reductase and using NADPH as a reducing cofactor.<ref name="wikipedia"/><ref name="Steuber"/> The second step in the pathway is the production of fructose from sorbitol, catalyzed by sorbitol dehydrogenase, which is NAD+ dependent. <ref name="wikipedia"/><ref name="Steuber"/> Under normal blood glucose levels most glucose is metabolized through glycolysis or the pentose phosphate pathway while only a small amount of glucose is metabolized through the polyol pathway.<ref name="wikipedia"/>
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Revision as of 06:53, 11 March 2011

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Contents

Aldose Reductase (2IKH)

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Wikipedia

Introduction

Aldose reductase is an oxidoreductase/dehydrogenase enzyme.[1] It reduces aldehydes and carbonyl, including monosaccharides to their corresponding alcohol products using NADPH as a cofactor.[1][2] Aldose reductase is most well known in the first step of the polyol pathway of glucose metabolism.[1][2]

Sub Title

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Polyol Pathway and Diabetes

The polyol pathway involves the synthesis of fructose from glucose, but does not require energy from ATP like glycolysis does.[1] [2] The first step of the pathway is the production of sorbitol from glucose, catalyzed by aldose reductase and using NADPH as a reducing cofactor.[1][2] The second step in the pathway is the production of fructose from sorbitol, catalyzed by sorbitol dehydrogenase, which is NAD+ dependent. [1][2] Under normal blood glucose levels most glucose is metabolized through glycolysis or the pentose phosphate pathway while only a small amount of glucose is metabolized through the polyol pathway.[1]

References

  1. ↑ 1.0 1.1 1.2 1.3 1.4 1.5 1.6 Wikipedia. Aldose Reductase. http://en.wikipedia.org/wiki/Aldose_reductase
  2. ↑ 2.0 2.1 2.2 2.3 2.4 Steuber H, Heine A, Klebe G. Structural and thermodynamic study on aldose reductase: nitro-substituted inhibitors with strong enthalpic binding contribution. J Mol Biol. 2007 May 4;368(3):618-38. Epub 2006 Dec 15. PMID:17368668 doi:10.1016/j.jmb.2006.12.004
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