Title |
Crystal structure of Saccharomyces cerevisiae 6-phosphogluconate dehydrogenase Gnd1
|
---|---|
Published in |
BMC Molecular and Cell Biology, June 2007
|
DOI | 10.1186/1472-6807-7-38 |
Pubmed ID | |
Authors |
Weiwei He, Yi Wang, Wei Liu, Cong-Zhao Zhou |
Abstract |
As the third enzyme of the pentose phosphate pathway, 6-phosphogluconate dehydrogenase (6PGDH) is the main generator of cellular NADPH. Both thioredoxin reductase and glutathione reductase require NADPH as the electron donor to reduce oxidized thioredoxin or glutathione (GSSG). Since thioredoxin and GSH are important antioxidants, it is not surprising that 6PGDH plays a critical role in protecting cells from oxidative stress. Furthermore the activity of 6PGDH is associated with several human disorders including cancer and Alzheimer's disease. The 3D structural investigation would be very valuable in designing small molecules that target this enzyme for potential therapeutic applications. |
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