Structural and Functional Properties of Glycerol-3-Phosphate Dehydrogenase from a Mammalian Hibernator
β Scribed by Marc de la Roche; Shannon N. Tessier; Kenneth B. Storey
- Publisher
- Springer
- Year
- 2011
- Tongue
- English
- Weight
- 912 KB
- Volume
- 31
- Category
- Article
- ISSN
- 1573-4943
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An NAD-dependent glycerol-3-phosphate dehydrogenase (sn-glycerol-3-phosphate:NAD+ oxidoreductase, EC 1.1.1.8) has been isolated and purified from Saccharomyces cerevisiae by affinity and exclusion chromatography. The enzyme was purified 5 1 OO-fold to a specific activity of 158. It has a molecular w
## Abstract The mitochondrial FADβdependent glycerolβ3βphosphate dehydrogenase (FADβGPDH), recently reported in plants, has been detailed in yeast and animal systems. It oxidizes glycerolβ3βphosphate (Gβ3βP) to dihydroxyacetone phosphate (DHAP) on the outer surface of mitochondrial inner membrane.
The half-lives of the enzyme at 50 C were 6 and33 min, respectively, for the BALB/cJ and C57BL/6J strains. Enzyme preparations from the two strains of mice were compared with respect to the following properties and found to be essentially indistinguishable: K m values for dihydroxyacetone phosphate,