## Abstract The specific activities (and activity per organism) of Lβlactate dehydrogenase (LDH) and glycerolβ3βphosphate dehydrogenase (G3PDH) were determined for developmental stages of the mosquito __Anopheles albimanus__. The G3PDH specific activity is initially quite low, then undergoes a 5βfo
Heterologous expression of Zygosaccharomyces rouxii glycerol 3-phosphate dehydrogenase gene (ZrGPD1) and glycerol dehydrogenase gene (ZrGCY1) in Saccharomyces cerevisiae
β Scribed by Yasuo Watanabe; Syoko Tsuchimoto; Youichi Tamai
- Publisher
- John Wiley and Sons
- Year
- 2004
- Tongue
- English
- Weight
- 377 KB
- Volume
- 4
- Category
- Article
- ISSN
- 1567-1356
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β¦ Synopsis
We examined the effects of heterologous expression of the open reading frames (ORF) of two genes on salt tolerance and glycerol production in a Saccharomyces cerevisiae strain deficient in glycerol synthesis (gpd1vgpd2v). When the ORF of the Zygosaccharomyces rouxii glycerol 3-phosphate dehydrogenase gene (ZrGPD1) was expressed under the control of the GAL10 promoter, salt tolerance and glycerol production increased; when the ORF of the glycerol dehydrogenase gene (ZrGCY1) was expressed under the control of the GAL1 promoter, no such changes were observed. Zrgcy1p had a weak effect on glycerol production. These results suggest that Zrgpd1p is the primary enzyme involved in Z. rouxii glycerol production, following a mechanism similar to that of S. cerevisiae (Gpd1p). When the ORFs of the S. cerevisiae glycerol 3-phosphatase gene (GPP2) and ZrGPD1 were simultaneously expressed, glycerol production increased, compared with that in yeast expressing only ZrGPD1.
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## Glycerol phosphate dehydrogenase (GPDH) is a metabolic enzyme that catalyzes the conversion of dihy droxyacetone phosphate to glycerol-3-phosphate. It provides phospholipid precursors for lipid biosynthesis and energy metabolism. In the brain, GPDH enzymatic activity, protein, mRNA are exclusiv
Increases in the mRNA levels of two neuroglial markers, glutamine synthetase (EC 6.3.1.2; GS) and glycerolphosphate dehydrogenase (EC 1.1.1.8; GPDH), were observed in hydrocortisone-treated cultures of astrocytes and oligodendrocytes, respectively, and in C6 cells by Northern blot analysis and in si