The α-glycerophosphate cycle inDrosophila melanogaster. I. Biochemical and developmental aspects

@article{OBrien2004TheC,
  title={The $\alpha$-glycerophosphate cycle inDrosophila melanogaster. I. Biochemical and developmental aspects},
  author={Stephen J. O’Brien and Ross J. MacIntyre},
  journal={Biochemical Genetics},
  year={2004},
  volume={7},
  pages={141-161}
}
The two α-glycerophosphate dehydrogenases ofDrosophila melanogaster (mitochondrial αGPO and soluble αGPDH) have been biochemically characterized in a preliminary investigation of the α-glycerophosphate cycle inDrosophila. The soluble enzyme is NAD linked and can be distinguished from the mitochondrial oxidase in terms of locational specificity,pH optimum, salt precipitation, and electrophoretic behavior. The mitochondrial enzyme is NAD independent and exhibits behavior typical of a lipoprotein… 
Origin of α-glycerophosphate dehydrogenase isozymes in Drosophila melanogaster and their functional relationship in the α-glycerophosphate cycle
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Observations suggest that all α-GPDH isozymes are the product of a single structural gene and that the multiple forms of this enzyme arise during successive developmental stages through an epigenetic modification of the primary Gpdh+ polypeptide.
Structural analysis of glycerol-3-phosphate dehydrogenase from severalDrosophila species
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Preliminary protein structural studies of glycerol-3-phosphate dehydrogenase (α-GPDH) from Drosophila spp.
Structural analysis of glycerol-3-phosphate dehydrogenase from severalDrosophila species
TLDR
Preliminary protein structural studies of glycerol-3-phosphate dehydrogenase (α-GPDH) from Drosophila spp.
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The malate dehydrogenases of D. melanogaster have been resolved into a cytoplasmic form (cMDH) and a mitochondrial matrix form (mMDH), and both enzymes exhibit markedly similar properties with respect to catalytic activity, pH optima, pH optimum shift in response to different ionic environments, and molecular weight as determined by sucrose density gradient sedimentation.
Quantitative subunit hybridization of drosophilaα-Glycerophosphate dehydrogenase
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Electrophoretic patterns of reactivatedα-glycerophosphate dehydrogenases which were mixed following inactivation of two species' enzymes, demonstrate that high pH dissociates the enzyme into its constituent subunits and reactivation involves subunit reassociation.
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Developmental regulation of glycerol-3-phosphate dehydrogenase synthesis inDrosophila
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Analysis of GPDH synthesis in the adult segments reveals that this enzyme is synthesized in head, thorax, and abdomen, and indicates that the cell type-specific control of G PDH occurs at several levels.
sn-glycerol-3-phosphate oxidase and alcohol tolerance inDrosophila melanogaster larvae
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Although GPO was induced to higher activity levels by dietary ethanol in larvae of all the test lines, GPO activity was greater in lines representing the area outside the wine cellar, implying that the cellar environment selected against individuals with high levels of GPO.
Adaptation ofDrosophila enzymes to temperature. III. Evolutionary conservatism in mitochondrial enzymes
TLDR
Factors support the view that the function, and probably the structure, of mitochondrial enzymes are better conserved in evolution than those of the corresponding enzymes found in the cytosol.
Thermal stability of α-glycerophosphate dehydrogenase in Drosophila
TLDR
The results of this study show that the thermal stability of enzyme molecules is different in different species, and this holds true also in the species in which the enzymes have been found to be identical by other means.
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