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Subcellular origin of the surface fluorescence of reduced nicotinamide nucleotides in the isolated perfused rat heart.

Surface fluorometric measurements and indicator metabolite determinations in the isolated perfused rat heart showed that the NADH + NADPH fluorescence of the intact tissue originates largely from the mitochondria. The redox potential of the lactate dehydrogenase system calculated from the endogenous lactate/pyruvate ratios was closely similar to that of the glycerol-3-phosphate dehydrogenase system calculated from the concentrations of glycerol-3-phosphate and dihydroxyacetone phosphate in the tissue. Thus, in contrast to the liver, the cytosolic redox state of the NADH/NAD+ system in isolated perfused heart oxidizing external glucose or fatty acid is not amenable to optical monitoring, but can be assessed from the state of the lactate dehydrogenase or glycerol-3-phosphate dehydrogenase systems.

Animals↗
PubMed1986

sn-Glycerol-3-phosphate oxidase and alcohol tolerance in Drosophila melanogaster larvae.

The role of sn-glycerol-3-phosphate oxidase (GPO; EC 1.1.99.5) in the variation of ethanol tolerance in Drosophila melanogaster was assessed in isofemale lines derived from individuals collected at the Chateau Tahbilk Winery and Wandin North Orchard of Victoria, Australia. When fed an undefined medium (semolina-treacle) with 6% ethanol (v/v), larvae of lines with high GPO activities survived better than did larvae of lines with low GPO activities. 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. This implied that the cellar environment selected against individuals with high levels of GPO. These data do not explain the established difference in tolerance between cellar and outside populations. The GPO activities of lines were not dependent upon the activities of the lipogenic enzyme, glycerol-3-phosphate dehydrogenase; the major ethanol-degrading enzyme, alcohol dehydrogenase; or the citric acid cycle enzyme, fumarase. Thus, GPO activity is an important component of the metabolic mechanism of ethanol tolerance in larvae, but the mode of action of GPO has not been defined.

Alcohol Dehydrogenase↗
PubMed2001

Shared nucleotide composition biases among species and their impact on phylogenetic reconstructions of the Drosophilidae.

Compositional changes are a major feature of genome evolution. Overlooking nucleotide composition differences among sequences can seriously mislead phylogenetic reconstructions. Large compositional variation exists among the members of the family Drosophilidae. Until now, however, base composition differences have been largely neglected in the formulations of the nucleotide substitution process used to reconstruct the phylogeny of this important group of species. The present study adopts a maximum-likelihood framework of phylogenetic inference in order to analyze five nuclear gene regions and shows that (1) the pattern of compositional variation in the Drosophilidae does not match the phylogeny of the species; (2) accounting for the heterogeneous GC content with Galtier and Gouy's nucleotide substitution model leads to a tree that differs in significant aspects from the tree inferred when the nucleotide composition differences are ignored, even though both phylogenetic hypotheses attain strong nodal support in the bootstrap analyses; and (3) the LogDet distance correction cannot completely overcome the distorting effects of the compositional variation that exists among the species of the Drosophilidae. Our analyses confidently place the Chymomyza genus as an outgroup closer than the genus Scaptodrosophila to the Drosophila genus and conclusively support the monophyly of the Sophophora subgenus.

Alcohol Dehydrogenase↗
PubMed1991

Glycerol catabolism in Aspergillus nidulans.

Glycerol is catabolized in Aspergillus nidulans by glycerol kinase and a mitochondrial FAD-dependent sn-glycerol 3-phosphate dehydrogenase. The levels of both enzymes are controlled by carbon catabolite repression and by specific induction. Biochemical and genetical analyses show that dihydroxyacetone and D-glyceraldehyde are converted into glycerol and then catabolized by the same pathway. D-Glyceraldehyde can be reduced by NADP(+)-dependent glycerol dehydrogenase or by alcohol dehydrogenase I, while dihydroxyacetone is only reduced by the first enzyme. Three new glycerol non-utilizing mutants have been found. These three mutations define three hitherto unknown loci, glcE, glcF and glcG. The mutation in glcG leads to a greatly decreased sn-glycerol-3-phosphate dehydrogenase activity.

Alcohol Dehydrogenase↗