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PubMed2002

Decreasing acetic acid accumulation by a glycerol overproducing strain of Saccharomyces cerevisiae by deleting the ALD6 aldehyde dehydrogenase gene.

Glycerol is a major fermentation product of Saccharomyces cerevisiae that contributes to the sensory character of wine. Diverting sugar to glycerol overproduction and away from ethanol production by overexpressing the glycerol 3-phosphate dehydrogenase gene,GPD2, caused S. cerevisiae to produce more than twice as much acetic acid as the wild-type strain (S288C background) in anaerobic cell culture. Deletion of the aldehyde dehydrogenase gene, ALD6, in wild-type and GPD2 overexpressing strains (GPD2-OP) decreased acetic acid production by three- and four-fold, respectively. In conjunction with reduced acetic acid production, the GPD2-OP ald6Delta strain produced more glycerol and less ethanol than the wild-type. The growth rate and fermentation rate were similar for the modified and wild-type strains, although the fermentation rate for the GPD2 ald6Delta strain was slightly less than that of the other strains from 24h onwards. Analysis of the metabolome of the mutants revealed that genetic modification affected the production of some secondary metabolites of fermentation, including acids, esters, aldehydes and higher alcohols, many of which are flavour-active in wine. Modification of GPD2 and ALD6 expression represents an effective strategy to increase the glycerol and decrease the ethanol concentration during fermentation, and alters the chemical composition of the medium such that, potentially, novel flavour diversity is possible. The implications for the use of these modifications in commercial wine production require further investigation in wine yeast strains.

Acetic Acid↗
PubMed1988

Association of allozyme heterozygosity and sternopleural chaetae number in Drosophila melanogaster.

Variation at two polymorphic allozyme loci (Adh and alpha Gpdh) has been assayed in relation to sternopleural chaetae number in flies derived from a cage population of D. melanogaster known to be under stabilising selection with respect to chaetae number. Central phenotypes were significantly more heterozygous at these loci than more extreme phenotypes. Analysis of the base population and of divergent directional selection lines derived from it suggested that alleles at Adh and alpha Gpdh have a pleiotropic effect on chaetae number or are in strong linkage disequilibrium with chaetae factors. In addition, homozygotes at Adh and alpha Gpdh were observed to have a higher variance in chaetae number than heterozygotes. It is concluded that additive and homeostatic models of gene action might both partly explain the higher heterozygosity of central phenotypes.

Alcohol Dehydrogenase↗
PubMed1998

Detection of individual variation in enzyme activity in natural populations of Drosophila melanogaster.

The method allows the determination of the activity level of enzymes in a single fly and assessing the genetic composition of the given individual at these enzyme loci. Three isofemale lines were constructed which were monomorphic at several enzyme loci. Samples were prepared in two different ways: (i) individual samples--individuals were homogenised separately; (ii) collective samples--a common homogenate was prepared from several individuals. Oregon-R strain was also used to prepare a standard homogenate. The activities of alcohol dehydrogenase (ADH), alpha-glycerophosphate dehydrogenase (alpha GPDH), isocitrate dehydrogenase (IDH), and 6-phosphogluconate dehydrogenase (6PGDH), were measured in each sample on starch gel after the proteins were separated by electrophoresis. Enzyme activities were assessed by the optical density of the bands. Gel and position weights were estimated on the basis of the statistical analyses of the activities measured in the standard samples. Gel weights were then used to account for the activity differences among the gels while position weights were applied to correct for the general tendencies in the activities observed within the gels. The gel and position weighted activities of individual and collective samples were compared in the isofemale lines. The individual samples had approximately two times as much variation as the collective samples for all four enzymes. The electrophoretic method is sensitive enough to study the structure of the phenotypic variation in enzyme activity in the natural populations. The total variation among the standard samples was close to the within subline component of variation obtained for the collective samples (measurement error). This shows that the standard samples can be used to estimate the size of the measurement error.

Alcohol Dehydrogenase↗
PubMed1984

Enhancement of aldehyde dehydrogenase activity in rat liver by clofibrate feeding.

Treatment over a 3-week period of male rats with the hypolipidemic drug clofibrate results in a more than twofold increase of aldehyde dehydrogenase activity in liver homogenate and mitochondrial fraction. As a comparable rise is also found in the postmitochondrial fraction, it is suggested that not only the mitochondrial but also the microsomal moiety of aldehyde dehydrogenase is induced by clofibrate. Possibly the known enhancement of ethanol catabolism and some protective effect on the liver of clofibrate-treated animals is due, at least in part, to the increased acetaldehyde oxidation by liver aldehyde dehydrogenase.

Aldehyde Dehydrogenase↗
PubMed1982

Activities of muscle energy supplying enzymes after 5 days complete fasting in young men.

The effect of 5 days' complete fasting on the activity of 7 enzymes of energy supplying metabolism was studied in the vastus lateralis muscles of 9 healthy male volunteers. There was a significant decrease of lactate dehydrogenase (by 66%), triosephosphate dehydrogenase (by 61%), malate:NAD dehydrogenase (by 48%), hexokinase (by 40%), 3-hydroxyacyl-CoA-dehydrogenase (by 40%), triosephosphate dehydrogenase/3-hydroxyacyl-CoA-dehydrogenase (by 35%), citrate synthase (by 33%). Glycerolphosphate:NAD dehydrogenase activity did not decrease significantly. These findings suggest a) that utilization of the major energy substrates decreases; b) that the decrease mainly concerns the catabolism of carbohydrates, that of fatty acids to a lesser extent; c) that the decreased capacity of carbohydrate catabolism is partly compensated for by the predominance of the more economic aerobic-oxidative pathway; d) that the reducing equivalents formed in the cytosol may be transported via the glycerolphosphate shuttle into the respiratory chain to a greater extent, so that a greater portion is not lost by the reduction of pyruvate to lactate.

Adult↗
PubMed1999

Phylogeny of Drosophila and related genera: conflict between molecular and anatomical analyses.

Drosophila species are extensively used in biological research; yet, important phylogenetic relationships within the genus and with related genera remain unresolved. The combined data for three genes (Adh, Sod, and Gpdh) statistically resolves outstanding issues. We define the genus Drosophila inclusively so as to include Scaptomyza and Zaprionus (considered distinct genera in the taxonomy of Wheeler, 1981) but excluding Scaptodrosophila. The genus Drosophila so defined is monophyletic. The subgenus Sophophora (including the melanogaster, obscura, and willistoni groups) is monophyletic and the sister clade to all other Drosophila subgenera. The Hawaiian Drosophila (including Scaptomyza) is a monophyletic group, but the subgenus Drosophila is not monophyletic, because the immigrans group is more closely related to the subgenus Hirtodrosophila than to other species of the subgenus Drosophila, such as the virilis and repleta groups.

Alcohol Dehydrogenase↗