Many studies of alcohol adaptation in Drosophila melanogaster have focused on the Adh polymorphism, yet the metabolic elimination of alcohol should involve many enzymes and pathways. Here we evaluate the effects of glycerol-3-phosphate dehydrogenase (Gpdh) and cytosolic malate dehydrogenase (Mdh1) genotype activity on adult tolerance to ethanol. We have created a set of P-element-excision-deriv...

The mechanism of reduction of p-nitrosophenol (pNSP) catalyzed by horse liver alcohol dehydrogenase (HADH) and human a-alcohol dehydrogenase (a-ADH) has been compared in transient and steady-state experiments. Our results indicate that pNSP reduction catalyzed by these two ADH proceeds by different mechanisms. In one mechanism, shown by Equation 1, pNSP is reduced to p-aminophenol (PAP) via tw...

The distribution of the alcohol dehydrogenase gene (adh) among different Archaea was investigated by Southern blot analysis revealing the potentiality of the adh gene as a specific marker for the genus Sulfolobus. Moreover, the in vivo expression of the adh gene from a new isolate of Sulfolobus solfataricus, G theta, was studied to investigate gene regulation in Archaea. Primer extension analys...

The accumulation of alcohol dehydrogenase (ADH) in arachidonic acid-elicited potato (Solanum tuberosum L.) tuber discs was studied. In accordance with our previous report of the accumulation of Adh mRNA beginning 2 hours after elicitor treatment (DP Matton, CP Constabel, N Brisson [1990] Plant Mol Biol 14: 775-783), immunoprecipitation of ADH from in vivo labeled discs indicated that ADH synthe...

A trans-acting regulatory gene that alters in vivo protein levels of alcohol dehydrogenase (ADH) has been mapped to a region of the third chromosome of Drosophila melanogaster. The gene has been found to affect the in vivo stability of ADH protein. It was not found to alter levels of total protein of two other enzymes assayed. The action of the gene over development and its possible mode of con...

Multiple alcohol dehydrogenases (ADH) were demonstrated in Acinetobacter sp. strain HO1-N. ADH-A and ADH-B were distinguished on the basis of electrophoretic mobility, pyridine nucleotide cofactor requirement, and substrate specificity. ADH-A is a soluble, NAD-linked, inducible ethanol dehydrogenase (EDH) exhibiting an apparent Km for ethanol of 512 microM and a Vmax of 138 nmol/min. An ethanol...

Two ethyl methanesulfonate-induced mutants of the alcohol-dehydrogenase gene in maize have been analyzed. The enzyme subunits produced by the mutants seem to be structurally altered in such a way that the subunit specified by the null allele Adh(1) (0(5657)) does not dimerize with "wild-type" subunits, and that specified by Adh(1) (S(296)) does so only to a limited extent.

The dependence of the flux in the alcohol-degrading pathway on the activity of alcohol dehydrogenase was investigated in Drosophila larvae. Third-instar larvae were supplied with [2-13C]ethanol as a dietary carbon source. Specific carbon enrichments in de novo synthesized fatty acids were determined in vitro by means of 13C nuclear magnetic resonance spectroscopy. Carbon fluxes deduced from the...

Introduction m a n y a c c e p t e d chemical methods for blood alcohol involve the oxidation of alcohol after a separation step1’ 2 and the subsequent determination of the excess of oxidant. On the other hand, enzymatic procedures1-4 are based on the conversion of diphosphopyridine nucleotide (DPN) to its reduced form (DPNH), catalysed by alcohol dehydrogenase (ADH) in the presence of ethyl-al...

Enantioselective production of (S)-2-phenyl-1-propanol is important as in order to be applied industry, a high degree optical purity required. Besides organocatalysts and metal complexes, biocatalysts can used for its synthesis their isolated form or whole-cell biocatalysts, both which have various advantages disadvantages. In this research, Saccharomyces cerevisiae, biocatalyst, recombinant ho...