The alcohol dehydrogenase polymorphism of Drosophila melanogaster in relation to environmental ethanol, ethanol tolerance and alcohol dehydrogenase activity
نویسندگان
چکیده
منابع مشابه
Molecular control of the induction of alcohol dehydrogenase by ethanol in Drosophila melanogaster larvae.
The activity of alcohol dehydrogenase (ADH:EC 1.1.1.1), the initial enzyme in the major pathway for ethanol degradation, is induced in Drosophila melanogaster larvae by low concentrations of dietary ethanol. Two lines of evidence indicate that the metabolic products of the ADH pathway for ethanol degradation are not directly involved in the induction of Adh. First, the accumulation of the proxi...
متن کاملThe metabolism of ethanol-derived acetaldehyde by alcohol dehydrogenase (EC 1.1.1.1) and aldehyde dehydrogenase (EC 1.2.1.3) in Drosophila melanogaster larvae.
Both aldehyde dehydrogenase (ALDH, EC 1.2.1.3) and the aldehyde dehydrogenase activity of alcohol dehydrogenase (ADH, EC 1.1.1.1) were found to coexist in Drosophila melanogaster larvae. The enzymes, however, showed different inhibition patterns with respect to pyrazole, cyanamide and disulphiram. ALDH-1 and ALDH-2 isoenzymes were detected in larvae by electrophoretic methods. Nonetheless, in t...
متن کاملDrosophila melanogaster alcohol dehydrogenase: product-inhibition studies.
The Drosophila melanogaster alleloenzymes AdhS and AdhF have been studied with respect to product inhibition by using the two substrate couples propan-2-ol/acetone and ethanol/acetaldehyde together with the coenzyme couple NAD+/NADH. With both substrate couples the reaction was consistent with an ordered Bi Bi mechanism. The substrates added to the enzyme in a compulsory order, with coenzyme as...
متن کاملElectrophoretic variability at the alcohol dehydrogenase locus in Drosophila melanogaster.
In crder to assess the extent of electrophoretic variation at the alcohol dehydrogenase locus in a natural population of Drosophila melanogmter KREITMAN ( 1980) screened ninety-six isochromosomal lines and two lines carrying “fast’’ thermostability variants of the enzyme using eight different conditions of acrylamide electrophoresis. Although he found no sdditional mobility variation within the...
متن کاملMutant alcohol dehydrogenase leads to improved ethanol tolerance in Clostridium thermocellum.
Clostridium thermocellum is a thermophilic, obligately anaerobic, gram-positive bacterium that is a candidate microorganism for converting cellulosic biomass into ethanol through consolidated bioprocessing. Ethanol intolerance is an important metric in terms of process economics, and tolerance has often been described as a complex and likely multigenic trait for which complex gene interactions ...
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ژورنال
عنوان ژورنال: Heredity
سال: 1988
ISSN: 0018-067X,1365-2540
DOI: 10.1038/hdy.1988.58