Alcohol dehydrogenase of Drosophila melanogaster: metabolic differences mediated through cryptic allozymes
نویسندگان
چکیده
منابع مشابه
Drosophila 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 کاملPost-translational control of alcohol dehydrogenase levels in Drosophila melanogaster.
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...
متن کاملDrosophila melanogaster alcohol dehydrogenase: mechanism of aldehyde oxidation and dismutation.
Drosophila alcohol dehydrogenase (Adh) catalyses the oxidation of both alcohols and aldehydes. In the latter case, the oxidation is followed by a reduction of the aldehyde, i.e. a dismutation reaction. At high pH, dismutation is accompanied by a small release of NADH, which is not observed at neutral pH. Previously it has been emphasized that kinetic coefficients obtained by measuring the incre...
متن کاملEnzyme variation, metabolic flux and fitness: alcohol dehydrogenase in Drosophila melanogaster.
Although there are many in vitro studies of enzyme activity of genetic variants at the Adh locus in D. melanogaster, little is known about the corresponding metabolic activity in living flies. We report here such measurements of the metabolic flux in the conversion of ethanol to the two products, CO2 and lipids, for six different active genotypes, containing the predominant naturally recurring ...
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...
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ژورنال
عنوان ژورنال: Heredity
سال: 1986
ISSN: 0018-067X,1365-2540
DOI: 10.1038/hdy.1986.82