Acetaldehyde oxidation in Drosophila melanogaster and Drosophila simulans: Evidence for the presence of an NAD+-dependent dehydrogenase

Garcin, Françoise; Côté, Johanne; Radouco-Thomas, Simone; Kasienczuk, Denis; Chawla, S. S.; Radouco-Thomas, C

doi:10.1016/0305-0491(83)90314-0

Cited by 9 publications

(5 citation statements)

References 28 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The role of ALDH in D. melanogaster larvae was controversial until recently (Garcin et al, 1983(Garcin et al, , 1985Heinstra et al, 1989). Inhibitor studies have shown that ADH catalyzes both the conversion of ethanol to acetaldehyde and the oxidation of acetaldehyde into acetate in D. melanogaster larvae (Geer et al, 1985;Heinstra et al, 1983;Moxon et al, 1985).…”

Section: The Metabolic Fate Of Ethanolmentioning

confidence: 99%

The biological basis of ethanol tolerance in Drosophila

Geer

Heinstra

McKechnie

1993

Comparative Biochemistry and Physiology Part B: Comparative Bio

View full text Add to dashboard Cite

Section: The Metabolic Fate Of Ethanolmentioning

confidence: 99%

The biological basis of ethanol tolerance in Drosophila

Geer

Heinstra

McKechnie

1993

Comparative Biochemistry and Physiology Part B: Comparative Bio

View full text Add to dashboard Cite

“…The probable in situ distribution of alcohol elimination in larvae is about 60% in the fat body and 30% in the alimentary tract (Heinstra et al, 1989;Fibia, Enjuanes & Gonzfilez, 1989;Anderson, Brown & McDonald, 1991). It appears that the ADH enzyme is involved in the in vivo conversion of acetaldehyde into acetate in larvae, whereas the aldehyde dehydrogenase (ALDH, EC 1.2.1.3) enzyme is mainly responsible for this conversion in adults (Heinstra et al, 1983(Heinstra et al, , 1989Eisses et al, 1985;Geer, Langevin & McKechnie, 1985;Geer, Miller & Heinstra, 1991;Moxon et al, 1985;Garcin et al, 1983Garcin et al, , 1985Eisses, 1989;Anderson & Barnett, 1991;Leal & Barbancho, 1992Miller, Heinstra & Geer, 1992). The biotransformation of the highly toxic compound acetaldehyde has been extensively studied and debated (e.g., David et al, 1978;Deltombe-Lietaert et al, 1979;Gelfand & McDonald, 1980;David, 1988).…”

Section: Metabolic-physiology Of Alcohol Degradationmentioning

confidence: 99%

Evolutionary genetics of the Drosophila alcohol dehydrogenase gene-enzyme system

Heinstra

1993

Genetica

View full text Add to dashboard Cite

Evolutionary genetics embodies a broad research area that ranges from the DNA level to studies of genetic aspects in populations. In all cases the purpose is to determine the impact of genetic variation on evolutionary change. The broad range of evolutionary genetics requires the involvement of a diverse group of researchers: molecular biologists, (population) geneticists, biochemists, physiologists, ecologists, ethologists and theorists, each of which has its own insights and interests. For example, biochemists are often not concerned with the physiological function of a protein (with respect to pH, substrates, temperature, etc.), while ecologists, in turn, are often not interested in the biochemical-physiological aspects underlying the traits they study. This review deals with several evolutionary aspects of the Drosophila alcohol dehydrogenase gene-enzyme system, and includes my own personal viewpoints. I have tried to condense and integrate the current knowledge in this field as it has developed since the comprehensive review by van Delden (1982). Details on specific issues may be gained from Sofer and Martin (1987), Sullivan, Atkinson and Starmer (1990); Chambers (1988, 1991); Geer, Miller and Heinstra (1991); and Winberg and McKinley-McKee (1992).

show abstract

“…However, there are two viewpoints with respect to the second step of the ethanol degradation pathway in D. melanogaster. According to one viewpoint, this reaction is catalysed by an ALDH enzyme (Lietaert et al, 1982;Garcin et al, 1983Garcin et al, , 1985David et al, 1984), whereas it has also been postulated that Drosophila ADH has dual catalytic properties and can oxidize acetaldehyde as well as ethanol (Heinstra et al, 1983;Eisses et al, 1985;Geer et al, 1985;Moxom et al, 1985). Unlike the mammalian ADH, the ADH of Drosophila is not a metalloenzyme, and it differs significantly in size and amino acid sequence (Jornvall et al, 1981(Jornvall et al, , 1984); consequently, the diverse properties of the ADHs are not surprising.…”

Section: Introductionmentioning

confidence: 99%

The 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

Heinstra

Geer

Seykens

et al. 1989

Biochemical Journal

View full text Add to dashboard Cite

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 tracer studies in vivo, more than 75% of the acetaldehyde converted to acetate by the ADH ethanol-degrading pathway appeared to be also catalysed by the ADH enzyme. The larval fat body probably was the major site of this pathway.

show abstract

Acetaldehyde oxidation in Drosophila melanogaster and Drosophila simulans: Evidence for the presence of an NAD+-dependent dehydrogenase

Cited by 9 publications

References 28 publications

The biological basis of ethanol tolerance in Drosophila

The biological basis of ethanol tolerance in Drosophila

Evolutionary genetics of the Drosophila alcohol dehydrogenase gene-enzyme system

The 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

Contact Info

Product

Resources

About