Literature DB >> 6803751

An electrophoretically cryptic alcohol dehydrogenase variant in Drosophila melanogaster. III. Biochemical properties and comparison with common enzyme forms.

G K Chambers, A V Wilks, J B Gibson.   

Abstract

The biochemical properties of the heat-stable alcohol dehydrogenase variant ADH-FCh.D. have been investigated and compared with those of the two common enzyme forms ADH-F and ADH-S. The results show that ADH-F and ADH-S differ with respect to substrate specificity, their response to high concentrations of secondary alcohols and their apparent Michaelis constants for three alcohols in two different buffer systems. In all these tests the enzyme ADH-FCh.D. resembles ADH-S much more closely than ADH-F. It is concluded that if natural selection is to distinguish between the alleles AdhS and AdhFCh.D. then it most probably does so on the basis of the superior thermostability of ADH-FCh.D. The biochemical properties of all three enzymes are discussed in relation to the role of alcohol dehydrogenase in the exploitation of alcohol by D. melanogaster.

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Year:  1981        PMID： 6803751     DOI： 10.1071/bi9810625

Source DB:  PubMed          Journal:  Aust J Biol Sci        ISSN： 0004-9417


  9 in total

1.  Genetic variation at the alcohol dehydrogenase locus in Drosophila melanogaster in relation to environmental variation: Ethanol levels in breeding sites and allozyme frequencies.

Authors:  J B Gibson; T W May; A V Wilks
Journal:  Oecologia       Date:  1981-01       Impact factor: 3.225

2.  The alcohol dehydrogenase alleloenzymes AdhS and AdhF from the fruitfly Drosophila melanogaster: an enzymatic rate assay to determine the active-site concentration.

Authors:  J O Winberg; R Hovik; J S McKinley-McKee
Journal:  Biochem Genet       Date:  1985-04       Impact factor: 1.890

3.  Variation in the biochemical properties of the Drosophila alcohol dehydrogenase allozymes.

Authors:  G K Chambers; A V Wilks; J B Gibson
Journal:  Biochem Genet       Date:  1984-02       Impact factor: 1.890

4.  Genetic variation at the alcohol dehydrogenase locus in Drosophila melanogaster: a third ubiquitous allele.

Authors:  J B Gibson; A V Wilks; G K Chambers
Journal:  Experientia       Date:  1982-06-15

5.  Alcohol dehydrogenase thermostability variants in Drosophila melanogaster: comparison of activity ratios and enzyme levels.

Authors:  B Sampsell; E Steward
Journal:  Biochem Genet       Date:  1983-12       Impact factor: 1.890

6.  The purification and biochemical properties of alcohol dehydrogenase--"fast (Chateau Douglas)" from Drosophila melanogaster.

Authors:  G K Chambers
Journal:  Biochem Genet       Date:  1984-06       Impact factor: 1.890

7.  Drosophila melanogaster alcohol dehydrogenase. Biochemical properties of the NAD+-plus-acetone-induced isoenzyme conversion.

Authors:  J O Winberg; J S McKinley-McKee
Journal:  Biochem J       Date:  1988-04-01       Impact factor: 3.857

8.  The AdhS alleloenzyme of alcohol dehydrogenase from Drosophila melanogaster. Variation of kinetic parameters with pH.

Authors:  J O Winberg; J S McKinley-McKee
Journal:  Biochem J       Date:  1988-10-15       Impact factor: 3.857

9.  Biochemical properties of alcohol dehydrogenase from Drosophila lebanonensis.

Authors:  J O Winberg; R Hovik; J S McKinley-McKee; E Juan; R Gonzalez-Duarte
Journal:  Biochem J       Date:  1986-04-15       Impact factor: 3.857
  9 in total

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