Literature DB >> 3134011

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

J O Winberg1, J S McKinley-McKee.   

Abstract

The NAD+ + acetone-induced isoenzyme conversion of the Drosophila melanogaster AdhS alleloenzyme was studied. Absorption and fluorescence spectra as well as electrophoretic and kinetic methods show that the conversion process proceeds through three steps. Initially a binary enzyme-NAD+ complex is formed, followed by a ternary enzyme-NAD+-acetone complex with a KEO,Ac of 1.7 M. The last step is a rate-limiting irreversible process in which NAD+ and acetone are covalently linked to the enzyme. A Vm of 2.4 min-1 was obtained at pH 8.6.

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Year:  1988        PMID: 3134011      PMCID: PMC1148987          DOI: 10.1042/bj2510223

Source DB:  PubMed          Journal:  Biochem J        ISSN: 0264-6021            Impact factor:   3.857


  35 in total

1.  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

2.  Multiple forms of drosophila alcohol dehydrogenase. 3. Conversion of one form to another by nicotinamide adenine dinucleotide or acetone.

Authors:  K B Jacobson; J B Murphy; J A Knopp; J R Ortiz
Journal:  Arch Biochem Biophys       Date:  1972-03       Impact factor: 4.013

3.  Isoenzymes of Drosophila alcohol dehydrogenase. I. Isolation and interconversion of different forms.

Authors:  K B Jacobson; J B Murphy; F C Hartman
Journal:  J Biol Chem       Date:  1970-03-10       Impact factor: 5.157

4.  Interconversion of isoenzymes of Drosophila alcohol dehydrogenase. II. Physical characterization of the enzyme and its subunits.

Authors:  K B Jacobson; P Pfuderer
Journal:  J Biol Chem       Date:  1970-08-10       Impact factor: 5.157

5.  Structural analysis of an electrophoretically cryptic alcohol dehydrogenase variant from an Australian population of Drosophila melanogaster.

Authors:  G K Chambers; W G Laver; S Campbell; J B Gibson
Journal:  Proc Natl Acad Sci U S A       Date:  1981-05       Impact factor: 11.205

6.  Anion-binding to liver alcohol dehydrogenase, studied by rate of alkylation.

Authors:  C H Reynolds; J S McKinley-McKee
Journal:  Eur J Biochem       Date:  1969-10

7.  Alcohol dehydrogenase of Drosophila: interconversion of isoenzymes.

Authors:  K B Jacobson
Journal:  Science       Date:  1968-01-19       Impact factor: 47.728

8.  Alcohol dehydrogenase from the fruitfly Drosophila melanogaster. Inhibition studies of the alleloenzymes AdhS and AdhUF.

Authors:  J O Winberg; D R Thatcher; J S McKinley-McKee
Journal:  Biochim Biophys Acta       Date:  1982-05-21

9.  Alcohol Dehydrogenase in Drosophila melanogaster: Isozymes and Genetic Variants.

Authors:  E H Grell; K B Jacobson; J B Murphy
Journal:  Science       Date:  1965-07-02       Impact factor: 47.728

10.  An electrophoretically cryptic alcohol dehydrogenase variant in Drosophila melanogaster. I. Activity ratios, thermostability, genetic localization and comparison with two other thermostable variants.

Authors:  J B Gibson; G K Chambers; A V Wilks; J G Oakeshott
Journal:  Aust J Biol Sci       Date:  1980-08
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  3 in total

1.  Evolution of enzymatic activities of testis-specific short-chain dehydrogenase/reductase in Drosophila.

Authors:  Jianming Zhang; Huyuan Yang; Manyuan Long; Liming Li; Antony M Dean
Journal:  J Mol Evol       Date:  2010-08-31       Impact factor: 2.395

2.  Drosophila melanogaster alcohol dehydrogenase: mechanism of aldehyde oxidation and dismutation.

Authors:  J O Winberg; J S McKinley-McKee
Journal:  Biochem J       Date:  1998-02-01       Impact factor: 3.857

3.  Drosophila melanogaster alcohol dehydrogenase: product-inhibition studies.

Authors:  J O Winberg; J S McKinley-McKee
Journal:  Biochem J       Date:  1994-08-01       Impact factor: 3.857

  3 in total

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