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Mazi, Vasiliki E.; Cosmidis, Nikos; Loukas, M.; Clonis, Yannis D.; Ζούρος, Ε.

doi:10.1023/a:1018733110240

Biochemical Genetics

1998

DOI: 10.1023/a:1018733110240

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Vasiliki E. Mazi¹,

Nikos Cosmidis²,

M. Loukas³

et al.

Abstract: Purified alcohol dehydrogenases from olive fruit flies of genotypes SS, II, and SI were biochemically compared. The enzymes were found to differ in the specific activity, in the influence of pH and temperature on activity, and in the affinity with different substrate-alcohols. The probable relationships of these findings with the dramatic changes in allele frequencies observed when natural populations are introduced in the laboratory are discussed.

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Cited by 7 publications

(1 citation statement)

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“…A number of short-chain ADH genes have been cloned and characterized from a variety of fruit-fly species, such as Drosophila melanogaster (Benach et al , 1999), Drosophila lebanonensis (Benach et al , 1999), Ceratitis capitata (Mediterranean fruit flies) (Gasperi et al , 1994) and Bactrocera (Dacus) oleae (olive fly) (Mazi et al , 1998). Whereas short-chain ADHs from Drosophila and certain closely related insects use small alcohols as substrates, all the other known members of this group are mostly steroid and prostaglandin dehydrogenases of both prokaryotic and mammalian origin (Benach et al , 2005).…”

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Cloning, expression and characterization of alcohol dehydrogenases in the silkworm Bombyx mori

et al. 2011

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Alcohol dehydrogenases (ADH) are a class of enzymes that catalyze the reversible oxidation of alcohols to corresponding aldehydes or ketones, by using either nicotinamide adenine dinucleotide (NAD) or nicotinamide adenine dinucleotide phosphate (NADP), as coenzymes. In this study, a short-chain ADH gene was identified in Bombyx mori by 5′-RACE PCR. This is the first time the coding region of BmADH has been cloned, expressed, purified and then characterized. The cDNA fragment encoding the BmADH protein was amplified from a pool of silkworm cDNAs by PCR, and then cloned into E. coli expression vector pET-30a(+). The recombinant His-tagged BmADH protein was expressed in E. coli BL21 (DE3), and then purified by metal chelating affinity chromatography. The soluble recombinant BmADH, produced at low-growth temperature, was instrumental in catalyzing the ethanol-dependent reduction of NAD+, thereby indicating ethanol as one of the substrates of BmADH.

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Cloning, expression and characterization of alcohol dehydrogenases in the silkworm Bombyx mori

et al. 2011

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Characterization of Two Alcohol Dehydrogenase (Adh) Loci from the Olive Fruit Fly, Bactrocera (Dacus) oleae and Implications for Adh Duplication in Dipteran Insects

et al. 2001

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We report the cloning and structural characterization of two Adh loci of the olive fruit fly, Bactrocera oleae. Each of the two genes, named Adh1 and Adh2, consists of three exons and two introns for a total length of 1981 and 988 nucleotides, respectively. Their deduced amino acid sequences of 257 and 258 residues exhibit a 77% identity and display the characteristics of the insect ADH enzymes, which belong to the short-chain dehydrogenases/reductases family. The Adh genes of B. oleae are compared to the two genes of the Mediterranean fly, Ceratitis capitata, the only other species of the Tephritidae family in which the Adh genes have been studied. On the basis of amino acid divergence the four genes form two clusters each containing one gene from each species, as expected if there was one duplication event before speciation. On the basis of nucleotide sequence the four sequences form two clusters each containing the two sequences from the same species, as expected if there was a separate duplication event in each species. To help decide between the two alternatives, we compared at both the amino acid and DNA level the Adh genes of five Drosophila species that are known to carry two such genes and observed that, with only one exception at the amino acid level, conspecific loci cluster together. We conclude that the information we have at present does not allow a firm choice between the hypothesis of a single duplication event that occurred before the split of Bactrocera and Ceratitis from their common ancestor and the hypothesis of two independent duplication events, one in each of the two genera.

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The dual function of ovo/shavenbaby in germline and epidermis differentiation is conserved between Drosophila melanogaster and the olive fruit fly Bactrocera oleae

Khila¹,

Haidani²,

Víncent³

et al. 2003

Insect Biochemistry and Molecular Biology

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Cited by 7 publications

References 25 publications

Cloning, expression and characterization of alcohol dehydrogenases in the silkworm Bombyx mori

Cloning, expression and characterization of alcohol dehydrogenases in the silkworm Bombyx mori

Characterization of Two Alcohol Dehydrogenase (Adh) Loci from the Olive Fruit Fly, Bactrocera (Dacus) oleae and Implications for Adh Duplication in Dipteran Insects

The dual function of ovo/shavenbaby in germline and epidermis differentiation is conserved between Drosophila melanogaster and the olive fruit fly Bactrocera oleae

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