Determination of some biochemical and structural features of alcohol dehydrogenases from Drosophila simulans and Drosophila virilis. Comparison of their properties with the Drosophila melanogaster Adhs enzyme

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Abstract
The biochemical properties of the enzyme alcohol dehydrogenase of 2 Drosophila spp., D. simulans and D. virilis, were studied and compared with those of D. melanogaster Adhs enzyme. All of them consist of 2 identical subunits of MW 27,800 and share significant similarities in function. The substrate specificities of these enzymes were characterized, and Km(app.) and Vmax.(app) values were calculated. All these alcohol dehydrogenases show greater affinity for secondary rather than for primary alcohols. The amino acid compositions of the 3 enzymes were determined, and there is a close similarity between the D. simulans and the D. melanogaster enzymes, but there are significant differences from the alcohol dehydrogenase of D. virilis. The N-terminal amino acid is blocked and the C-terminal amino acid is the same for all 3 alcohol dehydrogenases. The enzymes from the 3 spp. were carboxymethylated and digested with trypsin. The peptide maps reveal more homologies between the enzymes of D. simulans and D. melanogaster than with the enzyme of D. virilis.