Juan E, González-Duarte R
Biochem J. 1981 Apr 1;195(1):61-9. doi: 10.1042/bj1950061.
The biochemical properties of the enzyme alcohol dehydrogenase of two different Drosophila species, Drosophila simulans and Drosophila virilis, were studied and compared with those of Drosophila melanogaster Adhs enzyme. All of them consist of two identical subunits of molecular weight 27800 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 three 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 three alcohol dehydrogenases. The enzymes from the three species were carboxymethylated and digested with trypsin. The peptide 'maps' reveal, as expected, more homologies between the enzymes of D. simulans and D. melanogaster than with the enzyme of D. virilis.
对两种不同果蝇物种——拟暗果蝇（Drosophila simulans）和粗壮果蝇（Drosophila virilis）的乙醇脱氢酶的生化特性进行了研究，并与黑腹果蝇（Drosophila melanogaster）的Adhs酶的生化特性进行了比较。它们均由两个分子量为27800的相同亚基组成，并且在功能上具有显著的相似性。对这些酶的底物特异性进行了表征，并计算了Km（表观）和Vmax（表观）值。所有这些乙醇脱氢酶对仲醇的亲和力比对伯醇的亲和力更高。测定了这三种酶的氨基酸组成，拟暗果蝇和黑腹果蝇的酶之间有密切的相似性，但与粗壮果蝇的乙醇脱氢酶有显著差异。三种乙醇脱氢酶的N端氨基酸均被封闭，C端氨基酸相同。对来自这三个物种的酶进行了羧甲基化处理并用胰蛋白酶消化。肽“图谱”显示，正如预期的那样，拟暗果蝇和黑腹果蝇的酶之间的同源性比与粗壮果蝇的酶之间的同源性更高。
