The molecular evolution of amylase duplicates genes in D. melanogaster group

Drosophila melanogaster is a species of fly in the family Drosophilidae. The alpha–amylase system of Drosophila is one of the most intensively examined systems of genes in the field of evolutionary research. Alpha–amylase (EC 3.2.1.1, alpha–1,4– glucan–4–glucanohydrolase) is a digestive enzyme. Its role in the digestive process is to break down starch into glucose and maltose to produce energy. There are six major and minor isozymes of amylase that have been recorded in natural populations of D. melanogaster (Inomata & Yamazaki T).1 Amylase activity is repressed by its produce, glucose, and maltose. It is induced by the substrate starch. Population genetic surveys provide information about the molecular characterization of fitness–related genes upon which natural selection acts. Differences in activity levels and the inducibility has been recorded within and between species. This variation is caused because of a mRNA abundance. However, the difference in the catalytic efficiency of an individual izozymer contributes to the recorded differences in activity between and within species. In addition to the differences in inducibility, differences in developmental and organ– specific expression have been recorded Popadić et al.2