Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1930862 | Biochemical and Biophysical Research Communications | 2011 | 5 Pages |
The earthworm enzyme Eisenia fetida Protease-III-1 (EfP-III-1) is known as a trypsin-like protease which is localized in the alimentary canal of the earthworm. Here, we show that EfP-III-1 also acts as a novel deoxyribonuclease. Unlike most DNases, this earthworm enzyme recognizes 5′-phosphate dsDNA (5′P DNA) and degrades it without sequence specificity, but does not recognize 5′OH DNA. As is the case for most DNases, Mg2+ was observed to markedly enhance the DNase activity of EfP-III-1. Whether the earthworm enzyme functioned as a DNase or as a protease depended on the pH values of the enzyme solution. The protein acted as a protease under alkaline conditions whereas it exhibited DNase activity under acid conditions. At pH 7.0, the enzyme could work as either a DNase or a protease. Given the complex living environment of the earthworm, this dual function of EfP-III-1 may play an important role in the alimentary digestion of the earthworm.
► For the first time it was found that Eisenia fetida Protease-III-1could act as a DNase. ► E. fetida Protease-III-1 degraded the DNA with specificity. ► Different pH environments affected the dual functions of E. fetida Protease-III-1.