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Updated: Aug 30, 2026

Measuring In Vitro ATPase Activity for Enzymatic Characterization
Published on: August 23, 2016
ATP N-glycosidase - a novel ATP-converting activity from a marine sponge Axinella polypoides
Tõnu Reintamm1, Annika Lopp, Anne Kuusksalu
1Laboratory of Molecular Genetics, National Institute of Chemical Physics and Biophysics, Tallinn, Estonia.
Abstract:
A novel nucleosidase enzymatic activity was discovered in the marine sponge Axinella polypoides. This enzyme, designated as ATP N-glycosidase, converts adenosine-5'-triphosphate into adenine and ribose-5-triphosphate. The crude extract of A. polypoides was capable of hydrolysing 25 micro mol ATP.min-1 per g wet weight of sponge. The catalytic activity of a sponge crude extract per mg total protein is comparable with specific activities of purified plant adenosine and bacterial AMP nucleosidases. The preferred substrate for the novel enzyme is ATP but any compound containing adenosine-5'-diphosphoryl fragment is also cleaved. The biochemical properties (Km, Kip, environmental requirements) of ATP N-glycosidase show similarities with previously described adenine-specific nucleosidases; however, the pattern of its biochemical characteristics does not match with that of any of those enzymes.
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