Open AccessATP N‐glycosidase – a novel ATP‐converting activity from a marine sponge Axinella polypoides
Author(s) -
Reintamm Tõnu,
Lopp Annika,
Kuusksalu Anne,
Pehk Tõnis,
Kelve Merike
Publication year - 2003
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1046/j.1432-1033.2003.03805.x
Subject(s) - sponge , enzyme , glycoside hydrolase , biochemistry , adenosine triphosphate , adenosine , chemistry , biology , stereochemistry , botany
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 µmol 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 ( K m , K ip , 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.