A number of nucleoside diphosphate and triphosphate hydrolases as well as some
yet uncharacterized proteins have been found to belong to the same family [1,2]. This family currently consist of:
Yeast guanosine-diphosphatase (EC 184.108.40.206) (GDPase) (gene GDA1). GDA1 is
a golgi integral membrane enzyme that catalyzes the hydrolysis of GDP to
Potato apyrase (EC 220.127.116.11) (adenosine diphosphatase) (ADPase). Apyrase
acts on both ATP and ADP to produce AMP.
Mammalian vascular ATP-diphosphohydrolase (EC 18.104.22.168) (also known as
lymphoid cell activation antigen CD39).
Toxoplasma gondii nucleoside-triphosphatases (EC 22.214.171.124) (NTPase). NTPase
hydrolyses various nucleoside triphosphates to produce the corresponding
nucleoside mono- and diphosphates. This enzyme is secreted into the
invaded host cell into the parasitophorous vacuole, a specialized
compartment where the parasite intracellulary resides.
Pea nucleoside-triphosphatases (EC 126.96.36.199) (NTPase).
Caenorhabditis elegans hypothetical protein C33H5.14.
Caenorhabditis elegans hypothetical protein R07E4.4.
Yeast chromosome V hypothetical protein YER005w.
The above uncharacterized proteins all seem to be membrane-bound.
All these proteins share a number of conserved domains. We have selected the
best conserved of these domains. It is located in the central section of the
December 2004 / Pattern and text revised.
PROSITE method (with tools and information) covered by this documentation:
Handa M., Guidotti G.
Purification and cloning of a soluble ATP-diphosphohydrolase (apyrase) from potato tubers (Solanum tuberosum).
Vasconcelos E.G., Ferreira S.T., de Carvalho T.M.U., de Souza W., Kettlun A.M., Mancilla M., Valenzuela M.A., Verjovski-Almeida S.
Partial purification and immunohistochemical localization of ATP diphosphohydrolase from Schistosoma mansoni. Immunological cross-reactivities with potato apyrase and Toxoplasma gondii nucleoside triphosphate hydrolase.
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