3.6.1.5 a ribonucleoside 5'-triphosphate + H2O - 3.6.1.5 ADP + 2 H2O - 3.6.1.5 ADP + H2O - 3.6.1.5 ADP + H2O very low activity 3.6.1.5 ADP + H2O hydrolysis of extracellular ADP 3.6.1.5 ADP + H2O 68% activity compared to ATP 3.6.1.5 AMP + H2O - 3.6.1.5 AMP + H2O hydrolysis of extracellular AMP, low activity 3.6.1.5 ATP + 2 H2O - 3.6.1.5 ATP + 2 H2O 100% activity 3.6.1.5 ATP + 2 H2O inhibition of platelet aggregation in the placenta 3.6.1.5 ATP + 2 H2O salvage of purine nucleobases in primary urine 3.6.1.5 ATP + 2 H2O regulation of extracellular ATP-level 3.6.1.5 ATP + 2 H2O inhibition of platelet aggregation 3.6.1.5 ATP + 2 H2O overall reaction 3.6.1.5 ATP + 2 H2O dissipation of ATP by CD39 reduces P2X7 receptor stimulation and thereby suppresses baseline leukocyte alphaMbeta2-integrin expression. As alphaMbeta2-integrin blockade reverses the postischemic, inflammatory phenotype of Cd39-/- mice. Phosphohydrolytic activity on the leukocyte surface suppresses cell-cell interactions that would otherwise promote thrombosis or inflammation 3.6.1.5 ATP + 2 H2O best substrate in hepatic stellate cells 3.6.1.5 ATP + 2 H2O CG5276 functions as apyrase converting extracellular ATP to ADP and AMP 3.6.1.5 ATP + 2 H2O ATP is hydrolyzed by NTPDase1 via ADP to AMP, without significant release of ADP 3.6.1.5 ATP + H2O - 3.6.1.5 ATP + H2O hydrolysis of extracellular ATP 3.6.1.5 ATP + H2O ATP incubated with NTPDase2 is readily converted into ADP, but very poorly into AMP 3.6.1.5 CDP + H2O - 3.6.1.5 CTP + 2 H2O - 3.6.1.5 CTP + H2O - 3.6.1.5 GDP + H2O - 3.6.1.5 GTP + 2 H2O - 3.6.1.5 GTP + H2O - 3.6.1.5 additional information enzyme abrogates platelet aggregation and recruitment in intact vessels 3.6.1.5 additional information enzyme terminates P2 receptor-mediated signal transmission 3.6.1.5 additional information enzyme inhibits ADP-, collagen-, and thrombin-induced human platelet aggregation in dose-dependent manner 3.6.1.5 additional information enzyme inhibits ADP-induced human platelet aggregation 3.6.1.5 additional information enzyme is involved in regulating ATP signaling associated primarily with auditory neurotransmission 3.6.1.5 additional information apyrase, an ecto-enzyme with ADPase and ATPase activities, rapidly metabolizes ADP and ATP released from platelets and endothelial cells, thereby reducing platelet activation and recruitment. The recombinant apyrase inhibits ADP-, collagen- and thrombin-induced human platelet aggregation, overview 3.6.1.5 additional information ATPDase2 plays a non-redundant role in the parasite-host interplay 3.6.1.5 additional information the enzyme acts in a multienzyme complex transforming ATP into adenosine without accumulation of intermediates 3.6.1.5 additional information the enzyme plays a role in the salvage of purines from the extracellular medium in the organism 3.6.1.5 additional information apyrases are non-energy-coupled nucleotide phosphohydrolases that hydrolyze nucleoside triphosphates and nucleoside diphosphates to nucleoside monophosphates and orthophosphates, critical role for the GS52 ecto-apyrase during nodulation 3.6.1.5 additional information apyrases hydrolyze nucleoside triphosphates and diphosphates 3.6.1.5 additional information CD39 can regulate platelet activation from either the endothelial or leukocyte compartment. CD39 on monocytes and neutrophils regulates their own sequestration into ischemic cerebral tissue, by catabolizing nucleotides released by injured cells, thereby inhibiting their chemotaxis, adhesion, and transmigration. Leukocyte ectoapyrases modulate the ambient vascular nucleotide milieu. Dissipation of ATP by CD39 reduces P2X7 receptor stimulation and thereby suppresses baseline leukocyte alphaMbeta2-integrin expression. As alphaMbeta2-integrin blockade reverses the postischemic, inflammatory phenotype of Cd39-/- mice 3.6.1.5 additional information Ecto-NTPDase1 is required in the infection process of trypanosomes into mammalian cells, overview. Ecto-NTPDase act as facilitators of infection and virulence in vitro and in vivo 3.6.1.5 additional information Lpg1905 is essentially required for intracellular replication of Legionella pneumophila in eukaryotic cells leading to the Legionnaires disease, a severe and potentially fatal form of pneumonia 3.6.1.5 additional information salivary apyrases are nucleotide-metabolising enzymes that blood-feeding parasites utilise for modulation of extracellular nucleotides to prevent platelet activation and aggregation 3.6.1.5 additional information apyrases hydrolyze the phosphodiester bonds of nucleoside tri- and diphosphates to orthophosphate and mononucleodides 3.6.1.5 additional information substrate specificity in myofibroblasts and quiescent-like hepatic stellate cells, overview 3.6.1.5 additional information Ruviapyrase does not show cytotoxicity against breast cancer (MCF-7) cells and haemolytic activity, it exhibits marginal anticoagulant and strong antiplatelet activity, and dose-dependently reverses the ADP-induced platelet aggregation. The catalytic activity and platelet deaggregation property of Ruviapyrase is significantly inhibited by EDTA, DTT and IAA, and neutralized by commercial monovalent and polyvalent antivenom 3.6.1.5 TTP + 2 H2O - 3.6.1.5 UDP + 2 H2O - 3.6.1.5 UDP + H2O - 3.6.1.5 UDP + H2O best substrate in myofibroblasts 3.6.1.5 UDP + H2O very low activity with UDP 3.6.1.5 UTP + 2 H2O - 3.6.1.5 UTP + H2O -