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ADP + H2O
AMP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
GDP + H2O
GMP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
UDP + H2O
UMP + phosphate
-
-
-
?
UTP + H2O
UDP + phosphate
-
-
-
?
a ribonucleoside 5'-triphosphate + H2O
a ribonucleoside 5'-phosphate + 2 phosphate + 2 H+
-
-
-
?
ADP + H2O
AMP + phosphate
ATP + 2 H2O
AMP + 2 phosphate
CDP + H2O
CMP + phosphate
-
-
-
-
?
CTP + 2 H2O
CMP + 2 phosphate
-
-
-
-
?
GTP + 2 H2O
GMP + 2 phosphate
-
-
-
-
?
UDP + H2O
UMP + phosphate
UTP + 2 H2O
UMP + 2 phosphate
additional information
?
-
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
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
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
best substrate in hepatic stellate cells
-
-
?
UDP + H2O
UMP + phosphate
-
-
-
-
?
UDP + H2O
UMP + phosphate
-
-
-
?
UDP + H2O
UMP + phosphate
-
-
-
?
UDP + H2O
UMP + phosphate
-
best substrate in myofibroblasts
-
-
?
UTP + 2 H2O
UMP + 2 phosphate
-
-
-
-
?
UTP + 2 H2O
UMP + 2 phosphate
-
-
-
?
UTP + 2 H2O
UMP + 2 phosphate
-
-
-
?
additional information
?
-
adenine nucleotides are the best substrates. The other nucleotides (GTP, UTP, GDP, and UDP) are also hydrolyzed when added to the reaction instead of ATP or ADP, which demonstrates a broad substrate specificity for E-NTPDase expressed on the surface of peritoneal cavity cells
-
-
-
additional information
?
-
-
adenine nucleotides are the best substrates. The other nucleotides (GTP, UTP, GDP, and UDP) are also hydrolyzed when added to the reaction instead of ATP or ADP, which demonstrates a broad substrate specificity for E-NTPDase expressed on the surface of peritoneal cavity cells
-
-
-
additional information
?
-
no substrate: AMP
-
-
?
additional information
?
-
-
no substrate: AMP
-
-
?
additional information
?
-
-
enzyme abrogates platelet aggregation and recruitment in intact vessels
-
-
?
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
-
-
?
additional information
?
-
-
substrate specificity in myofibroblasts and quiescent-like hepatic stellate cells, overview
-
-
?
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EDTA
analyzed in presence and absence of, control reaction
ARL 67156
selective inhibitor
additional information
discrimination between total ATPase activity and ecto-ATPase activity by using vanadate, oligomycin and N-ethylmaleimide as inhibitors of ATPases of type P, F and V to focus on ecto-ATPase activity
-
additional information
-
discrimination between total ATPase activity and ecto-ATPase activity by using vanadate, oligomycin and N-ethylmaleimide as inhibitors of ATPases of type P, F and V to focus on ecto-ATPase activity
-
additional information
oligomycin (an inhibitor of mitochondrial ATPases), orthovanadate (an inhibitor of transport ATPases, acid phosphatases, and phosphotyrosine phosphatases), Ap5A (an inhibitor of adenylate kinase [AK]), ouabain (a classic inhibitor of Na+-ATPase and K+-ATPase), NEM (Ca2+-ATPases and Mg2+-ATPases, AK and sulfhydryl group modifier), levamisole (inhibitor of alkaline phosphatase), tetramisole (inhibitor of alkaline phosphatase), and sodium azide (inhibitor of mitochondrial ATPases) below 10 mM do not show an inhibitory effect on ATP and ADP hydrolysis by E-NTPDase
-
additional information
-
oligomycin (an inhibitor of mitochondrial ATPases), orthovanadate (an inhibitor of transport ATPases, acid phosphatases, and phosphotyrosine phosphatases), Ap5A (an inhibitor of adenylate kinase [AK]), ouabain (a classic inhibitor of Na+-ATPase and K+-ATPase), NEM (Ca2+-ATPases and Mg2+-ATPases, AK and sulfhydryl group modifier), levamisole (inhibitor of alkaline phosphatase), tetramisole (inhibitor of alkaline phosphatase), and sodium azide (inhibitor of mitochondrial ATPases) below 10 mM do not show an inhibitory effect on ATP and ADP hydrolysis by E-NTPDase
-
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Lavoie, E.G.; Kukulski, F.; Levesque, S.A.; Lecka, J.; Sevigny, J.
Cloning and characterization of mouse nucleoside triphosphate diphosphohydrolase-3
Biochem. Pharmacol.
67
1917-1926
2004
Mus musculus (Q8BFW6), Mus musculus
brenda
Bigonnesse, F.; Levesque, S.A.; Kukulski, F.; Lecka, J.; Robson, S.C.; Fernandes, M.J.G.; Sevigny, J.
Cloning and characterization of mouse nucleoside triphosphate diphosphohydrolase-8
Biochemistry
43
5511-5519
2004
Mus musculus (Q8K0L2), Mus musculus
brenda
Sevigny, J.; Sundberg, C.; Braun, N.; Guckelberger, O.; Csizmadia, E.; Qawi, I.; Imai, M.; Zimmermann, H.; Robson, S.C.
Differential catalytic properties and vascular topography of murine nucleoside triphosphate diphosphohydrolase 1 (NTPDase1) and NTPDase2 have implications for thromboregulation
Blood
99
2801-2809
2002
Mus musculus
brenda
Shi, J.D.; Kukar, T.; Wang, C.Y.; Li, Q.Z.; Cruz, P.E.; Davoodi-Semiromi, A.; Yang, P.; Gu, Y.; Lian, W.; Wu, D.H.; She, J.X.
Molecular cloning and characterization of a novel mammalian endo-apyrase (LALP1)
J. Biol. Chem.
276
17474-17478
2001
Mus musculus (Q3TCT4), Mus musculus, Homo sapiens (Q9NQZ7), Homo sapiens
brenda
Hyman, M.C.; Petrovic-Djergovic, D.; Visovatti, S.H.; Liao, H.; Yanamadala, S.; Bouis, D.; Su, E.J.; Lawrence, D.A.; Broekman, M.J.; Marcus, A.J.; Pinsky, D.J.
Self-regulation of inflammatory cell trafficking in mice by the leukocyte surface apyrase CD39
J. Clin. Invest.
119
1136-1149
2009
Mus musculus
brenda
Ricatti, M.J.; Alfie, L.D.; Lavoie, E.G.; Sevigny, J.; Schwarzbaum, P.J.; Faillace, M.P.
Immunocytochemical localization of NTPDases1 and 2 in the neural retina of mouse and zebrafish
Synapse
63
291-307
2009
Danio rerio, Mus musculus (P55772), Mus musculus
brenda
Andrade, C.; Wink, M.; Margis, R.; Borojevic, R.; Battastini, A.; Guma, F.
Changes in E-NTPDase 3 expression and extracellular nucleotide hydrolysis during the myofibroblast/lipocyte differentiation
Mol. Cell. Biochem.
339
79-87
2010
Mus musculus
brenda
Syed, S.K.; Kauffman, A.L.; Beavers, L.S.; Alston, J.T.; Farb, T.B.; Ficorilli, J.; Marcelo, M.C.; Brenner, M.B.; Bokvist, K.; Barrett, D.G.; Efanov, A.M.
Ectonucleotidase NTPDase3 is abundant in pancreatic beta-cells and regulates glucose-induced insulin secretion
Am. J. Physiol. Endocrinol. Metab.
305
E1319-E1326
2013
Homo sapiens (O75355), Homo sapiens, Mus musculus (Q8BFW6), Mus musculus
brenda
Vandenbeuch, A.; Anderson, C.B.; Parnes, J.; Enjyoji, K.; Robson, S.C.; Finger, T.E.; Kinnamon, S.C.
Role of the ectonucleotidase NTPDase2 in taste bud function
Proc. Natl. Acad. Sci. USA
110
14789-14794
2013
Mus musculus (O55026)
brenda
Pelletier, J.; Salem, M.; Lecka, J.; Fausther, M.; Bigonnesse, F.; Sevigny, J.
Generation and characterization of specific antibodies to the murine and human ectonucleotidase NTPDase8
Front. Pharmacol.
8
115
2017
Homo sapiens (Q5MY95), Homo sapiens, Mus musculus (Q8K0L2), Mus musculus
brenda
Dias, D.A.; de Barros Penteado, B.; Dos Santos, L.D.; Dos Santos, P.M.; Arruda, C.C.P.; Schetinger, M.R.C.; Leal, D.B.R.; Dos Santos Jaques, J.A.
Characterization of ectonucleoside triphosphate diphosphohydrolase (E-NTPDase; EC 3.6.1.5) activity in mouse peritoneal cavity cells
Cell Biochem. Funct.
35
358-363
2017
Mus musculus (P55772), Mus musculus, Mus musculus BALB/c (P55772)
brenda