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Information on EC 3.6.1.5 - apyrase and Organism(s) Mus musculus and UniProt Accession P55772
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3.6.1.5 apyraseIUBMB Comments
Apyrases are active against both di- and triphosphate nucleotides (NDPs and NTPs) and hydrolyse NTPs to nucleotide monophosphates (NMPs) in two distinct successive phosphate-releasing steps, with NDPs as intermediates. They differ from ATPases, which specifically hydrolyse ATP, by hydrolysing both ATP and ADP. The eukaryotic enzymes requires Ca2+, but Mg2+ can substitute. Most of the ecto-ATPases that occur on the cell surface and hydrolyse extracellular nucleotides belong to this enzyme family.
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Word Map
- 3.6.1.5
- platelet
-
purinergic
- agonist
- endothelial
- suramin
- ntpdases
- 5'-nucleotidase
- thrombin
- utp
- fibrinogen
-
thromboxane
-
salivary
-
blocker
- ecto-nucleotidases
-
ecto-5\'-nucleotidase
-
purinoceptors
-
platelet-rich
- aspirin
- 5'-triphosphate
-
ecto-enzymes
- ouabain
-
ppads
- oligomycin
-
adp-induced
-
synaptosomes
- serca2
- hirudin
-
blood-feeding
-
atp-mediated
- carbenoxolone
-
tyrode
-
hemichannels
-
alpha,beta-methylene
- arl
-
pannexins
-
atp-hydrolyzing
- luciferin-luciferase
-
adenosinergic
- agriculture
-
e-type
- phlebotomus
- analysis
- pharmacology
-
hematophagous
-
adp-dependent
- medicine
-
preretinal
-
gel-filtered
- ap5a
-
aggregometry
-
bzatp
- drug development
-
ectonucleotide
-
3.1.3.5
- atpgammas
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
hide(Overall reactions are displayed. Show all >>)
Synonyms
apyrase, ecto-atpase, adpase, ntpdase3, atp diphosphohydrolase, entpd1, atpase 2, ecto-apyrase, ectonucleoside triphosphate diphosphohydrolase, atpdase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
adenosine diphosphatase
-
-
-
-
ADPase
-
-
-
-
ATP-diphosphatase
-
-
-
-
ATP-diphosphohydrolase
-
-
-
-
ATPDase
-
-
-
-
CD39 antigen
-
-
-
-
Golgi nucleoside diphosphatase
-
-
-
-
HB6
-
-
-
-
Lymphoid cell activation antigen
-
-
-
-
NTPDase1
-
-
-
-
NTPDase3
NTPDase3
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphorous acid anhydride hydrolysis
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
nucleoside triphosphate phosphohydrolase (nucleoside monophosphoate-forming)
Apyrases are active against both di- and triphosphate nucleotides (NDPs and NTPs) and hydrolyse NTPs to nucleotide monophosphates (NMPs) in two distinct successive phosphate-releasing steps, with NDPs as intermediates. They differ from ATPases, which specifically hydrolyse ATP, by hydrolysing both ATP and ADP. The eukaryotic enzymes requires Ca2+, but Mg2+ can substitute. Most of the ecto-ATPases that occur on the cell surface and hydrolyse extracellular nucleotides belong to this enzyme family.
CAS REGISTRY NUMBER
COMMENTARY
9000-95-7
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
a ribonucleoside 5'-triphosphate + H2O
a ribonucleoside 5'-phosphate + 2 phosphate + 2 H+
-
-
-
?
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
-
-
?
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
?
-
-
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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
a ribonucleoside 5'-triphosphate + H2O
a ribonucleoside 5'-phosphate + 2 phosphate + 2 H+
-
-
-
?
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
-
-
?
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
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Mg2+
additional information
Ca2+
absolute requirement for divalent cation, Ca2+ fulfilling requirement best
Mg2+
absolute requirement for divalent cation, Ca2+ fulfilling requirement best
additional information
Ca2+-ATP and Ca2+-ADP hydrolysis are superior to hydrolysis with Mg2+-ATP and Mg2+-ADP as substrates
additional information
-
Ca2+-ATP and Ca2+-ADP hydrolysis are superior to hydrolysis with Mg2+-ATP and Mg2+-ADP as substrates
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
immunocytochemical localization in retinal layers, compartmentalized regulation of extracellular nucleotide/nucleoside concentration in the retinal layers, potential role for extracellular nucleotide mediated-signaling in the retina of vertebrates
additional information
-
immunocytochemical localization in retinal layers, compartmentalized regulation of extracellular nucleotide/nucleoside concentration in the retinal layers, potential role for extracellular nucleotide mediated-signaling in the retina of vertebrates
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
sharp thin band in, mainly restricted to horizontal cell processes in
expression in, also in intraretinal blood vessels of, no expression in Müller glia, highly in optic fiber bundles
-
hepatic stellate cell line. Both phenotypes of GRX cell line express NTPDase 3 and 5, but only activated cells express NTPDase 6, quantitative real-time PCR expression analysis of Entpd genes, overview
-
cardiac vasulature, endothelium, endocardium and to a lesser extent in vascular smooth muscle
additional information
-
NTPs may be hydrolyzed mainly by NTPDase 3 in GRX cells and the increase in the NTPs hydrolysis observed in lipocytes is probably related to the up-regulation of Entpd3 mRNA expression
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
downregulation of NTPDase3 expression in MIN-6 cells inhibits extracellular ATP hydrolysis and insulin secretion
malfunction
the excessive levels of extracellular ATP in the enzyme knockout animals desensitize the P2X receptors associated with nerve fibers, thereby depressing taste responses
physiological function
-
ecto-nucleoside triphosphate diphosphohydrolases, E-NTPDases, regulate the concentration of extracellular nucleotides, signaling molecules that play a role in the pathogenesis of hepatic fibrosis. Up-regulation of Entpd3 mRNA expression modulates the extracellular concentration of nucleotides/nucleosides and affect P2-receptor signaling differently in quiescent-like cells and may play a role in the regulation of hepatic stellate cell functions
physiological function
the enzyme modulates insulin secretion by controlling activation of purinergic receptors
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). ENTP1_MOUSE
510
2
57205
Swiss-Prot
Secretory Pathway (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
amino acid sequence shows eight putative N-glycosilation sites
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
Cd39-/- mice phenotype with increased levels of macrophages and neutrophils, cerebral ischemia effects, overview. 50% increase in the number of alphaMbeta2-integrin high-expressing monocytes in Cd39-/- mice compared with wild-type controls. Although an acute rescue from CD39 deficiency can be obtained through administration of an apyrase or solCD39 analog, a permanent rescue can be obtained via bone marrow reconstitution with CD39-bearing cells
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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
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
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
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
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
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
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
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)
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
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)
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